Journal articles: 'Decarboxylases'

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Raasakka, Arne, Elaheh Mahootchi, Ingeborg Winge, Weisha Luan, Petri Kursula, and Jan Haavik. "Structure of the mouse acidic amino acid decarboxylase GADL1." Acta Crystallographica Section F Structural Biology Communications 74, no. 1 (January 1, 2018): 65–73. http://dx.doi.org/10.1107/s2053230x17017848.

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Pyridoxal 5′-phosphate (PLP) is a ubiquitous cofactor in various enzyme classes, including PLP-dependent decarboxylases. A recently discovered member of this class is glutamic acid decarboxylase-like protein 1 (GADL1), which lacks the activity to decarboxylate glutamate to γ-aminobutyrate, despite its homology to glutamic acid decarboxylase. Among the acidic amino acid decarboxylases, GADL1 is most similar to cysteine sulfinic acid decarboxylase (CSAD), but the physiological function of GADL1 is unclear, although its expression pattern and activity suggest a role in neurotransmitter and neuroprotectant metabolism. The crystal structure of mouse GADL1 is described, together with a solution model based on small-angle X-ray scattering data. While the overall fold and the conformation of the bound PLP are similar to those in other PLP-dependent decarboxylases, GADL1 adopts a more loose conformation in solution, which might have functional relevance in ligand binding and catalysis. The structural data raise new questions about the compactness, flexibility and conformational dynamics of PLP-dependent decarboxylases, including GADL1.

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Aono, Riku, Tomoya Yoshihara, Hotaka Nishida, and Kuniki Kino. "Screening and characterization of a novel reversible 4-hydroxyisophthalic acid decarboxylase from Cystobasidium slooffiae HTK3." Bioscience, Biotechnology, and Biochemistry 85, no. 7 (May 4, 2021): 1658–64. http://dx.doi.org/10.1093/bbb/zbab082.

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ABSTRACT Owing to carboxylation activity, reversible decarboxylases can use CO2 as a C1-building block to produce useful carboxylic acids. Although many reversible decarboxylases can synthesize aromatic monocarboxylic acids, only a few reversible decarboxylases have been reported to date that catalyze the synthesis of aromatic dicarboxylic acids. In the present study, a reversible 4-hydroxyisophthalic acid decarboxylase was identified in Cystobasidium slooffiae HTK3. Furthermore, recombinant 4-hydroxyisophthalic acid decarboxylase was prepared, characterized, and used for 4-hydroxyisophthalic acid production from 4-hydroxybenzoic acid.

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Fang, Mingyu, Xing Wang, Zhikun Jia, Qiongju Qiu, Peng Li, Li Chen, and Hui Yang. "A Simple and Efficient Method for the Substrate Identification of Amino Acid Decarboxylases." International Journal of Molecular Sciences 23, no. 23 (November 22, 2022): 14551. http://dx.doi.org/10.3390/ijms232314551.

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Amino acid decarboxylases convert amino acids into different biogenic amines which regulate diverse biological processes. Therefore, identifying the substrates of amino acid decarboxylases is critical for investigating the function of the decarboxylases, especially for the new genes predicted to be amino acid decarboxylases. In the present work, we have established a simple and efficient method to identify the substrates and enzymatic activity of amino acid decarboxylases based on LC-MS methods. We chose GAD65 and AADC as models to validate our method. GAD65 and AADC were expressed in HEK 293T cells and purified through immunoprecipitation. The purified amino acid decarboxylases were subjected to enzymatic reaction with different substrate mixtures in vitro. LC-MS analysis of the reaction mixture identified depleted or accumulated metabolites, which corresponded to candidate enzyme substrates and products, respectively. Our method successfully identified the substrates and products of known amino acid decarboxylases. In summary, our method can efficiently identify the substrates and products of amino acid decarboxylases, which will facilitate future amino acid decarboxylase studies.

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de las RIVAS, BLANCA, ÁNGELA MARCOBAL, ALFONSO V. CARRASCOSA, and ROSARIO MUÑOZ. "PCR Detection of Foodborne Bacteria Producing the Biogenic Amines Histamine, Tyramine, Putrescine, and Cadaverine." Journal of Food Protection 69, no. 10 (October 1, 2006): 2509–14. http://dx.doi.org/10.4315/0362-028x-69.10.2509.

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This study describes an easy PCR method for the detection of foodborne bacteria that potentially produce histamine, tyramine, putrescine, and cadaverine. Synthetic oligonucleotide pairs for the specific detection of the gene coding for each group of bacterial histidine, tyrosine, ornithine, or lysine decarboxylases were designed. Under the conditions used in this study, the assay yielded fragments of 372 and 531 bp from histidine decarboxylase–encoding genes, a 825-bp fragment from tyrosine decarboxylases, fragments of 624 and 1,440 bp from ornithine decarboxylases, and 1,098- and 1,185-bp fragments from lysine decarboxylases. This is the first PCR method for detection of cadaverine-producing bacteria. The method was successfully applied to several biogenic amine–producing bacterial strains.

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Sköldberg, Filip, Fredrik Rorsman, Jaakko Perheentupa, Mona Landin-Olsson, Eystein S. Husebye, Jan Gustafsson, and Olle Kämpe. "Analysis of Antibody Reactivity against Cysteine Sulfinic Acid Decarboxylase, A Pyridoxal Phosphate-Dependent Enzyme, in Endocrine Autoimmune Disease." Journal of Clinical Endocrinology & Metabolism 89, no. 4 (April 1, 2004): 1636–40. http://dx.doi.org/10.1210/jc.2003-031161.

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Abstract The structurally related group II pyridoxal phosphate (PLP)-dependent amino acid decarboxylases glutamic acid decarboxylase (GAD), aromatic l-amino acid decarboxylase (AADC), and histidine decarboxylase (HDC) are known autoantigens in endocrine disorders. We report, for the first time, the prevalence of serum autoantibody reactivity against cysteine sulfinic acid decarboxylase (CSAD), an enzyme that shares 50% amino acid identity with the 65- and 67-kDa isoforms of GAD (GAD-65 and GAD-67), in endocrine autoimmune disease. Three of 83 patients (3.6%) with autoimmune polyendocrine syndrome type 1 (APS1) were anti-CSAD positive in a radioimmunoprecipitation assay. Anti-CSAD antibodies cross-reacted with GAD-65, and the anti-CSAD-positive sera were also reactive with AADC and HDC. The low frequency of anti-CSAD reactivity is in striking contrast to the prevalence of antibodies against GAD-65, AADC, and HDC in APS1 patients, suggesting that different mechanisms control the immunological tolerance toward CSAD and the other group II decarboxylases. Moreover, CSAD may be a useful mold for the construction of recombinant chimerical antigens in attempts to map conformational epitopes on other group II PLP-dependent amino acid decarboxylases.

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WENDAKOON, CHITRA N., and MORIHIKO SAKAGUCHI. "Inhibition of Amino Acid Decarboxylase Activity of Enterobacter aerogenes by Active Components in Spices." Journal of Food Protection 58, no. 3 (March 1, 1995): 280–83. http://dx.doi.org/10.4315/0362-028x-58.3.280.

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The water and ethanol extracts of several commercially available spices were examined for their inhibitory action on the decarboxylase activity of a crude extract of Enterobacter aerogenes. The water extracts had a negligible effect on histidine decarboxylase activity, except for water extract of cloves which reduced the activity by about 40%. However, the ethanol extracts had a rather higher inhibitory action upon histidine, lysine, and ornithine decarboxylases. Of the spices used, cloves, cinnamon, sage, nutmeg, and allspice were very effective in inhibiting the decarboxylases. Among the components of those spices, cinnamaldehyde and eugenol were found to be effective inhibitors.

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Pegg, Anthony E. "S-Adenosylmethionine decarboxylase." Essays in Biochemistry 46 (October 30, 2009): 25–46. http://dx.doi.org/10.1042/bse0460003.

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S-Adenosylmethionine decarboxylase is a key enzyme for the synthesis of polyamines in mammals, plants and many other species that use aminopropyltransferases for this pathway. It catalyses the formation of S-adenosyl-1-(methylthio)-3-propylamine (decarboxylated S-adenosylmethionine), which is used as the aminopropyl donor. This is the sole function of decarboxylated S-adenosylmethionine. Its content is therefore kept very low and is regulated by variation in the activity of S-adenosylmethionine decarboxylase according to the need for polyamine synthesis. All S-adenosylmethionine decarboxylases have a covalently bound pyruvate prosthetic group, which is essential for the decarboxylation reaction, and have similar structures, although they differ with respect to activation by cations, primary sequence and subunit composition. The present chapter describes these features, the mechanisms for autocatalytic generation of the pyruvate from a proenzyme precursor and for the decarboxylation reaction, and the available inhibitors of this enzyme, which have uses as anticancer and anti-trypanosomal agents. The intricate mechanisms for regulation of mammalian S-adenosylmethionine decarboxylase activity and content are also described.

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Henning, Helge, Christian Leggewie, Martina Pohl, Michael Müller, Thorsten Eggert, and Karl-Erich Jaeger. "Identification of Novel Benzoylformate Decarboxylases by Growth Selection." Applied and Environmental Microbiology 72, no. 12 (September 29, 2006): 7510–17. http://dx.doi.org/10.1128/aem.01541-06.

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ABSTRACT A growth selection system was established using Pseudomonas putida, which can grow on benzaldehyde as the sole carbon source. These bacteria presumably metabolize benzaldehyde via the β-ketoadipate pathway and were unable to grow in benzoylformate-containing selective medium, but the growth deficiency could be restored by expression in trans of genes encoding benzoylformate decarboxylases. The selection system was used to identify three novel benzoylformate decarboxylases, two of them originating from a chromosomal library of P. putida ATCC 12633 and the third from an environmental-DNA library. The novel P. putida enzymes BfdB and BfdC exhibited 83% homology to the benzoylformate decarboxylase from P. aeruginosa and 63% to the enzyme MdlC from P. putida ATCC 12633, whereas the metagenomic BfdM exhibited 72% homology to a putative benzoylformate decarboxylase from Polaromonas naphthalenivorans. BfdC was overexpressed in Escherichia coli, and the enzymatic activity was determined to be 22 U/ml using benzoylformate as the substrate. Our results clearly demonstrate that P. putida KT2440 is an appropriate selection host strain suitable to identify novel benzoylformate decarboxylase-encoding genes. In principle, this system is also applicable to identify a broad range of different industrially important enzymes, such as benzaldehyde lyases, benzoylformate decarboxylases, and hydroxynitrile lyases, which all catalyze the formation of benzaldehyde.

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Kim, Alexander D., David E. Graham, Steven H. Seeholzer, and George D. Markham. "S-Adenosylmethionine Decarboxylase from the Archaeon Methanococcus jannaschii: Identification of a Novel Family of Pyruvoyl Enzymes." Journal of Bacteriology 182, no. 23 (December 1, 2000): 6667–72. http://dx.doi.org/10.1128/jb.182.23.6667-6672.2000.

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ABSTRACT Polyamines are present in high concentrations in archaea, yet little is known about their synthesis, except by extrapolation from bacterial and eucaryal systems. S-Adenosylmethionine (AdoMet) decarboxylase, a pyruvoyl group-containing enzyme that is required for spermidine biosynthesis, has been previously identified in eucarya and Escherichia coli. Despite spermidine concentrations in the Methanococcales that are several times higher than in E. coli, no AdoMet decarboxylase gene was recognized in the complete genome sequence ofMethanococcus jannaschii. The gene encoding AdoMet decarboxylase in this archaeon is identified herein as a highly diverged homolog of the E. coli speD gene (less than 11% identity). The M. jannaschii enzyme has been expressed inE. coli and purified to homogeneity. Mass spectrometry showed that the enzyme is composed of two subunits of 61 and 63 residues that are derived from a common proenzyme; these proteins associate in an (αβ)2 complex. The pyruvoyl-containing subunit is less than one-half the size of that in previously reported AdoMet decarboxylases, but the holoenzyme has enzymatic activity comparable to that of other AdoMet decarboxylases. The sequence of theM. jannaschii enzyme is a prototype of a class of AdoMet decarboxylases that includes homologs in other archaea and diverse bacteria. The broad phylogenetic distribution of this group suggests that the canonical SpeD-type decarboxylase was derived from an archaeal enzyme within the gamma proteobacterial lineage. Both SpeD-type and archaeal-type enzymes have diverged widely in sequence and size from analogous eucaryal enzymes.

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MORII, HIDEAKI, and KENTARO KASAMA. "Activity of Two Histidine Decarboxylases from Photobacterium phosphoreum at Different Temperatures, pHs, and NaCl Concentrations." Journal of Food Protection 67, no. 8 (August 1, 2004): 1736–42. http://dx.doi.org/10.4315/0362-028x-67.8.1736.

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The major causative agent of scombroid poisoning is histamine formed by bacterial decarboxylation of histidine. The authors reported previously that histamine was exclusively formed by the psychrotrophic halophilic bacteria Photobacterium phosphoreum in scombroid fish during storage at or below 10°C. Moreover, histamine-forming ability was affected by two histidine decarboxylases: constitutive and inducible enzymes. This article reports the effect of various growth and reaction conditions, such as temperature, pH, and NaCl concentration, on the activity of two histidine decarboxylases that were isolated and separated by gel chromatography from cell-free extracts of P. phosphoreum. The histidine decarboxylase activity of the cell-free extracts was highest in 7°C culture; in 5% NaCl, culture growth was inhibited, and growth was best in the culture grown at pH 6.0. Moreover, percent activity of the constitutive and inducible enzymes was highest for the inducible enzyme in cultures grown at 7°C and pH 7.5 and in 5% NaCl. The temperature and pH dependences of histidine decarboxylase differed between the constitutive and inducible enzymes; that is, the activity of histidine decarboxylases was optimum at 30°C and pH6.5 for the inducible enzyme and 40°C and pH 6.0 for the constitutive enzyme. The differences in the temperature and pH dependences between the two enzymes extended the activity range of histidine decarboxylase under reaction conditions. On the other hand, histidine decarboxylase activity was optimum in 0% NaCl for the two enzymes. Additionally, the effects of reaction temperature, pH, and NaCl concentration on the constitutive enzyme activity of the cell-free extracts were almost the same as those on the whole histidine decarboxylase activity of the cell-free extracts, suggesting that the constitutive enzyme activity reflected the whole histidine decarboxylase activity.

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Connil, Nathalie, Yoann Le Breton, Xavier Dousset, Yanick Auffray, Alain Rincé, and Hervé Prévost. "Identification of the Enterococcus faecalis Tyrosine Decarboxylase Operon Involved in Tyramine Production." Applied and Environmental Microbiology 68, no. 7 (July 2002): 3537–44. http://dx.doi.org/10.1128/aem.68.7.3537-3544.2002.

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ABSTRACT Screening of a library of Enterococcus faecalis insertional mutants allowed isolation of a mutant affected in tyramine production. The growth of this mutant was similar to that of the wild-type E. faecalis JH2-2 strain in Maijala broth, whereas high-performance liquid chromatography analyses showed that tyramine production, which reached 1,000 μg ml−1 for the wild-type strain, was completely abolished. Genetic analysis of the insertion locus revealed a gene encoding a decarboxylase with similarity to eukaryotic tyrosine decarboxylases. Sequence analysis revealed a pyridoxal phosphate binding site, indicating that this enzyme belongs to the family of amino acid decarboxylases using this cofactor. Reverse transcription-PCR analyses demonstrated that the gene (tdc) encoding the putative tyrosine decarboxylase of E. faecalis JH2-2 is cotranscribed with the downstream gene encoding a putative tyrosine-tyramine antiporter and with the upstream tyrosyl-tRNA synthetase gene. This study is the first description of a tyrosine decarboxylase gene in prokaryotes.

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Canellakis, E. S., D. A. Kyriakidis, C. A. Rinehart, S. C. Huang, C. Panagiotidis, and W. F. Fong. "Regulation of polyamine biosynthesis by antizyme and some recent developments relating the induction of polyamine biosynthesis to cell growth." Bioscience Reports 5, no. 3 (March 1, 1985): 189–204. http://dx.doi.org/10.1007/bf01119588.

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This review considers the role of antizyme, of amino acids and of protein synthesis in the regulation of polyamine biosynthesis.The ornithine decarboxylase of eukaryotic ceils and of Escherichia coli coli can be non-competitively inhibited by proteins, termed antizymes, which are induced by di-and poly- amines. Some antizymes have been purified to homogeneity and have been shown to be structurally unique to the cell of origin. Yet, the E. coli antizyme and the rat liver antizyme cross react and inhibit each other's biosynthetic decarboxylases. These results indicate that aspects of the control of polyamine biosynthesis have been highly conserved throughout evolution.Evidence for the physiological role of the antizyme in mammalian cells rests upon its identification in normal uninduced cells, upon the inverse relationship that exists between antizyme and ornithine decarboxylase as well as upon the existence of the complex of ornithine decarboxylase and antizyme in vivo. Furthermore, the antizyme has been shown to be highly specific; its Keq for ornithine decarboxylase is 1.4 × 1011 M-1. In addition, mammalian ceils contain an anti-antizyme, a protein that specifically binds to the antizyme of an ornithine decarboxylase-antizyme complex and liberates free ornithine decarboxylase from the complex. In B. coli, in which polyamine biosynthesis is mediated both by ornithine decarboxylase and by arginine decarboxylase, three proteins (one acidic and two basic) have been purified, each of which inhibits both these enzymes. They do not inhibit the biodegradative ornithine and arginine decarboxylases nor lysine decarboxylase. The two basic inhibitors have been shown to correspond to the ribosomal proteins S20/L26 and L34, respectively. The relationship of the acidic antizyme to other known B. coli proteins remains to be determined.

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Dodds, R. A., A. A. Pitsillides, and G. T. Frost. "A quantitative cytochemical method for ornithine decarboxylase activity." Journal of Histochemistry & Cytochemistry 38, no. 1 (January 1990): 123–27. http://dx.doi.org/10.1177/38.1.2104632.

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Although decarboxylases, particularly ornithine decarboxylase, are of considerable importance in cell metabolism, it has been impossible to demonstrate their activity histochemically, as this depends on trapping carbon dioxide at neutral pH values. A new reagent, lead hydroxyisobutyrate, has been shown capable of such trapping. It has been applied to the demonstration of ornithine decarboxylase activity in mouse kidney. Optimal concentrations of substrate, co-factor and trapping agent, as well as the pH optimum, have been determined for cryostat sections stabilized with a collagen polypeptide. The activity was inhibited by the specific ornithine decarboxylase inhibitor alpha-difluoromethyl ornithine.

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Komori, Hirofumi, Yoko Nitta, Hiroshi Ueno, and Yoshiki Higuchi. "Structural basis for the histamine synthesis by human histidine decarboxylase." Acta Crystallographica Section A Foundations and Advances 70, a1 (August 5, 2014): C458. http://dx.doi.org/10.1107/s2053273314095412.

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Histamine is a bioactive amine responsible for a variety of physiological reactions, including allergy, gastric acid secretion, and neurotransmission. In mammals, histamine production from histidine is catalyzed by histidine decarboxylase (HDC). Mammalian HDC is a pyridoxal 5'-phosphate (PLP)-dependent decarboxylase and belongs to the same family as mammalian glutamate decarboxylase (GAD) and mammalian aromatic L-amino acid decarboxylase (AroDC). The decarboxylases of this family function as homodimers and catalyze the formation of physiologically important amines like GABA and dopamine via decarboxylation of glutamate and DOPA, respectively. Despite high sequence homology, both AroDC and HDC react with different substrates. For example, AroDC catalyzes the decarboxylation of several aromatic L-amino acids, but has little activity on histidine. Although such differences are known, the substrate specificity of HDC has not been extensively studied because of the low levels of HDC in the body and the instability of recombinant HDC, even in a well-purified form. However, knowledge about the substrate specificity and decarboxylation mechanism of HDC is valuable from the viewpoint of drug development, as it could help lead to designing of novel drugs to prevent histamine biosynthesis. We have determined the crystal structure of human HDC in complex with inhibitors, histidine methyl ester (HME) and alpha-fluoromethyl histidine (FMH). These structures showed the detailed features of the PLP-inhibitor adduct (external aldimine) in the active site of HDC. These data provided insight into the molecular basis for substrate recognition among the PLP-dependent L-amino acid decarboxylases.

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Pal Chowdhury, Piyali, Soumik Basu, Arindam Dutta, and Tapan K. Dutta. "Functional Characterization of a Novel Member of the Amidohydrolase 2 Protein Family, 2-Hydroxy-1-Naphthoic Acid Nonoxidative Decarboxylase from Burkholderia sp. Strain BC1." Journal of Bacteriology 198, no. 12 (April 11, 2016): 1755–63. http://dx.doi.org/10.1128/jb.00250-16.

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ABSTRACTThe gene encoding a nonoxidative decarboxylase capable of catalyzing the transformation of 2-hydroxy-1-naphthoic acid (2H1NA) to 2-naphthol was identified, recombinantly expressed, and purified to homogeneity. The putative gene sequence of the decarboxylase (hndA) encodes a 316-amino-acid protein (HndA) with a predicted molecular mass of 34 kDa. HndA exhibited high identity with uncharacterized amidohydrolase 2 proteins of variousBurkholderiaspecies, whereas it showed a modest 27% identity with γ-resorcylate decarboxylase, a well-characterized nonoxidative decarboxylase belonging to the amidohydrolase superfamily. Biochemically characterized HndA demonstrated strict substrate specificity toward 2H1NA, whereas inhibition studies with HndA indicated the presence of zinc as the transition metal center, as confirmed by atomic absorption spectroscopy. A three-dimensional structural model of HndA, followed by docking analysis, identified the conserved metal-coordinating and substrate-binding residues, while their importance in catalysis was validated by site-directed mutagenesis.IMPORTANCEMicrobial nonoxidative decarboxylases play a crucial role in the metabolism of a large array of carboxy aromatic chemicals released into the environment from a variety of natural and anthropogenic sources. Among these, hydroxynaphthoic acids are usually encountered as pathway intermediates in the bacterial degradation of polycyclic aromatic hydrocarbons. The present study reveals biochemical and molecular characterization of a 2-hydroxy-1-naphthoic acid nonoxidative decarboxylase involved in an alternative metabolic pathway which can be classified as a member of the small repertoire of nonoxidative decarboxylases belonging to the amidohydrolase 2 family of proteins. The strict substrate specificity and sequence uniqueness make it a novel member of the metallo-dependent hydrolase superfamily.

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Vuralhan, Zeynep, Marijke A. H. Luttik, Siew Leng Tai, Viktor M. Boer, Marcos A. Morais, Dick Schipper, Marinka J. H. Almering, et al. "Physiological Characterization of the ARO10-Dependent, Broad-Substrate-Specificity 2-Oxo Acid Decarboxylase Activity of Saccharomyces cerevisiae." Applied and Environmental Microbiology 71, no. 6 (June 2005): 3276–84. http://dx.doi.org/10.1128/aem.71.6.3276-3284.2005.

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ABSTRACT Aerobic, glucose-limited chemostat cultures of Saccharomyces cerevisiae CEN.PK113-7D were grown with different nitrogen sources. Cultures grown with phenylalanine, leucine, or methionine as a nitrogen source contained high levels of the corresponding fusel alcohols and organic acids, indicating activity of the Ehrlich pathway. Also, fusel alcohols derived from the other two amino acids were detected in the supernatant, suggesting the involvement of a common enzyme activity. Transcript level analysis revealed that among the five thiamine-pyrophospate-dependent decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3), only ARO10 was transcriptionally up-regulated when phenylalanine, leucine, or methionine was used as a nitrogen source compared to growth on ammonia, proline, and asparagine. Moreover, 2-oxo acid decarboxylase activity measured in cell extract from CEN.PK113-7D grown with phenylalanine, methionine, or leucine displayed similar broad-substrate 2-oxo acid decarboxylase activity. Constitutive expression of ARO10 in ethanol-limited chemostat cultures in a strain lacking the five thiamine-pyrophosphate-dependent decarboxylases, grown with ammonia as a nitrogen source, led to a measurable decarboxylase activity with phenylalanine-, leucine-, and methionine-derived 2-oxo acids. Moreover, even with ammonia as the nitrogen source, these cultures produced significant amounts of the corresponding fusel alcohols. Nonetheless, the constitutive expression of ARO10 in an isogenic wild-type strain grown in a glucose-limited chemostat with ammonia did not lead to any 2-oxo acid decarboxylase activity. Furthermore, even when ARO10 was constitutively expressed, growth with phenylalanine as the nitrogen source led to increased decarboxylase activities in cell extracts. The results reported here indicate the involvement of posttranscriptional regulation and/or a second protein in the ARO10-dependent, broad-substrate-specificity decarboxylase activity.

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Li, Zhi-Min, Ziwei Hu, Xiaoqin Wang, Suhang Chen, Weiyan Yu, Jianping Liu, and Zhimin Li. "Biochemical and Structural Insights into a Thiamine Diphosphate-Dependent α-Ketoglutarate Decarboxylase from Cyanobacterium Microcystis aeruginosa NIES-843." International Journal of Molecular Sciences 24, no. 15 (July 30, 2023): 12198. http://dx.doi.org/10.3390/ijms241512198.

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α-Ketoglutarate decarboxylase is a crucial enzyme in the tricarboxylic acid cycle of cyanobacteria, catalyzing the non-oxidative decarboxylation of α-ketoglutarate to produce succinate semialdehyde and CO2. The decarboxylation process is reliant on the cofactor of thiamine diphosphate. However, this enzyme’s biochemical and structural properties have not been well characterized. In this work, two α-ketoglutarate decarboxylases encoded by MAE_06010 and MiAbw_01735 genes from Microcystis aeruginosa NIES-843 (MaKGD) and NIES-4325 (MiKGD), respectively, were overexpressed and purified by using an Escherichia coli expression system. It was found that MaKGD exhibited 9.2-fold higher catalytic efficiency than MiKGD, which may be attributed to the absence of glutamate decarboxylase in Microcystis aeruginosa NIES-843. Further biochemical investigation of MaKGD demonstrated that it displayed optimum activity at pH 6.5–7.0 and was most activated by Mg2+. Additionally, MaKGD showed substrate specificity towards α-ketoglutarate. Structural modeling and autodocking results revealed that the active site of MaKGD contained a distinct binding pocket where α-ketoglutarate and thiamine diphosphate interacted with specific amino acid residues via hydrophobic interactions, hydrogen bonds and salt bridges. Furthermore, the mutagenesis study provided strong evidence supporting the importance of certain residues in the catalysis of MaKGD. These findings provide new insights into the structure-function relationships of α-ketoglutarate decarboxylases from cyanobacteria.

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Schaeffer, J. M., and M. R. Donatelli. "Characterization of a high-affinity membrane-associated ornithine decarboxylase from the free-living nematode Caenorhabditis elegans." Biochemical Journal 270, no. 3 (September 15, 1990): 599–604. http://dx.doi.org/10.1042/bj2700599.

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Ornithine decarboxylase has been identified and characterized in the free-living nematode Caenorhabditis elegans. Unlike previously described ornithine decarboxylases, the enzyme activity is membrane-associated and remains in the membrane fraction after treatment with high salt, detergents or phosphatidylinositol-specific phospholipase C. Ornithine has an apparent Km value of 2.7 microM for ornithine decarboxylase. The enzyme is competitively inhibited by arginine and lysine with Ki values of 4.0 and 24.4 microM respectively. None of the other naturally occurring amino acids inhibited more than 10% of the enzyme activity at concentrations up to 1 mM. Agmatine, putrescine, spermidine and spermine inhibit ornithine decarboxylase in a non-competitive manner with Ki values of 10, 53.5, 59 and 855 microM respectively. A similar ornithine decarboxylase activity was also identified in membrane preparations from the parasitic nematode Haemonchus contortus.

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Christ, Marbeth, Hansruedi Felix, and Jost Harr. "Inhibitors Influencing Plant Enzymes of the Polyamine Biosynthetic Pathway." Zeitschrift für Naturforschung C 44, no. 1-2 (February 1, 1989): 49–54. http://dx.doi.org/10.1515/znc-1989-1-209.

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Absract Several enzymes involved in polyamine biosynthesis namely ornithine, arginine and S-adenosylmethionine decarboxylase as well as spermidine synthase, were analyzed in partially purified wheat extracts. For all enzymes effective inhibitors were found. Among them the most interesting was l-aminooxy-3-aminopropane, which inhibited all three decarboxylases. Classical polyamine biosynthesis inhibitors like difluoromethylornithine, difluoromethylarginine. methyl glyoxal bis- (guanylhydrazone) and cyclohexylamine were also inhibitory on plant enzymes. A remarkable difference in the amount of arginine and ornithine decarboxylase existed in wheat. Arginine decarboxylase seems to be more important at least during the early stage of development. Influence of polyamine synthesis inhibitors on polyamine levels is more likely to come from arginine decarboxylase inhibitors. As inhibitors of all essential enzymes involved in plant polyamine biosynthesis were found, the study of the importance of polyamines in plant physiology will be considerably facilitated.

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Romagnoli, Gabriele, Marijke A. H. Luttik, Peter Kötter, Jack T. Pronk, and Jean-Marc Daran. "Substrate Specificity of Thiamine Pyrophosphate-Dependent 2-Oxo-Acid Decarboxylases in Saccharomyces cerevisiae." Applied and Environmental Microbiology 78, no. 21 (August 17, 2012): 7538–48. http://dx.doi.org/10.1128/aem.01675-12.

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ABSTRACTFusel alcohols are precursors and contributors to flavor and aroma compounds in fermented beverages, and some are under investigation as biofuels. The decarboxylation of 2-oxo acids is a key step in the Ehrlich pathway for fusel alcohol production. InSaccharomyces cerevisiae, five genes share sequence similarity with genes encoding thiamine pyrophosphate-dependent 2-oxo-acid decarboxylases (2ODCs).PDC1,PDC5, andPDC6encode differentially regulated pyruvate decarboxylase isoenzymes;ARO10encodes a 2-oxo-acid decarboxylase with broad substrate specificity, andTHI3has not yet been shown to encode an active decarboxylase. Despite the importance of fusel alcohol production inS. cerevisiae, the substrate specificities of these five 2ODCs have not been systematically compared. When the five 2ODCs were individually overexpressed in apdc1Δpdc5Δpdc6Δaro10Δthi3Δ strain, only Pdc1, Pdc5, and Pdc6 catalyzed the decarboxylation of the linear-chain 2-oxo acids pyruvate, 2-oxo-butanoate, and 2-oxo-pentanoate in cell extracts. The presence of a Pdc isoenzyme was also required for the production ofn-propanol andn-butanol in cultures grown on threonine and norvaline, respectively, as nitrogen sources. These results demonstrate the importance of pyruvate decarboxylases in the natural production ofn-propanol andn-butanol byS. cerevisiae. No decarboxylation activity was found for Thi3 with any of the substrates tested. Only Aro10 and Pdc5 catalyzed the decarboxylation of the aromatic substrate phenylpyruvate, with Aro10 showing superior kinetic properties. Aro10, Pdc1, Pdc5, and Pdc6 exhibited activity with all branched-chain and sulfur-containing 2-oxo acids tested but with markedly different decarboxylation kinetics. The high affinity of Aro10 identified it as a key contributor to the production of branched-chain and sulfur-containing fusel alcohols.

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COSTANTINI, ANTONELLA, MANUELA CERSOSIMO, VINCENZO DEL PRETE, and EMILIA GARCIA-MORUNO. "Production of Biogenic Amines by Lactic Acid Bacteria: Screening by PCR, Thin-Layer Chromatography, and High-Performance Liquid Chromatography of Strains Isolated from Wine and Must." Journal of Food Protection 69, no. 2 (February 1, 2006): 391–96. http://dx.doi.org/10.4315/0362-028x-69.2.391.

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Biogenic amines are frequently found in wine and other fermented food. We investigated the ability of 133 strains of lactic acid bacteria isolated from musts and wines of different origins to produce histamine, tyramine, and putrescine. We detected the genes responsible for encoding the corresponding amino acid decarboxylases through PCR assays using two primer sets for every gene: histidine decarboxylase (hdc), tyrosine decarboxylase (tdc), and ornithine decarboxylase (odc); these primers were taken from the literature or designed by us. Only one strain of Lactobacillus hilgardii was shown to possess the hdc gene, whereas four strains of Lactobacillus brevis had the tdc gene. None of the Oenococcus oeni strains, the main agents of malolactic fermentation, was a biogenic amine producer. All PCR amplicon band–positive results were confirmed by thin-layer chromatography and high-performance liquid chromatography analyses.

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Zeida, Mitsuhiro, Marco Wieser, Toyokazu Yoshida, Tsuyoshi Sugio, and Toru Nagasawa. "Purification and Characterization of Gallic Acid Decarboxylase from Pantoea agglomerans T71." Applied and Environmental Microbiology 64, no. 12 (December 1, 1998): 4743–47. http://dx.doi.org/10.1128/aem.64.12.4743-4747.1998.

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ABSTRACT Oxygen-sensitive gallic acid decarboxylase from Pantoea(formerly Enterobacter) agglomerans T71 was purified from a cell extract after stabilization by reducing agents. This enzyme has a molecular mass of approximately 320 kDa and consists of six identical subunits. It is highly specific for gallic acid. Gallic acid decarboxylase is unique among similar decarboxylases in that it requires iron as a cofactor, as shown by plasma emission spectroscopy (which revealed an iron content of 0.8 mol per mol of enzyme subunit), spectrophotometric analysis (absorption shoulders at 398 and 472 nm), and inhibition of the enzyme activity by 2,2′-bipyridyl, o-phenanthroline, and EDTA. Another interesting feature of this strain is the fact that it contains a tannase, which is used together with the gallic acid decarboxylase in a two-enzyme resting cell bioconversion to synthesize valuable pyrogallol from readily available tannic acid.

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23

MICHAEL, Anthony J., Judith M. FURZE, Michael J. C. RHODES, and Daniel BURTIN. "Molecular cloning and functional identification of a plant ornithine decarboxylase cDNA." Biochemical Journal 314, no. 1 (February 15, 1996): 241–48. http://dx.doi.org/10.1042/bj3140241.

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A cDNA for a plant ornithine decarboxylase (ODC), a key enzyme in putrescine and polyamine biosynthesis, has been isolated from root cultures of the solanaceous plant Datura stramonium. Reverse transcription–PCR employing degenerate oligonucleotide primers representing conserved motifs from other eukaryotic ODCs was used to isolate the cDNA. The longest open reading frame potentially encodes a peptide of 431 amino acids and exhibits similarity to other eukaryotic ODCs, prokaryotic and eukaryotic arginine decarboxylases (ADCs), prokaryotic meso-diaminopimelate decarboxylases and the product of the tabA gene of Pseudomonas syringae cv. tabaci. Residues involved at the active site of the mouse ODC are conserved in the plant enzyme. The plant ODC does not possess the C-terminal extension found in the mammalian enzyme, implicated in rapid turnover of the protein, suggesting that the plant ODC may have a longer half-life. Expression of the plant ODC in Escherichia coli and demonstration of ODC activity confirmed that the cDNA encodes an active ODC enzyme. This is the first description of the primary structure of a eukaryotic ODC isolated from an organism where the alternative ADC route to putrescine is present.

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Bitonti, A. J., J. A. Dumont, and P. P. McCann. "Characterization of Trypanosoma brucei bruceiS-adenosyl-l-methionine decarboxylase and its inhibition by Berenil, pentamidine and methylglyoxal bis(guanylhydrazone)." Biochemical Journal 237, no. 3 (August 1, 1986): 685–89. http://dx.doi.org/10.1042/bj2370685.

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Trypanosoma brucei brucei S-adenosyl-L-methionine (AdoMet) decarboxylase was found to be relatively insensitive to activation by putrescine as compared with the mammalian enzyme, being stimulated by only 50% over a 10,000-fold range of putrescine concentrations. The enzyme was not stimulated by up to 10 mM-Mg2+. The Km for AdoMet was 30 microM, similar to that of other eukaryotic AdoMet decarboxylases. T.b. brucei AdoMet decarboxylase activity was apparently irreversibly inhibited in vitro by Berenil and reversibly by pentamidine and methylglyoxal bis(guanylhydrazone). Berenil also inhibited trypanosomal AdoMet decarboxylase by 70% within 4 h after administration to infected rats and markedly increased the concentration of putrescine in trypanosomes that were exposed to the drug in vivo. Spermidine and spermine blocked the curative effect of Berenil on model mouse T.b. brucei infections. This effect of the polyamines was probably not due to reversal of Berenil's inhibitory effects on the AdoMet decarboxylase.

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25

Burdychová, Radka. "Identification and typization of bacteria of the genus Enterococcus supposed to be used for the production of functional foods." Acta Universitatis Agriculturae et Silviculturae Mendelianae Brunensis 55, no. 2 (2007): 9–14. http://dx.doi.org/10.11118/actaun200755020009.

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In this study, the species identification of 12 probiotic strains of the genusEnterococcusfrom Culture Collection of Dairy Microorganisms Lactoflora (CCDM, Milcom, Tábor, Czech Republic) were done using PCR described by DUTKA-MALEN et al. (1995). All strains were classified to be of the genusEnterococcusand speciesE. faecium.These strains are supposed to be used as probiotics for the production of functional foods. According to the fact thatE. faeciumwas described to have decarboxylase activity responsible for biogenic amine production in fermented products, the presence of genes coding for microbial tyrosine and histidine decarboxylase was screened in all strains using PCR described by COTON et al. (2004). Whereas the presence of DNA sequences for histidine decarboxylase was not detected in any strain, specific DNA sequences coding for tyrosine decarboxylases were detected in all tested strains. When applying as starter probiotic cultures to fermented milk products, the production of biogenic amine tyramine have to be observed during both fermentation and storage.

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Escutia, Marta R., Laura Bowater, Anne Edwards, Andrew R. Bottrill, Matthew R. Burrell, Rubén Polanco, Rafael Vicuña, and Stephen Bornemann. "Cloning and Sequencing of Two Ceriporiopsis subvermispora Bicupin Oxalate Oxidase Allelic Isoforms: Implications for the Reaction Specificity of Oxalate Oxidases and Decarboxylases." Applied and Environmental Microbiology 71, no. 7 (July 2005): 3608–16. http://dx.doi.org/10.1128/aem.71.7.3608-3616.2005.

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ABSTRACT Oxalate oxidase is thought to be involved in the production of hydrogen peroxide for lignin degradation by the dikaryotic white rot fungus Ceriporiopsis subvermispora. This enzyme was purified, and after digestion with trypsin, peptide fragments of the enzyme were sequenced using quadrupole time-of-flight mass spectrometry. Starting with degenerate primers based on the peptide sequences, two genes encoding isoforms of the enzyme were cloned, sequenced, and shown to be allelic. Both genes contained 14 introns. The sequences of the isoforms revealed that they were both bicupins that unexpectedly shared the greatest similarity to microbial bicupin oxalate decarboxylases rather than monocupin plant oxalate oxidases (also known as germins). We have shown that both fungal isoforms, one of which was heterologously expressed in Escherichia coli, are indeed oxalate oxidases that possess ≤0.2% oxalate decarboxylase activity and that the organism is capable of rapidly degrading exogenously supplied oxalate. They are therefore the first bicupin oxalate oxidases to have been described. Heterologous expression of active enzyme was dependent on the addition of manganese salts to the growth medium. Molecular modeling provides new and independent evidence for the identity of the catalytic site and the key amino acid involved in defining the reaction specificities of oxalate oxidases and oxalate decarboxylases.

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27

Stevenson, Lindsay G., and Philip N. Rather. "A Novel Gene Involved in Regulating the Flagellar Gene Cascade in Proteus mirabilis." Journal of Bacteriology 188, no. 22 (September 15, 2006): 7830–39. http://dx.doi.org/10.1128/jb.00979-06.

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ABSTRACT In this study, we identified a transposon insertion in a novel gene, designated disA, that restored swarming motility to a putrescine-deficient speA mutant of Proteus mirabilis. A null allele in disA also increased swarming in a wild-type background. The DisA gene product was homologous to amino acid decarboxylases, and its role in regulating swarming was investigated by examining the expression of genes in the flagellar cascade. In a disA mutant background, we observed a 1.4-fold increase in the expression of flhDC, which encodes FlhD2C2, the master regulator of the flagellar gene cascade. However, the expressions of class 2 (fliA, flgM) and class 3 (flaA) genes were at least 16-fold higher in the disA background during swarmer cell differentiation. Overexpression of DisA on a high-copy-number plasmid did not significantly decrease flhDC mRNA accumulation but resulted in a complete block in mRNA accumulation for both fliA and flaA. DisA overexpression also blocked swarmer cell differentiation. The disA gene was regulated during the swarming cycle, and a single-copy disA::lacZ fusion exhibited a threefold increase in expression in swarmer cells. Given that DisA was similar to amino acid decarboxylases, a panel of decarboxylated amino acids was tested for effects similar to DisA overexpression, and phenethylamine, the product of phenylalanine decarboxylation, was capable of inhibiting both swarming and the expression of class 2 and class 3 genes in the flagellar regulon. A DisA-dependent decarboxylated amino acid may inhibit the formation of active FlhD2C2 heterotetramers or inhibit FlhD2C2 binding to DNA.

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28

Buckel, Wolfgang. "Sodium ion-translocating decarboxylases." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1505, no. 1 (May 2001): 15–27. http://dx.doi.org/10.1016/s0005-2728(00)00273-5.

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29

MARCOBAL, ÁNGELA, BLANCA de las RIVAS, M. VICTORIA MORENO-ARRIBAS, and ROSARIO MUÑOZ. "Multiplex PCR Method for the Simultaneous Detection of Histamine-, Tyramine-, and Putrescine-Producing Lactic Acid Bacteria in Foods." Journal of Food Protection 68, no. 4 (April 1, 2005): 874–78. http://dx.doi.org/10.4315/0362-028x-68.4.874.

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In a screening of primers, we have selected three pairs of primers for a multiplex PCR assay for the simultaneous detection of lactic acid bacteria (LAB) strains, which potentially produce histamine, tyramine, and putrescine on fermented foods. These primers were based on sequences from histidine, tyrosine, and ornithine decarboxylases from LAB. Under the optimized conditions, the assay yielded a 367-bp DNA fragment from histidine decarboxylases, a 924-bp fragment from tyrosine decarboxylases, and a 1,446-bp fragment from ornithine decarboxylases. When the DNAs of several target organisms were included in the same reaction, two or three corresponding amplicons of different sizes were observed. This assay was useful for the detection of amine-producing bacteria in control collection strains and in a LAB collection. No amplification was observed with DNA from nonproducing LAB strains. This article is the first describing a multiplex PCR approach for the simultaneous detection of potentially amine-producing LAB in foods. It can be easily incorporated into the routine screening for the accurate selection of starter LAB and in food control laboratories.

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HELJASVAARA, Ritva, Ildiko VERESS, Maria HALMEKYTÖ, Leena ALHONEN, Juhani JÄNNE, Pasi LAAJALA, and Antti PAJUNEN. "Transgenic mice overexpressing ornithine and S-adenosylmethionine decarboxylases maintain a physiological polyamine homoeostasis in their tissues." Biochemical Journal 323, no. 2 (April 15, 1997): 457–62. http://dx.doi.org/10.1042/bj3230457.

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Recent work has shown that transgenic mice overexpressing human ornithine decarboxylase display no marked changes in the tissue concentrations of spermidine or spermine in spite of a dramatic increase in putrescine levels. In the tissues of transgenic mice carrying the human spermidine synthase gene and in those of hybrid mice overexpressing both ornithine decarboxylase and spermidine synthase, spermidine and spermine levels remain within normal limits. To test whether the amount of the propylamine group donor, decarboxylated S-adenosylmethionine, limits the conversion of putrescine into the higher polyamines, we have produced transgenic mouse lines harbouring the rat S-adenosylmethionine decarboxylase gene in their genome. However, neither these mice nor the hybrid mice overexpressing both ornithine decarboxylase and S-adenosylmethionine decarboxylase displayed significant changes in their spermidine and spermine tissue levels. To study the mechanism by which cells maintain the constancy of the polyamine concentrations, we have determined the metabolic flux of polyamines in transgenic primary fibroblasts using pulse labelling. The results indicate that the polyamine flow is faster in transgenic primary fibroblasts than in non-transgenic fibroblasts and that the intracellular homoeostasis of higher polyamines is maintained at least partly by the acetylation of spermidine and spermine and their secretion into the medium.

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31

Macrae, M., R. H. Plasterk, and P. Coffino. "The ornithine decarboxylase gene of Caenorhabditis elegans: cloning, mapping and mutagenesis." Genetics 140, no. 2 (June 1, 1995): 517–25. http://dx.doi.org/10.1093/genetics/140.2.517.

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Abstract The gene (odc-1) encoding ornithine decarboxylase, a key enzyme in polyamine biosynthesis, was cloned and characterized. Two introns interrupt the coding sequence of the gene. The deduced protein contains 422 amino acids and is homologous to ornithine decarboxylases of other eukaryotic species. In vitro translation of a transcript of the cDNA yielded an enzymatically active product. The mRNA is 1.5 kb in size and is formed by trans-splicing to SL1, a common 5' RNA segment. odc-1 maps to the middle of LG V, between dpy-11 and unc-42 and near a breakpoint of the nDf32 deficiency strain. Enzymatic activity is low in starved stage 1 (L1) larva and, after feeding, rises progressively as the worms develop. Targeted gene disruption was used to create a null allele. Homozygous mutants are normally viable and show no apparent defects, with the exception of a somewhat reduced brood size. In vitro assays for ornithine decarboxylase activity, however, show no detectable enzymatic activity, suggesting that ornithine decarboxylase is dispensible for nematode growth in the laboratory.

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32

Tcherkez, Guillaume. "Viewpoint: How large is the carbon isotope fractionation of the photorespiratory enzyme glycine decarboxylase?" Functional Plant Biology 33, no. 10 (2006): 911. http://dx.doi.org/10.1071/fp06098.

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Despite the intense effort developed over the past 10 years to determine the 12C / 13C isotope fractionation associated with photorespiration, much uncertainty remains about the amplitude, and even the sign, of the 12C / 13C isotope fractionation of glycine decarboxylase, the enzyme that produces CO2 during the photorespiratory cycle. In fact, leaf gas-exchange data have repeatedly indicated that CO2 evolved by photorespiration is depleted in 13C compared with the source material, while glycine decarboxylase has mostly favoured 13C in vitro. Here I give theoretical insights on the glycine decarboxylase reaction and show that (i), both photorespiration and glycine decarboxylation must favour the same carbon isotope — the in vitro measurements being probably adulterated by the high sensitivity of the enzyme to assay conditions and the possible reversibility of the reaction in these conditions, and (ii), simplified quantum chemistry considerations as well as comparisons with other pyridoxal 5′-phosphate-dependent decarboxylases indicate that the carbon isotope fractionation favour the 12C isotope by ~20‰, a value that is consistent with the value of the photorespiratory fractionation (f) obtained by gas-exchange experiments.

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33

Persson, L., A. Jeppsson, and S. Nasizadeh. "Turnover of trypanosomal ornithine decarboxylases." Biochemical Society Transactions 31, no. 2 (April 1, 2003): 411–14. http://dx.doi.org/10.1042/bst0310411.

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Interestingly, there is a major difference in turnover rate between ornithine decarboxylases (ODCs) from various trypanosomatids. ODCs from Trypanosoma brucei and Leishmania donovani are both stable proteins, whereas ODC from Crithidia fasciculata is a metabolically unstable protein in the parasite. C. fasciculata ODC is also rapidly degraded in mammalian systems, whereas the closely related L. donovani ODC is not. The degradation of C. fasciculata ODC in the mammalian systems is shown to be dependent on a functional 26 S proteasome. However, in contrast to the degradation of mammalian ODC, the degradation of C. fasciculata ODC does not involve antizyme. Instead, it appears the degradation of C. fasciculata ODC may be associated with poly-ubiquitination of the enzyme.

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34

Ward, Owen P., and Ajay Singh. "Enzymatic asymmetric synthesis by decarboxylases." Current Opinion in Biotechnology 11, no. 6 (December 2000): 520–26. http://dx.doi.org/10.1016/s0958-1669(00)00139-7.

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35

Jones, R. M., and P. M. Jordan. "Purification and properties of the uroporphyrinogen decarboxylase from Rhodobacter sphaeroides." Biochemical Journal 293, no. 3 (August 1, 1993): 703–12. http://dx.doi.org/10.1042/bj2930703.

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Uroporphyrinogen decarboxylase (EC 4.1.1.37) was purified 600-fold from Rhodobacter sphaeroides grown anaerobically in the light. The enzyme, under both denaturing and non-denaturing conditions, is a monomer of M(r) 41,000. The Km values are 1.8 microM and 6.0 microM for the conversion of uroporphyrinogen I and III to coproporphyrinogen I and III respectively. The enzyme is susceptible to inhibition by both uroporphyrinogen and uroporphyrin. The pH optimum is 6.8 and the isoelectric point is 4.4. The importance of cysteine and arginine residues is implicated from studies with inhibitors. The sequence of the first 29 amino acids of the N-terminus shows a high degree of similarity to the primary structures of other uroporphyrinogen decarboxylases. Studies on the order of decarboxylation of the four acetic acid side chains of uroporphyrinogen III suggest that at high substrate levels a random route is preferred.

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36

MARAS, Bruno, Paola DOMINICI, Donatella BARRA, Francesco BOSSA, and C. Borri VOLTATTORNI. "Pig kidney 3,4-dihydroxyphenylalanine (Dopa) decarboxylase. Primary structure and relationship to other amino acid decarboxylases." European Journal of Biochemistry 201, no. 2 (October 1991): 385–91. http://dx.doi.org/10.1111/j.1432-1033.1991.tb16295.x.

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37

Berthold, Catrine L., Cory G. Toyota, Patricia Moussatche, Martin D. Wood, Finian Leeper, Nigel G. J. Richards, and Ylva Lindqvist. "Crystallographic Snapshots of Oxalyl-CoA Decarboxylase Give Insights into Catalysis by Nonoxidative ThDP-Dependent Decarboxylases." Structure 15, no. 7 (July 2007): 853–61. http://dx.doi.org/10.1016/j.str.2007.06.001.

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38

Kang, Un Jung, and Tong H. Joh. "Deduced amino acid sequence of bovine aromatic l-amino acid decarboxylase: homology to other decarboxylases." Molecular Brain Research 8, no. 1 (June 1990): 83–87. http://dx.doi.org/10.1016/0169-328x(90)90013-4.

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39

Yamani, Mohammed I., and Friedrich Untermann. "Development of a histidine decarboxylase medium and its application to detect other amino acid decarboxylases." International Journal of Food Microbiology 2, no. 5 (September 1985): 273–78. http://dx.doi.org/10.1016/0168-1605(85)90040-6.

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40

Forouhar, Farhad, Scott Lew, Jayaraman Seetharaman, Rong Xiao, Thomas B. Acton, Gaetano T. Montelione, and Liang Tong. "Structures of bacterial biosynthetic arginine decarboxylases." Acta Crystallographica Section F Structural Biology and Crystallization Communications 66, no. 12 (November 16, 2010): 1562–66. http://dx.doi.org/10.1107/s1744309110040649.

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41

Erlander, Mark G., Niranjala J. K. Tillakaratne, Sophie Feldblum, Neela Patel, and Allan J. Tobin. "Two genes encode distinct glutamate decarboxylases." Neuron 7, no. 1 (July 1991): 91–100. http://dx.doi.org/10.1016/0896-6273(91)90077-d.

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42

Rosenberg, Robert M., Richard M. Herreid, George J. Piazza, and Marion H. O'Leary. "Indicator assay for amino acid decarboxylases." Analytical Biochemistry 181, no. 1 (August 1989): 59–65. http://dx.doi.org/10.1016/0003-2697(89)90393-x.

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43

Tabanelli, Giulia. "Biogenic Amines and Food Quality: Emerging Challenges and Public Health Concerns." Foods 9, no. 7 (July 1, 2020): 859. http://dx.doi.org/10.3390/foods9070859.

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In addition to pathogenic bacteria and viruses, some bioactive compounds and natural toxins such as biogenic amines (BAs) can be responsible for food poisoning. These compounds, produced mainly by bacteria through the action of decarboxylases, represent a risk for consumers’ health and are involved in several pathogenic syndromes, with histamine and tyramine being the most dangerous ones. Since the presence of dangerous amounts of BAs is associated with the relevant growth of spoiling decarboxylating microorganisms, BA content has been proposed as a food quality index in fresh products. Several factors, both intrinsic and technological, can regulate BA accumulation in foods influencing the decarboxylase-positive bacteria population and proteolysis phenomena, especially in fermented products where strains belonging to different species and genera, commonly found in these foods, have been characterized for their decarboxylase activities and have been associated with high levels of BAs. Due to their impact on human health and food quality, both the development of simple and rapid methods for BA detection and the increase of knowledge of factors involved in BA accumulation are needed to face new challenges in food chains and to reduce health concerns regarding food poisoning.

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Seiler, Nikolaus. "Functions of polyamine acetylation." Canadian Journal of Physiology and Pharmacology 65, no. 10 (October 1, 1987): 2024–35. http://dx.doi.org/10.1139/y87-317.

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Acetylation is a means to decrease the net positive charge of the plyamines and thus liberate polyamines from anionic binding sites. The acetyl derivatives can be removed from the cells by transport and catabolism. Intracellular polyamine metabolism can be formulated as a cyclic process, which explains the transformation of one polyamine into another. As a net result, this pathway metabolizes (in an energy-requiring manner) methionine to 5′-deoxy-5′-methylthioadenosine and β-alanine, and thus appears to be futile. It is suggested that the cyclic process is necessary for the precise control of cellular polyamine concentrations, as it allows relatively rapid spermine and spermidine concentration changes, in spite of a slow basal turnover rate. For the regulation of cellular polyamine metabolism, two decarboxylases, L-ornithine decarboxylase and S-adenosyl-L-methionine decarboxylase; the cytosolic acetyl-CoA:spermidine/spermine N1-acetyltransferase; and a polyamine transport system are required. The activity of the nucelar acetyltransferase is assumed to be the rate-limiting enzyme of nuclear polyamine turnover. The complexity and high level of sophistication of polyamine regulation is strong evidence for the important functional significance of the natural polyamines.

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Li, Tong, Pierre Juteau, Réjean Beaudet, François Lépine, Richard Villemur, and Jean-Guy Bisaillon. "Purification and characterization of a 4-hydroxybenzoate decarboxylase from an anaerobic coculture." Canadian Journal of Microbiology 46, no. 9 (September 1, 2000): 856–59. http://dx.doi.org/10.1139/w00-067.

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The oxygen-sensitive 4-hydroxybenzoate decarboxylase (4OHB-DC) activity from a phenol-carboxylating coculture, consisting of Clostridium-like strain 6 and an unidentified strain 7, was studied. Assays done with cell extracts showed that the optimal pH was 5.0-6.5 and the Kmwas 5.4 mM. The activity decreased by 50% in the presence of 5 mM EDTA, and it was restored and even enhanced by the addition of Mg++, Mn++, Zn++, or Ca++. After purification, the molecular mass of the enzyme was estimated as 420 kDa by gel chromatography, and as 119 kDa by SDS-PAGE, suggesting a homotetrameric structure. Its pI was 5.6. The N-terminal amino acid sequence showed 95% and 76% homology with the pyruvate-flavodoxin oxidoreductase (nifJ gene product) from Enterobacter agglomerans and Klebsiella pneumoniae, respectively. The purified enzyme also slowly catalyzed the reverse reaction, that is the phenol carboxylation. These characteristics suggest that this enzyme is different from other known decarboxylases. This includes the 4OHB-DC from Clostridium hydroxybenzoicum, which is the only one that had been purified before.Key words: purification, 4-hydroxybenzoate decarboxylase, coculture, phenol carboxylation, anaerobic conditions.

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Xue, Yaju, Yongliang Zhao, Xiuling Ji, Jiahao Yao, Peter Kamp Busk, Lene Lange, Yuhong Huang, and Suojiang Zhang. "Advances in bio-nylon 5X: discovery of new lysine decarboxylases for the high-level production of cadaverine." Green Chemistry 22, no. 24 (2020): 8656–68. http://dx.doi.org/10.1039/d0gc03100c.

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47

Romano, Andrea, Hein Trip, Aline Lonvaud-Funel, Juke S. Lolkema, and Patrick M. Lucas. "Evidence of Two Functionally Distinct Ornithine Decarboxylation Systems in Lactic Acid Bacteria." Applied and Environmental Microbiology 78, no. 6 (January 13, 2012): 1953–61. http://dx.doi.org/10.1128/aem.07161-11.

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ABSTRACTBiogenic amines are low-molecular-weight organic bases whose presence in food can result in health problems. The biosynthesis of biogenic amines in fermented foods mostly proceeds through amino acid decarboxylation carried out by lactic acid bacteria (LAB), but not all systems leading to biogenic amine production by LAB have been thoroughly characterized. Here, putative ornithine decarboxylation pathways consisting of a putative ornithine decarboxylase and an amino acid transporter were identified in LAB by strain collection screening and database searches. The decarboxylases were produced in heterologous hosts and purified and characterizedin vitro, whereas transporters were heterologously expressed inLactococcus lactisand functionally characterizedin vivo. Amino acid decarboxylation by whole cells of the original hosts was determined as well. We concluded that two distinct types of ornithine decarboxylation systems exist in LAB. One is composed of an ornithine decarboxylase coupled to an ornithine/putrescine transmembrane exchanger. Their combined activities results in the extracellular release of putrescine. This typical amino acid decarboxylation system is present in only a few LAB strains and may contribute to metabolic energy production and/or pH homeostasis. The second system is widespread among LAB. It is composed of a decarboxylase active on ornithine andl-2,4-diaminobutyric acid (DABA) and a transporter that mediates unidirectional transport of ornithine into the cytoplasm. Diamines that result from this second system are retained within the cytosol.

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Karvonen, E., L. Kauppinen, T. Partanen, and H. Pösö. "Irreversible inhibition of putrescine-stimulated S-adenosyl-l-methionine decarboxylase by berenil and pentamidine." Biochemical Journal 231, no. 1 (October 1, 1985): 165–69. http://dx.doi.org/10.1042/bj2310165.

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The putrescine-stimulated S-adenosyl-L-methionine decarboxylases from rat liver and yeast were strongly inhibited by Berenil and to a lesser extent by Pentamidine. Ten times greater drug concentrations were needed to achieve a similar level of inhibition of a Mg2+-stimulated bacterial enzyme. The inhibition was irreversible in that extensive dialyses or precipitation with (NH4)2SO4 did not restore enzyme activity. Putrescine did not protect the enzyme against Berenil, but adenosylmethionine either alone or with putrescine partially protected the irreversible action of Berenil. The compound 4,4′-diamidinodiphenylamine, which differs from Berenil only in lacking the azo group between benzene rings, was a weaker inhibitor than Berenil, and its inhibition was reversible. Berenil also inhibited the activity of adenosylmethionine decarboxylase in vivo, by depressing the activity of the enzyme in normal rat liver, for at least 24 h after a single injection (50 mg/kg body wt.) of the drug.

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Upadhyay, Rakesh K., Tahira Fatima, Avtar K. Handa, and Autar K. Mattoo. "Polyamines and Their Biosynthesis/Catabolism Genes Are Differentially Modulated in Response to Heat Versus Cold Stress in Tomato Leaves (Solanum lycopersicum L.)." Cells 9, no. 8 (July 22, 2020): 1749. http://dx.doi.org/10.3390/cells9081749.

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Polyamines (PAs) regulate growth in plants and modulate the whole plant life cycle. They have been associated with different abiotic and biotic stresses, but little is known about the molecular regulation involved. We quantified gene expression of PA anabolic and catabolic pathway enzymes in tomato (Solanum lycopersicum cv. Ailsa Craig) leaves under heat versus cold stress. These include arginase 1 and 2, arginine decarboxylase 1 and 2, agmatine iminohydrolase/deiminase 1, N-carbamoyl putrescine amidase, two ornithine decarboxylases, three S-adenosylmethionine decarboxylases, two spermidine synthases; spermine synthase; flavin-dependent polyamine oxidases (SlPAO4-like and SlPAO2) and copper dependent amine oxidases (SlCuAO and SlCuAO-like). The spatiotemporal transcript abundances using qRT-PCR revealed presence of their transcripts in all tissues examined, with higher transcript levels observed for SAMDC1, SAMDC2 and ADC2 in most tissues. Cellular levels of free and conjugated forms of putrescine and spermidine were found to decline during heat stress while they increased in response to cold stress, revealing their differential responses. Transcript levels of ARG2, SPDS2, and PAO4-like increased in response to both heat and cold stresses. However, transcript levels of ARG1/2, AIH1, CPA, SPDS1 and CuAO4 increased in response to heat while those of ARG2, ADC1,2, ODC1, SAMDC1,2,3, PAO2 and CuPAO4-like increased in response to cold stress, respectively. Transcripts of ADC1,2, ODC1,2, and SPMS declined in response to heat stress while ODC2 transcripts declined under cold stress. These results show differential expression of PA metabolism genes under heat and cold stresses with more impairment clearly seen under heat stress. We interpret these results to indicate a more pronounced role of PAs in cold stress acclimation compared to that under heat stress in tomato leaves.

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Giardina, G., R. Montioli, S. Gianni, B. Cellini, A. Paiardini, C. B. Voltattorni, and F. Cutruzzola. "Open conformation of human DOPA decarboxylase reveals the mechanism of PLP addition to Group II decarboxylases." Proceedings of the National Academy of Sciences 108, no. 51 (December 5, 2011): 20514–19. http://dx.doi.org/10.1073/pnas.1111456108.

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Journal articles on the topic 'Decarboxylases'

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