Relevant bibliographies by topics / Decarboxylases

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Decarboxylases'

Author: Grafiati
Published: 4 June 2021
Last updated: 31 July 2024

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Journal articles on the topic "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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Dissertations / Theses on the topic "Decarboxylases"

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Fogle, Emily Joyce. "Kinetic characterization of pyridoxal 5'-phosphate dependent decarboxylases : dialkylglycine decarboxylase and diaminopimelate decarboxylase /." For electronic version search Digital dissertations database. Restricted to UC campuses. Access is free to UC campus dissertations, 2005. http://uclibs.org/PID/11984.

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Spence, Michael Patrick. "Plant aromatic amino acid decarboxylases: Evolutionary divergence, physiological function, structure function relationships and biochemical properties." Diss., Virginia Tech, 2014. http://hdl.handle.net/10919/49432.

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Plant aromatic amino acid decarboxylases (AAADs) are a group of economically important enzymes categorically joined through their pyridoxal 5'-phosphate (PLP) dependence and sequence homology. Extensive evolutionary divergence of this enzyme family has resulted in a selection of enzymes with stringent aromatic amino acid substrate specificities. Variations in substrate specificities enable individual enzymes to catalyze key reactions in a diverse set of pathways impacting the synthesis of monoterpenoid indole alkaloids (including the pharmacologically active vinblastine and quinine), benzylisoquinoline alkaloids (including the pharmacologically active papaverine, codeine, morphine, and sanguinarine), and antioxidant and chemotherapeutic amides. Recent studies of plant AAAD proteins demonstrated that in addition to the typical decarboxylation enzymes, some annotated plant AAAD proteins are actually aromatic acetaldehyde synthases (AASs). These AASs catalyze a decarboxylation-oxidative deamination process of aromatic amino acids, leading to the production of aromatic acetaldehydes rather than the AAAD derived arylalkylamines. Research has implicated that plant AAS enzymes are involved in the production of volatile flower scents, floral attractants, and defensive phenolic acetaldehyde secondary metabolites. Historically, the structural elements responsible for differentiating plant AAAD substrate specificity and activity have been difficult to identify due to strong AAAD and AAS inter-enzyme homology. Through extensive bioinformatic analysis and experimental verification of plant AAADs, we have determined some structural elements unique to given types of AAADs. This document highlights structural components apparently responsible for the differentiation of activity and substrate specificity. In addition to producing primary sequence identifiers capable of AAAD activity and substrate specificity differentiation, this work has also demonstrated applications of AAAD enzyme engineering and novel activity identification.
Ph. D.
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Parsanejad, Reza. "Phosphoenolpyruvate carboxykinase and ornithine decarboxylase genes : allelic variations and associations with traits in poultry." Thesis, McGill University, 2003. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=84307.

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The objectives of this study were to identify genetic variants, develop the respective haplotypes (combination of alleles) and investigate the association of identified variants with economically important traits in two candidate genes. The first gene was Phosphoenolpyruvate carboxykinase (PEPCK) which is a key regulatory enzyme of gluconeogenesis. The second candidate gene, Ornithine decarboxylase (ODC), is a rate-limiting enzyme in polyamine biosynthesis. It has a significant role in DNA synthesis and cell proliferation. We first analyzed the genetic variability of PEPCK-C, the gene which codes for the cytosolic form of PEPCK. A 3792 by segment of 5'-region of the PEPCK-C gene (pos. -1723 to 2069) was sequenced in 32 White Leghorn chickens (a total of 64 genomes). A total of 19 single nucleotide polymorphisms (SNPs) were identified. We then analyzed the genetic variability of ODC. A 5 kb sequence of 3' end of the gene was sequenced in 20 White Leghorn chickens (a total of 40 genomes). A total of 63 variant sites were identified. The rate of insertion/deletion in ODC was 16%, whereas neither deletions nor insertions were present in PEPCK-C. Gene trees were constructed for both genes assuming maximal parsimony. This led to the delineation of 6 haplotypes in PEPCK-C. Two of the SNPs coincided with RFLP detectable by the restriction enzymes AciI and BstEII, respectively. Three haplotypes in ODC were defined. In the next step, White Leghorn chickens from a non-selected closed population were typed for these two PEPCK-C RFLP. The two RFLP gave rise to three alleles (or haplotype classes), which in turn defined six genotypes. A comparison of genotypes revealed significant differences in feed efficiency (FE) and residual feed consumption (RFC). There was significant interaction between PEPCK-C genotypes and mitochondrial PEPCK (PEPCK-M) genotypes defined by an RFLP. The latter enzyme catalyzes the same reaction, but is located in the matrix of t
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Blalock, LeeAnn Talarico. "Expression of pyruvate decarboxylase in a Gram positive host Sarcina ventriculi pyruvate decarboxylase versus other known pyruvate decarboxylases /." [Gainesville, Fla.] : University of Florida, 2003. http://purl.fcla.edu/fcla/etd/UFE0002366.

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Tran, Linh N. "Synthesizing Antifungal Agents." Fogler Library, University of Maine, 2007. http://www.library.umaine.edu/theses/pdf/TranLN2007.pdf.

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Pandey, Arti Sharma. "Structure based mechanistic studies on 2-ketopropyl coenzyme M oxidoreductase / carboxylase from Xanthobacter autotrophicus and [FeFe] hydrogenase from Clostridium pasteurianum." Diss., Montana State University, 2007. http://etd.lib.montana.edu/etd/2007/pandey/PandeyA1207.pdf.

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丘國明 and Kwok-ming Yao. "Purification and characterization of ornithine decarbozylase fromtetrahymena thermophila." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 1986. http://hub.hku.hk/bib/B31207480.

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Yao, Kwok-ming. "Purification and characterization of ornithine decarbozylase fromtetrahymena thermophila /." Hong Kong : [University of Hong Kong], 1986. http://sunzi.lib.hku.hk/hkuto/record.jsp?B12322829.

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Laitinen, Päivi. "Antizyme in the regulation of mouse brain ornithine decarboxylase." Oulu : University of Oulu, 1986. http://catalog.hathitrust.org/api/volumes/oclc/16882622.html.

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GLASS, JAMES RUSSELL. "POLYAMINE-MEDIATED DEGRADATION OF ORNITHINE DECARBOXYLASE IN CHINESE HAMSTER OVARY CELLS." Diss., The University of Arizona, 1987. http://hdl.handle.net/10150/184002.

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The objective of this research was to identify specific mechanisms involved in the regulation of ornithine decarboxylase, the first enzyme in the polyamine biosynthetic pathway. Immunochemical techniques were used to study post-translational modifications of the ODC protein in relation to activity alterations. Initial experimentation showed that Chinese hamster cells maintained in a defined medium express an ODC protein stable to intracellular degradation. Treatment of these cells with exogenous ornithine or polyamines resulted in a rapid loss of enzyme activity, without detectable changes in the enzyme specific activity. The loss of enzyme activity was a result of accelerated ODC degradation, as determined by immunoprecipitation of pre-labeled protein. In addition, spermidine, but not ornithine, totally inhibited new ODC synthesis. The mechanism of accelerated ODC degradation was investigated and found to occur by an apparent novel mechanism. Degradation of ODC was both ubiquitin-independent and non-lysosomal, and there was also no detectable accumulation of a modified form of ODC protein. In addition, it was found that a component of protein synthesis is required for this process, as inhibitors (cycloheximide, emetine, puromycin) blocked polyamine-accelerated degradation. ODC cDNA was used to synthesize both ODC specific mRNA and protein using in vitro synthesis. These systems may allow the generation of sufficient quantities of material which can be used to recreate in vitro the specific components involved in polyamine inhibition of ODC synthesis and the protease(s) responsible for degradation. The major finding of this work is the direct demonstration that ODC is a stable intracellular protein in the absence of putrescine and spermidine depleted cells (Chapter 2). In addition, that degradation occurs by a novel mechanism, with a requirement for some component of protein synthesis (Chapter 3). Finally, these studies describe the in vitro production of ODC protein and mRNA, which should facilitate further studies of polyamine regulation of ODC degradation and synthesis (Chapter 4).
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Books on the topic "Decarboxylases"

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Goddijn, Oscar Johannes Maria. Regulation of terpenoid indole alkaloid biosynthesis in Catharanthus roseus: The tryptophan decarboxylase gene. Alblasserdam: Offsetdrukkerij Haveka BV, 1992.

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Lee, J. K., ed. Orotidine Monophosphate Decarboxylase. Berlin, Heidelberg: Springer Berlin Heidelberg, 2004. http://dx.doi.org/10.1007/b84246.

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1949-, Sayler Gary S., and Blackburn James W. 1950-, eds. Microbiological decomposition of chlorinated aromatic compounds. New York: M. Dekker, 1987.

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K, Lee J., and Tantillo D. J, eds. Orotidine monophosphate decarboxylase: A mechanistic dialogue. Berlin: Springer, 2004.

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Shin-ichi, Hayashi, ed. Ornithine decarboxylase: Biology, enzymology, and molecular genetics. New York: Pergamon Press, 1989.

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Pritchard, Jane Elisabeth. Genetic characterization of cysteine sulphinic acid decarboxylase. Birmingham: University of Birmingham, 1999.

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Hoskin, Nathan. Polyamines and ornithine decarboxylase in carcinogenesis and neoplasia. Bethesda, MD: U.S. Dept. of Health and Human Services, Public Health Service, National Institutes of Health, National Cancer Institute, International Cancer Research Data Bank, 1988.

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Laitinen, Päivi. Antizyme in the regulation of mouse brain ornithine decarboxylase. Oulu: University of Oulu, 1986.

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Linden, Margareta. Role of putrescine in the regulation of ornithine decarboxylase and cell growth. [s.l.]: [s.n.], 1985.

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Johnen, Sandra. Biosynthese von Phosphonaten: Charakterisierung des rekombinanten Enzyms Phosphonopyruvat-Decarboxylase aus Streptomyces viridochromogenes Tü494. Jülich: Jülich Forschungszentrum Jülich, Zentralbibliothek, 2005.

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Book chapters on the topic "Decarboxylases"

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Gale, Ernest F. "The Bacterial Amino Acid Decarboxylases." In Advances in Enzymology - and Related Areas of Molecular Biology, 1–32. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/9780470122518.ch1.

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Makris, Thomas M. "CHAPTER 6. Cytochrome P450 Decarboxylases." In Dioxygen-dependent Heme Enzymes, 127–43. Cambridge: Royal Society of Chemistry, 2018. http://dx.doi.org/10.1039/9781788012911-00127.

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Ward, Owen P., Richard Wilcocks, Elizabeth Prosen, Scott Collins, Nolan J. Dewdney, and Yaping Hong. "Acyloin Formation Mediated by Benzoylformate Decarboxylases." In Microbial Reagents in Organic Synthesis, 67–75. Dordrecht: Springer Netherlands, 1992. http://dx.doi.org/10.1007/978-94-011-2444-7_6.

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Blaschko, H. "The Amino Acid Decarboxylases of Mammalian Tissue." In Advances in Enzymology - and Related Areas of Molecular Biology, 67–85. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/9780470122501.ch3.

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Gale, Ernest F. "Determination of Amino Acids by Use of Bacterial Amino Acid Decarboxylases." In Methods of Biochemical Analysis, 285–306. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/9780470110201.ch8.

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Gooch, Jan W. "Decarboxylate." In Encyclopedic Dictionary of Polymers, 196. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4419-6247-8_3330.

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Schomburg, Dietmar, and Margit Salzmann. "Pyruvate decarboxylase." In Enzyme Handbook 1, 1–5. Berlin, Heidelberg: Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-86605-0_1.

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Schomburg, Dietmar, and Margit Salzmann. "Valine decarboxylase." In Enzyme Handbook 1, 49–51. Berlin, Heidelberg: Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-86605-0_12.

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Schomburg, Dietmar, and Margit Salzmann. "Glutamate decarboxylase." In Enzyme Handbook 1, 53–56. Berlin, Heidelberg: Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-86605-0_13.

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Schomburg, Dietmar, and Margit Salzmann. "Hydroxyglutamate decarboxylase." In Enzyme Handbook 1, 57–59. Berlin, Heidelberg: Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-86605-0_14.

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Conference papers on the topic "Decarboxylases"

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Fei Zhu, Sheng Hu, Lehe Mei, Jun Huang, and Lehe Mei. "Integrated purification and immobilization of glutamate decarboxylase." In 2011 International Conference on Remote Sensing, Environment and Transportation Engineering (RSETE). IEEE, 2011. http://dx.doi.org/10.1109/rsete.2011.5965951.

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Gratz, M., S. Hofmann, C. Kuhn, S. Mahner, U. Jeschke, and A. Vattai. "Verminderte Expression der L-DOPA Decarboxylase im Abortgeschehen." In Jahrestagung der Österreichischen Gesellschaft für Gynäkologie und Geburtshilfe (OEGGG) gemeinsam mit der Bayerischen Gesellschaft für Geburtshilfe und Frauenheilkunde e.V (BGGF). Georg Thieme Verlag KG, 2017. http://dx.doi.org/10.1055/s-0037-1602266.

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Yip, Kenneth W., Zhan Zhang, Noriko Sakemura-Nakatsugawa, Jui-Wen Huang, Shijun Yue, Yulia Jitkova, Terence To, et al. "Abstract 2510: A porphodimethene chemical inhibitor of uroporphyrinogen decarboxylase." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-2510.

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Alptekin, Ahmet, Jane Ding, Bingwei Ye, and Han-Fei Ding. "Abstract 4374: The role of glycine decarboxylase in neuroblastoma." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-4374.

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Keough, Martin P., Karen DeFeo, Candace S. Hayes, and Susan K. Gilmour. "Abstract 2471: Immunosuppressive effect of elevated epidermal ornithine decarboxylase activity." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-2471.

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Barry, Elizabeth L., Leila A. Mott, Robert S. Sandler, Dennis J. Ahnen, and John A. Baron. "Abstract 2831: Ornithine decarboxylase polymorphisms and risk of colorectal adenoma." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-2831.

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Bernichi, João Victor Polegato, Robson Marques Figueiredo Rocha Teixeira, and Maria Stela Lessa Paganelli. "Aromatic L-amino acids decarboxylase (AADC) deficiency: a case report." In SBN Conference 2022. Thieme Revinter Publicações Ltda., 2023. http://dx.doi.org/10.1055/s-0043-1774571.

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North, ML, N. Khanna, H. Grasemann, and JA Scott. "Ornithine Decarboxylase Inhibition in an Acute Murine Model of Allergic Inflammation." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a4231.

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Kim, Hong Im, Chad R. Schultz, Andrea L. Buras, Elizabeth Friedman, Alyssa M. Fedorko, Leigh G. Seamon, Gadisetti Chandramouli, André S. Bachmann, and John I. Risinger. "Abstract 1242: Ornithine decarboxylase as a therapeutic target in endometrial cancer." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-1242.

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Schultz, Chad R., Martin C. Gruhlke, Alan J. Slusarenko, and Andre S. Bachmann. "Abstract 464: Allicin, a potent new ornithine decarboxylase inhibitor in neuroblastoma." In Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-464.

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Reports on the topic "Decarboxylases"

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Manni, Andrea. Relative Contribution of Ornithine Decarboxylase (ODC) Versus S-adenosylmethionine Decarboxylase (SAMDC) to Human Breast Cancer Progression and Development. Fort Belvoir, VA: Defense Technical Information Center, July 2002. http://dx.doi.org/10.21236/ada408110.

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Kuhajda, Francis P. Malonyl-CoA Decarboxylase (MCD) as a Potential Therapeutic Target for Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, May 2008. http://dx.doi.org/10.21236/ada508649.

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Locy, Robert D., Hillel Fromm, Joe H. Cherry, and Narendra K. Singh. Regulation of Arabidopsis Glutamate Decarboxylase in Response to Heat Stress: Modulation of Enzyme Activity and Gene Expression. United States Department of Agriculture, January 2001. http://dx.doi.org/10.32747/2001.7575288.bard.

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Most plants accumulate the nonprotein amino acid, g-aminobutyric acid (GABA), in response to heat stress. GABA is made from glutamate in a reaction catalyzed by glutamate decarboxylase (GAD), an enzyme that has been shown by the Israeli PI to be a calmodulin (CaM) binding protein whose activity is regulated in vitro by calcium and CaM. In Arabidopsis there are at least 5 GAD genes, two isoforms of GAD, GAD1 and GAD2, are known to be expressed, both of which appear to be calmodulin-binding proteins. The role of GABA accumulation in stress tolerance remains unclear, and thus the objectives of the proposed work are intended to clarify the possible roles of GABA in stress tolerance by studying the factors which regulate the activity of GAD in vivo. Our intent was to demonstrate the factors that mediate the expression of GAD activity by analyzing the promoters of the GAD1 and GAD2 genes, to determine the role of stress induced calcium signaling in the regulation of GAD activity, to investigate the role of phosphorylation of the CaM-binding domain in the regulation of GAD activity, and to investigate whether ABA signaling could be involved in GAD regulation via the following set of original Project Objectives: 1. Construction of chimeric GAD1 and GAD2 promoter/reporter gene fusions and their utilization for determining cell-specific expression of GAD genes in Arabidopsis. 2. Utilizing transgenic plants harboring chimeric GAD1 promoter-luciferase constructs for isolating mutants in genes controlling GAD1 gene activation in response to heat shock. 3. Assess the role of Ca2+/CaM in the regulation of GAD activity in vivo in Arabidopsis. 4. Study the possible phosphorylation of GAD as a means of regulation of GAD activity. 5. Utilize ABA mutants of Arabidopsis to assess the involvement of this phytohormone in GAD activation by stress stimuli. The major conclusions of Objective 1 was that GAD1 was strongly expressed in the elongating region of the root, while GAD2 was mainly expressed along the phloem in both roots and shoots. In addition, GAD activity was found not to be transcriptionally regulated in response to heat stress. Subsequently, The Israeli side obtained a GAD1 knockout mutation, and in light of the objective 1 results it was determined that characterization of this knockout mutation would contribute more to the project than the proposed Objective 2. The major conclusion of Objective 3 is that heat-stress-induced changes in GAD activity can be explained by heat-stress-induced changes in cytosolic calcium levels. No evidence that GAD activity was transcriptionally or translationally regulated or that protein phosphorylation was involved in GAD regulation (objective 4) was obtained. Previously published data by others showing that in wheat roots ABA regulated GABA accumulation proved not to be the case in Arabidopsis (Objective 5). Consequently, we put the remaining effort in the project into the selection of mutants related to temperature adaptation and GABA utilization and attempting to characterize events resulting from GABA accumulation. A set of 3 heat sensitive mutants that appear to have GABA related mutations have been isolated and partially characterized, and a study linking GABA accumulation to growth stimulation and altered nitrate assimilation were conducted. By providing a better understanding of how GAD activity was and was not regulated in vivo, we have ruled out the use of certain genes for genetically engineering thermotolerance, and suggested other areas of endeavor related to the thrust of the project that may be more likely approaches to genetically engineering thermotolerance.
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Fromm, Hillel, and Joe Poovaiah. Calcium- and Calmodulin-Mediated Regulation of Plant Responses to Stress. United States Department of Agriculture, September 1993. http://dx.doi.org/10.32747/1993.7568096.bard.

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We have taken a molecular approach to clone cellular targets of calcium/calmodulin (Ca2+/CaM). A 35S-labeled recombinant CaM was used as a probe to screen various cDNA expression libraries. One of the isolated clones from petunia codes for the enzyme glutamate decarboxylase (GAD) which catalyzes the conversion of glutamate to g-aminobutyric acid (GABA). The activity of plant GAD has been shown to be dramatically enhanced in response to cold and heat shock, anoxia, drought, mechanical manipulations and by exogenous application of the stress phytohormone ABA in wheat roots. We have purified the recombinant GAD by CaM-affinity chromatography and studied its regulation by Ca2+/CaM. At a physiological pH range (7.0-7.5), the purified enzyme was inactive in the absence of Ca2+ and CaM but could be stimulated to high levels of activity by the addition of exogenous CaM (K0.5 = 15 nM) in the presence of Ca2+ (K 0.5 = 0.8 mM). Neither Ca2+ nor CaM alone had any effect on GAD activity. Transgenic tobacco plants expressing a mutant petunia GAD lacking the CaM-binding domain, or transgenic plants expressing the intact GAD were prepared and studied in detail. We have shown that the CaM-binding domain is necessary for the regulation of glutamate and GABA metabolism and for normal plant development. Moreover, we found that CaM is tightly associated with a 500 kDa GAD complex. The tight association of CaM with its target may be important for the rapid modulation of GAD activity by Ca2+ signaling in response to stresses.
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Or, Etti, David Galbraith, and Anne Fennell. Exploring mechanisms involved in grape bud dormancy: Large-scale analysis of expression reprogramming following controlled dormancy induction and dormancy release. United States Department of Agriculture, December 2002. http://dx.doi.org/10.32747/2002.7587232.bard.

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The timing of dormancy induction and release is very important to the economic production of table grape. Advances in manipulation of dormancy induction and dormancy release are dependent on the establishment of a comprehensive understanding of biological mechanisms involved in bud dormancy. To gain insight into these mechanisms we initiated the research that had two main objectives: A. Analyzing the expression profiles of large subsets of genes, following controlled dormancy induction and dormancy release, and assessing the role of known metabolic pathways, known regulatory genes and novel sequences involved in these processes B. Comparing expression profiles following the perception of various artificial as well as natural signals known to induce dormancy release, and searching for gene showing similar expression patterns, as candidates for further study of pathways having potential to play a central role in dormancy release. We first created targeted EST collections from V. vinifera and V. riparia mature buds. Clones were randomly selected from cDNA libraries prepared following controlled dormancy release and controlled dormancy induction and from respective controls. The entire collection (7920 vinifera and 1194 riparia clones) was sequenced and subjected to bioinformatics analysis, including clustering, annotations and GO classifications. PCR products from the entire collection were used for printing of cDNA microarrays. Bud tissue in general, and the dormant bud in particular, are under-represented within the grape EST database. Accordingly, 59% of the our vinifera EST collection, composed of 5516 unigenes, are not included within the current Vitis TIGR collection and about 22% of these transcripts bear no resemblance to any known plant transcript, corroborating the current need for our targeted EST collection and the bud specific cDNA array. Analysis of the V. riparia sequences yielded 814 unigenes, of which 140 are unique (keilin et al., manuscript, Appendix B). Results from computational expression profiling of the vinifera collection suggest that oxidative stress, calcium signaling, intracellular vesicle trafficking and anaerobic mode of carbohydrate metabolism play a role in the regulation and execution of grape-bud dormancy release. A comprehensive analysis confirmed the induction of transcription from several calcium–signaling related genes following HC treatment, and detected an inhibiting effect of calcium channel blocker and calcium chelator on HC-induced and chilling-induced bud break. It also detected the existence of HC-induced and calcium dependent protein phosphorylation activity. These data suggest, for the first time, that calcium signaling is involved in the mechanism of dormancy release (Pang et al., in preparation). We compared the effects of heat shock (HS) to those detected in buds following HC application and found that HS lead to earlier and higher bud break. We also demonstrated similar temporary reduction in catalase expression and temporary induction of ascorbate peroxidase, glutathione reductase, thioredoxin and glutathione S transferase expression following both treatments. These findings further support the assumption that temporary oxidative stress is part of the mechanism leading to bud break. The temporary induction of sucrose syntase, pyruvate decarboxylase and alcohol dehydrogenase indicate that temporary respiratory stress is developed and suggest that mitochondrial function may be of central importance for that mechanism. These finding, suggesting triggering of identical mechanisms by HS and HC, justified the comparison of expression profiles of HC and HS treated buds, as a tool for the identification of pathways with a central role in dormancy release (Halaly et al., in preparation). RNA samples from buds treated with HS, HC and water were hybridized with the cDNA arrays in an interconnected loop design. Differentially expressed genes from the were selected using R-language package from Bioconductor project called LIMMA and clones showing a significant change following both HS and HC treatments, compared to control, were selected for further analysis. A total of 1541 clones show significant induction, of which 37% have no hit or unknown function and the rest represent 661 genes with identified function. Similarly, out of 1452 clones showing significant reduction, only 53% of the clones have identified function and they represent 573 genes. The 661 induced genes are involved in 445 different molecular functions. About 90% of those functions were classified to 20 categories based on careful survey of the literature. Among other things, it appears that carbohydrate metabolism and mitochondrial function may be of central importance in the mechanism of dormancy release and studies in this direction are ongoing. Analysis of the reduced function is ongoing (Appendix A). A second set of hybridizations was carried out with RNA samples from buds exposed to short photoperiod, leading to induction of bud dormancy, and long photoperiod treatment, as control. Analysis indicated that 42 genes were significant difference between LD and SD and 11 of these were unique.
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(Pyruvate decarboxylase: A key enzyme for alcohol production). Office of Scientific and Technical Information (OSTI), January 1989. http://dx.doi.org/10.2172/5454091.

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