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Journal articles on the topic '3-dioxygenase'

Author: Grafiati

Published: 4 June 2021

Last updated: 7 July 2024

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1

Mars, Astrid E., Jaap Kingma, Stefan R. Kaschabek, Walter Reineke, and Dick B. Janssen. "Conversion of 3-Chlorocatechol by Various Catechol 2,3-Dioxygenases and Sequence Analysis of the Chlorocatechol Dioxygenase Region of Pseudomonas putida GJ31." Journal of Bacteriology 181, no. 4 (1999): 1309–18. http://dx.doi.org/10.1128/jb.181.4.1309-1318.1999.

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ABSTRACT Pseudomonas putida GJ31 contains an unusual catechol 2,3-dioxygenase that converts 3-chlorocatechol and 3-methylcatechol, which enables the organism to use both chloroaromatics and methylaromatics for growth. A 3.1-kb region of genomic DNA of strain GJ31 containing the gene for this chlorocatechol 2,3-dioxygenase (cbzE) was cloned and sequenced. The cbzE gene appeared to be plasmid localized and was found in a region that also harbors genes encoding a transposase, a ferredoxin that was homologous to XylT, an open reading frame with similarity to a protein of ameta-cleavage pathway wit

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2

Khan, Ashraf A., Rong-Fu Wang, Wei-Wen Cao, Daniel R. Doerge, David Wennerstrom, and Carl E. Cerniglia. "Molecular Cloning, Nucleotide Sequence, and Expression of Genes Encoding a Polycyclic Aromatic Ring Dioxygenase from Mycobacterium sp. Strain PYR-1." Applied and Environmental Microbiology 67, no. 8 (2001): 3577–85. http://dx.doi.org/10.1128/aem.67.8.3577-3585.2001.

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ABSTRACT Mycobacterium sp. strain PYR-1 degrades high-molecular-weight polycyclic hydrocarbons (PAHs) primarily through the introduction of both atoms of molecular oxygen by a dioxygenase. To clone the dioxygenase genes involved in PAH degradation, two-dimensional (2D) gel electrophoresis of PAH-induced proteins from cultures of Mycobacterium sp. strain PYR-1 was used to detect proteins that increased after phenanthrene, dibenzothiophene, and pyrene exposure. Comparison of proteins from induced and uninduced cultures on 2D gels indicated that at least six major proteins were expressed (105, 81

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3

Kaschabek, Stefan R., Thomas Kasberg, Dagmar Müller, Astrid E. Mars, Dick B. Janssen, and Walter Reineke. "Degradation of Chloroaromatics: Purification and Characterization of a Novel Type of Chlorocatechol 2,3-Dioxygenase of Pseudomonas putida GJ31." Journal of Bacteriology 180, no. 2 (1998): 296–302. http://dx.doi.org/10.1128/jb.180.2.296-302.1998.

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ABSTRACT A purification procedure for a new kind of extradiol dioxygenase, termed chlorocatechol 2,3-dioxygenase, that converts 3-chlorocatechol productively was developed. Structural and kinetic properties of the enzyme, which is part of the degradative pathway used for growth ofPseudomonas putida GJ31 with chlorobenzene, were investigated. The enzyme has a subunit molecular mass of 33.4 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Estimation of the native M r value under nondenaturating conditions by gel filtration gave a molecular mass of 135 ± 10 kDa, indicating a homo

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4

Liu, Hong, Shu-Jun Wang, Jun-Jie Zhang, Hui Dai, Huiru Tang, and Ning-Yi Zhou. "Patchwork Assembly ofnag-Like Nitroarene Dioxygenase Genes and the 3-Chlorocatechol Degradation Cluster for Evolution of the 2-Chloronitrobenzene Catabolism Pathway in Pseudomonas stutzeri ZWLR2-1." Applied and Environmental Microbiology 77, no. 13 (2011): 4547–52. http://dx.doi.org/10.1128/aem.02543-10.

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ABSTRACTPseudomonas stutzeriZWLR2-1 utilizes 2-chloronitrobenzene (2CNB) as a sole source of carbon, nitrogen, and energy. To identify genes involved in this pathway, a 16.2-kb DNA fragment containing putative 2CNB dioxygenase genes was cloned and sequenced. Of the products from the 19 open reading frames that resulted from this fragment, CnbAc and CnbAd exhibited striking identities to the respective α and β subunits of the Nag-like ring-hydroxylating dioxygenases involved in the metabolism of nitrotoluene, nitrobenzene, and naphthalene. The encoding genes were also flanked by two copies of i

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5

Mahan, Kristina M., Joseph T. Penrod, Kou-San Ju, et al. "Selection for Growth on 3-Nitrotoluene by 2-Nitrotoluene-Utilizing Acidovorax sp. Strain JS42 Identifies Nitroarene Dioxygenases with Altered Specificities." Applied and Environmental Microbiology 81, no. 1 (2014): 309–19. http://dx.doi.org/10.1128/aem.02772-14.

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ABSTRACTAcidovoraxsp. strain JS42 uses 2-nitrotoluene as a sole source of carbon and energy. The first enzyme of the degradation pathway, 2-nitrotoluene 2,3-dioxygenase, adds both atoms of molecular oxygen to 2-nitrotoluene, forming nitrite and 3-methylcatechol. All three mononitrotoluene isomers serve as substrates for 2-nitrotoluene dioxygenase, but strain JS42 is unable to grow on 3- or 4-nitrotoluene. Using both long- and short-term selections, we obtained spontaneous mutants of strain JS42 that grew on 3-nitrotoluene. All of the strains obtained by short-term selection had mutations in th

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6

Boyd, Derek R., Narain D. Sharma, Ludmila V. Modyanova, et al. "Dioxygenase-catalyzed cis-dihydroxylation of pyridine-ring systems." Canadian Journal of Chemistry 80, no. 6 (2002): 589–600. http://dx.doi.org/10.1139/v02-062.

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Toluene dioxygenase-catalyzed dihydroxylation, in the carbocyclic rings of quinoline, 2-chloroquinoline, 2-methoxyquinoline, and 3-bromoquinoline, was found to yield the corresponding enantiopure cis-5,6- and -7,8-dihy dro diol metabolites using whole cells of Pseudomonas putida UV4. cis-Dihydroxylation at the 3,4-bond of 2-chloroquino line, 2-methoxyquinoline, and 2-quinolone was also found to yield the heterocyclic cis-dihydrodiol metabolite, (+)-cis-(3S,4S)-3,4-dihydroxy-3,4-dihydro-2-quinolone. Heterocyclic cis-dihydrodiol metabolites, resulting from dihydroxylation at the 5,6- and 3,4-bon

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7

Haddad, Sandra, D. Matthew Eby, and Ellen L. Neidle. "Cloning and Expression of the Benzoate Dioxygenase Genes from Rhodococcus sp. Strain 19070." Applied and Environmental Microbiology 67, no. 6 (2001): 2507–14. http://dx.doi.org/10.1128/aem.67.6.2507-2514.2001.

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ABSTRACT The bopXYZ genes from the gram-positive bacteriumRhodococcus sp. strain 19070 encode a broad-substrate-specific benzoate dioxygenase. Expression of the BopXY terminal oxygenase enabled Escherichia coli to convert benzoate or anthranilate (2-aminobenzoate) to a nonaromaticcis-diol or catechol, respectively. This expression system also rapidly transformed m-toluate (3-methylbenzoate) to an unidentified product. In contrast, 2-chlorobenzoate was not a good substrate. The BopXYZ dioxygenase was homologous to the chromosomally encoded benzoate dioxygenase (BenABC) and the plasmid-encoded t

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8

Tchesnokov, Egor P., Matthias Fellner, Eleni Siakkou, et al. "The Cysteine Dioxygenase Homologue fromPseudomonas aeruginosaIs a 3-Mercaptopropionate Dioxygenase." Journal of Biological Chemistry 290, no. 40 (2015): 24424–37. http://dx.doi.org/10.1074/jbc.m114.635672.

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9

Wallis, M. G., and S. K. Chapman. "3-Methylcatechol 2,3-dioxygenase - a comparison with other non-heme iron dioxygenases." Journal of Inorganic Biochemistry 43, no. 2-3 (1991): 563. http://dx.doi.org/10.1016/0162-0134(91)84538-k.

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10

Riegert, Ulrich, Gesche Heiss, Andrea Elisabeth Kuhm, et al. "Catalytic Properties of the 3-Chlorocatechol-Oxidizing 2,3-Dihydroxybiphenyl 1,2-Dioxygenase from Sphingomonas sp. Strain BN6." Journal of Bacteriology 181, no. 16 (1999): 4812–17. http://dx.doi.org/10.1128/jb.181.16.4812-4817.1999.

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ABSTRACT The 2,3-dihydroxybiphenyl dioxygenase from Sphingomonassp. strain BN6 (BphC1-BN6) differs from most other extradiol dioxygenases by its ability to oxidize 3-chlorocatechol to 3-chloro-2-hydroxymuconic semialdehyde by a distal cleavage mechanism. The turnover of different substrates and the effects of various inhibitors on BphC1-BN6 were compared with those of another 2,3-dihydroxybiphenyl dioxygenase from the same strain (BphC2-BN6) as well as with those of the archetypical catechol 2,3-dioxygenase (C23O-mt2) encoded by the TOL plasmid. Cell extracts containing C23O-mt2 or BphC2-BN6 c

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11

Feng, Yongmei, Hoon Eng Khoo, and Chit Laa Poh. "Purification and Characterization of Gentisate 1,2-Dioxygenases from Pseudomonas alcaligenes NCIB 9867 and Pseudomonas putida NCIB 9869." Applied and Environmental Microbiology 65, no. 3 (1999): 946–50. http://dx.doi.org/10.1128/aem.65.3.946-950.1999.

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ABSTRACT Two 3-hydroxybenzoate-inducible gentisate 1,2-dioxygenases were purified to homogeneity from Pseudomonas alcaligenes NCIB 9867 (P25X) and Pseudomonas putida NCIB 9869 (P35X), respectively. The estimated molecular mass of the purified P25X gentisate 1,2-dioxygenase was 154 kDa, with a subunit mass of 39 kDa. Its structure is deduced to be a tetramer. The pI of this enzyme was established to be 4.8 to 5.0. The subunit mass of P35X gentisate 1,2-dioxygenase was 41 kDa, and this enzyme was deduced to exist as a dimer, with a native molecular mass of about 82 kDa. The pI of P35X gentisate

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12

Potrawfke, Thomas, Jean Armengaud, and Rolf-Michael Wittich. "Chlorocatechols Substituted at Positions 4 and 5 Are Substrates of the Broad-Spectrum Chlorocatechol 1,2-Dioxygenase of Pseudomonas chlororaphis RW71." Journal of Bacteriology 183, no. 3 (2001): 997–1011. http://dx.doi.org/10.1128/jb.183.3.997-1011.2001.

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ABSTRACT The nucleotide sequence of a 10,528-bp region comprising the chlorocatechol pathway gene cluster tetRtetCDEF of the 1,2,3,4-tetrachlorobenzene via the tetrachlorocatechol-mineralizing bacterium Pseudomonas chlororaphis RW71 (T. Potrawfke, K. N. Timmis, and R.-M. Wittich, Appl. Environ. Microbiol. 64:3798–3806, 1998) was analyzed. The chlorocatechol 1,2-dioxygenase gene tetC was cloned and overexpressed inEscherichia coli. The recombinant gene product was purified, and the α,α-homodimeric TetC was characterized. Electron paramagnetic resonance measurements confirmed the presence of a h

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13

Soboleva, Tatiana, and Lisa Berreau. "3-Hydroxyflavones and 3-Hydroxy-4-oxoquinolines as Carbon Monoxide-Releasing Molecules." Molecules 24, no. 7 (2019): 1252. http://dx.doi.org/10.3390/molecules24071252.

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Carbon monoxide-releasing molecules (CORMs) that enable the delivery of controlled amounts of CO are of strong current interest for applications in biological systems. In this review, we examine the various conditions under which CO is released from 3-hydroxyflavones and 3-hydroxy-4-oxoquinolines to advance the understanding of how these molecules, or derivatives thereof, may be developed as CORMs. Enzymatic pathways from quercetin dioxygenases and 3-hydroxy-4-oxoquinoline dioxygenases leading to CO release are examined, along with model systems for these enzymes. Base-catalyzed and non-redox-

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14

Pollmann, Katrin, Victor Wray, and Dietmar H. Pieper. "Chloromethylmuconolactones as Critical Metabolites in the Degradation of Chloromethylcatechols: Recalcitrance of 2-Chlorotoluene." Journal of Bacteriology 187, no. 7 (2005): 2332–40. http://dx.doi.org/10.1128/jb.187.7.2332-2340.2005.

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ABSTRACT To elucidate possible reasons for the recalcitrance of 2-chlorotoluene, the metabolism of chloromethylcatechols, formed after dioxygenation and dehydrogenation by Ralstonia sp. strain PS12 tetrachlorobenzene dioxygenase and chlorobenzene dihydrodiol dehydrogenase, was monitored using chlorocatechol dioxygenases and chloromuconate cycloisomerases partly purified from Ralstonia sp. strain PS12 and Wautersia eutropha JMP134. Two chloromethylcatechols, 3-chloro-4-methylcatechol and 4-chloro-3-methylcatechol, were formed from 2-chlorotoluene. 3-Chloro-4-methylcatechol was transformed into

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15

Pierce, Brad S., Bishnu P. Subedi, Sinjinee Sardar, and Joshua K. Crowell. "The “Gln-Type” Thiol Dioxygenase fromAzotobacter vinelandiiIs a 3-Mercaptopropionic Acid Dioxygenase." Biochemistry 54, no. 51 (2015): 7477–90. http://dx.doi.org/10.1021/acs.biochem.5b00636.

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16

Pan, Zhiqiang, Zhou-Ya Xue, Guo-Fang Li, et al. "DNA Hydroxymethylation by Ten-eleven Translocation Methylcytosine Dioxygenase 1 and 3 Regulates Nociceptive Sensitization in a Chronic Inflammatory Pain Model." Anesthesiology 127, no. 1 (2017): 147–63. http://dx.doi.org/10.1097/aln.0000000000001632.

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Abstract Background Ten-eleven translocation methylcytosine dioxygenase converts 5-methylcytosine in DNA to 5-hydroxymethylcytosine, which plays an important role in gene transcription. Although 5-hydroxymethylcytosine is enriched in mammalian neurons, its regulatory function in nociceptive information processing is unknown. Methods The global levels of 5-hydroxymethylcytosine and ten-eleven translocation methylcytosine dioxygenase were measured in spinal cords in mice treated with complete Freund’s adjuvant. Immunoblotting, immunohistochemistry, and behavioral tests were used to explore the d

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17

Kudo, Yoshiki, and Jun Sugimoto. "The Role of the Placental Enzyme Indoleamine 2,3-Dioxygenase in Normal and Abnormal Human Pregnancy." International Journal of Molecular Sciences 25, no. 8 (2024): 4577. http://dx.doi.org/10.3390/ijms25084577.

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The biologically significant phenomenon that the fetus can survive immune attacks from the mother has been demonstrated in mammals. The survival mechanism depends on the fetus and placenta actively defending themselves against attacks by maternal T cells, achieved through the localized depletion of the amino acid L-tryptophan by an enzyme called indoleamine 2,3-dioxygenase. These findings were entirely unexpected and pose important questions regarding diseases related to human pregnancy and their prevention during human pregnancy. Specifically, the role of this mechanism, as discovered in mice

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18

Kasai, Daisuke, Eiji Masai, Keisuke Miyauchi, Yoshihiro Katayama, and Masao Fukuda. "Characterization of the Gallate Dioxygenase Gene: Three Distinct Ring Cleavage Dioxygenases Are Involved in Syringate Degradation by Sphingomonas paucimobilis SYK-6." Journal of Bacteriology 187, no. 15 (2005): 5067–74. http://dx.doi.org/10.1128/jb.187.15.5067-5074.2005.

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ABSTRACT Sphingomonas paucimobilis SYK-6 converts vanillate and syringate to protocatechuate (PCA) and 3-O-methylgallate (3MGA) in reactions with the tetrahydrofolate-dependent O-demethylases LigM and DesA, respectively. PCA is further degraded via the PCA 4,5-cleavage pathway, whereas 3MGA is metabolized via three distinct pathways in which PCA 4,5-dioxygenase (LigAB), 3MGA 3,4-dioxygenase (DesZ), and 3MGA O-demethylase (LigM) are involved. In the 3MGA O-demethylation pathway, LigM converts 3MGA to gallate, and the resulting gallate appears to be degraded by a dioxygenase other than LigAB or

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19

Müller, Christine, Franziska S. Birmes, Christian Rückert, Jörn Kalinowski, and Susanne Fetzner. "Rhodococcus erythropolis BG43 Genes Mediating Pseudomonas aeruginosa Quinolone Signal Degradation and Virulence Factor Attenuation." Applied and Environmental Microbiology 81, no. 22 (2015): 7720–29. http://dx.doi.org/10.1128/aem.02145-15.

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ABSTRACTRhodococcus erythropolisBG43 is able to degrade thePseudomonas aeruginosaquorum sensing signal molecules PQS (Pseudomonasquinolone signal) [2-heptyl-3-hydroxy-4(1H)-quinolone] and HHQ [2-heptyl-4(1H)-quinolone] to anthranilic acid. Based on the hypothesis that degradation of HHQ might involve hydroxylation to PQS followed by dioxygenolytic cleavage of the heterocyclic ring and hydrolysis of the resultingN-octanoylanthranilate, the genome was searched for corresponding candidate genes. Two gene clusters,aqdA1B1C1andaqdA2B2C2, each predicted to code for a hydrolase, a flavin monooxygenas

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20

Zhang, Y., K. L. Colabroy, T. P. Begley, and S. E. Ealick. "Structural studies on 3-hydroxyanthranilate-3,4-dioxygenase." Acta Crystallographica Section A Foundations of Crystallography 61, a1 (2005): c205. http://dx.doi.org/10.1107/s0108767305091282.

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21

Zheng, Yuxiang, and Alan R. Brash. "Dioxygenase Activity of Epidermal Lipoxygenase-3 Unveiled." Journal of Biological Chemistry 285, no. 51 (2010): 39866–75. http://dx.doi.org/10.1074/jbc.m110.155374.

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22

STRACHAN, Philip D., Andrew A. FREER, and Charles A. FEWSON. "Purification and characterization of catechol 1,2-dioxygenase from Rhodococcus rhodochrous NCIMB 13259 and cloning and sequencing of its catA gene." Biochemical Journal 333, no. 3 (1998): 741–47. http://dx.doi.org/10.1042/bj3330741.

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A method was developed for the purification of catechol 1,2-dioxygenase from Rhodococcus rhodochrous NCIMB 13259 that had been grown in the presence of benzyl alcohol. The enzyme has very similar apparent Km (1–2 µM) and Vmax (13–19 units/mg of protein) values for the intradiol cleavage of catechol, 3-methylcatechol and 4-methylcatechol and it is optimally active at pH 9. Cross-linking studies indicate that the enzyme is a homodimer. It contains 0.6 atoms of Fe per subunit. The enzyme was crystallized with 15% (w/v) poly(ethylene glycol) 4000/0.33 M CaCl2/25 mM Tris (pH 7.5) by using a microse

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23

Resnick, Sol M., Daniel S. Torok, and David T. Gibson. "Oxidation of carbazole to 3-hydroxycarbazole by naphthalene 1,2-dioxygenase and biphenyl 2,3-dioxygenase." FEMS Microbiology Letters 113, no. 3 (1993): 297–302. http://dx.doi.org/10.1111/j.1574-6968.1993.tb06530.x.

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24

Ge, Yong, and Lindsay D. Eltis. "Characterization of Hybrid Toluate and Benzoate Dioxygenases." Journal of Bacteriology 185, no. 18 (2003): 5333–41. http://dx.doi.org/10.1128/jb.185.18.5333-5341.2003.

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ABSTRACT Toluate dioxygenase of Pseudomonas putida mt-2 (TADOmt2) and benzoate dioxygenase of Acinetobacter calcoaceticus ADP1 (BADOADP1) catalyze the 1,2-dihydroxylation of different ranges of benzoates. The catalytic component of these enzymes is an oxygenase consisting of two subunits. To investigate the structural determinants of substrate specificity in these ring-hydroxylating dioxygenases, hybrid oxygenases consisting of the α subunit of one enzyme and the β subunit of the other were prepared, and their respective specificities were compared to those of the parent enzymes. Reconstituted

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25

Hedlund, Brian P., Allison D. Geiselbrecht, Timothy J. Bair, and James T. Staley. "Polycyclic Aromatic Hydrocarbon Degradation by a New Marine Bacterium, Neptunomonas naphthovorans gen. nov., sp. nov." Applied and Environmental Microbiology 65, no. 1 (1999): 251–59. http://dx.doi.org/10.1128/aem.65.1.251-259.1999.

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ABSTRACT Two strains of bacteria were isolated from creosote-contaminated Puget Sound sediment based on their ability to utilize naphthalene as a sole carbon and energy source. When incubated with a polycyclic aromatic hydrocarbon (PAH) compound in artificial seawater, each strain also degraded 2-methylnaphthalene and 1-methylnaphthalene; in addition, one strain, NAG-2N-113, degraded 2,6-dimethylnaphthalene and phenanthrene. Acenaphthene was not degraded when it was used as a sole carbon source but was degraded by both strains when it was incubated with a mixture of seven other PAHs. Degenerat

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26

Bui, Vu P., Minh Nguyen, Jeff Hansen, John Baker, and Tomas Hudlicky. "Enzymatic oxidation of cyclopropylbenzene: structures of new metabolites and possible mechanistic implications." Canadian Journal of Chemistry 80, no. 6 (2002): 708–13. http://dx.doi.org/10.1139/v02-098.

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Cyclopropylbenzene was subjected to whole-cell fermentation with either Escherichia coli JM109 (pDTG601) or E. coli JM109 (pDTG602), expressing toluene dioxygenase and toluene dioxygenase dihydrodiol dehydrogenase enzymes, respectively. The corresponding metabolites, 3-cyclopropylcyclohexa-3,5-diene-1,2-diol (3) and 3-cyclopropylbenzene-1,2-diol (5) have been isolated in yields of 2.5 and 1 g L1, respectively. The absolute stereochemistry correlation for 3 is provided, along with a preliminary discussion of its potential in asymmetric synthesis. Possible mechanistic implications are indicat

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27

Werwath, Jörn, Hans-Adolf Arfmann, Dietmar H. Pieper, Kenneth N. Timmis, and Rolf-Michael Wittich. "Biochemical and Genetic Characterization of a Gentisate 1,2-Dioxygenase from Sphingomonas sp. Strain RW5." Journal of Bacteriology 180, no. 16 (1998): 4171–76. http://dx.doi.org/10.1128/jb.180.16.4171-4176.1998.

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ABSTRACT A 4,103-bp long DNA fragment containing the structural gene of a gentisate 1,2-dioxygenase (EC 1.13.11.4 ), gtdA, fromSphingomonas sp. strain RW5 was cloned and sequenced. ThegtdA gene encodes a 350-amino-acid polypeptide with a predicted size of 38.85 kDa. Comparison of the gtdA gene product with protein sequences in databases, including those of intradiol or extradiol ring-cleaving dioxygenases, revealed no significant homology except for a low similarity (27%) to the 1-hydroxy-2-naphthoate dioxygenase (phdI) of the phenanthrene degradation in Nocardioides sp. strain KP7 (T. Iwabuch

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28

VELDHUIZEN, Edwin J. A., Frédéric H. VAILLANCOURT, Cheryl J. WHITING, et al. "Steady-state kinetics and inhibition of anaerobically purified human homogentisate 1,2-dioxygenase." Biochemical Journal 386, no. 2 (2005): 305–14. http://dx.doi.org/10.1042/bj20041370.

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HGO (homogentisate 1,2-dioxygenase; EC 1.13.11.5) catalyses the O2-dependent cleavage of HGA (homogentisate) to maleylacetoacetate in the catabolism of tyrosine. Anaerobic purification of heterologously expressed Fe(II)-containing human HGO yielded an enzyme preparation with a specific activity of 28.3± 0.6 μmol·min−1·mg−1 (20 mM Mes, 80 mM NaCl, pH 6.2, 25 °C), which is almost twice that of the most active preparation described to date. Moreover, the addition of reducing agents or other additives did not increase the specific activity, in contrast with previous reports. The apparent specifici

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29

HEYES, Melvyn P., Cai Y. CHEN, Eugene O. MAJOR, and Kuniaki SAITO. "Different kynurenine pathway enzymes limit quinolinic acid formation by various human cell types." Biochemical Journal 326, no. 2 (1997): 351–56. http://dx.doi.org/10.1042/bj3260351.

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Substantial increases in the tryptophan–kynurenine pathway metabolites, L-kynurenine and the neurotoxin quinolinic acid, occur in human brain, blood and systemic tissues during immune activation. Studies in vitrohave shown that not all human cells are capable of synthesizing quinolinate. To investigate further the mechanisms that limit L-kynurenine and quinolinate production, the activities of kynurenine pathway enzymes and the ability of different human cells to convert pathway intermediates into quinolinate were compared. Stimulation with interferon γ substantially increased indoleamine 2,3-

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30

Suzuki, T., and K. Yokouchi. "A myoglobin evolved from indoleamine 2, 3-dioxygenase." Seibutsu Butsuri 41, supplement (2001): S22. http://dx.doi.org/10.2142/biophys.41.s22_3.

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31

Đilović, Ivica, Francesca Gliubich, Giorgio Malpeli, Giuseppe Zanotti, and Dubravka Matković-Čalogović. "Crystal structure of bovine 3-hydroxyanthranilate 3,4-dioxygenase." Biopolymers 91, no. 12 (2009): 1189–95. http://dx.doi.org/10.1002/bip.21167.

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32

Wang, Chenghong, Qing Chen, Rui Wang, et al. "A Novel Angular Dioxygenase Gene Cluster Encoding 3-Phenoxybenzoate 1′,2′-Dioxygenase in Sphingobium wenxiniae JZ-1." Applied and Environmental Microbiology 80, no. 13 (2014): 3811–18. http://dx.doi.org/10.1128/aem.00208-14.

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ABSTRACTSphingobium wenxiniaeJZ-1 utilizes a wide range of pyrethroids and their metabolic product, 3-phenoxybenzoate, as sources of carbon and energy. A mutant JZ-1 strain, MJZ-1, defective in the degradation of 3-phenoxybenzoate was obtained by successive streaking on LB agar. Comparison of the draft genomes of strains JZ-1 and MJZ-1 revealed that a 29,366-bp DNA fragment containing a putative angular dioxygenase gene cluster (pbaA1A2B) is missing in strain MJZ-1. PbaA1, PbaA2, and PbaB share 65%, 52%, and 10% identity with the corresponding α and β subunits and the ferredoxin component of d

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33

Salter, M., and C. I. Pogson. "The role of tryptophan 2,3-dioxygenase in the hormonal control of tryptophan metabolism in isolated rat liver cells. Effects of glucocorticoids and experimental diabetes." Biochemical Journal 229, no. 2 (1985): 499–504. http://dx.doi.org/10.1042/bj2290499.

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The metabolism of L-tryptophan by isolated liver cells prepared from control, adrenalectomized, glucocorticoid-treated, acute-diabetic, chronic-diabetic and insulin-treated chronic-diabetic rats was studied. Liver cells from adrenalectomized rats metabolized tryptophan at rates comparable with the minimum diurnal rates of controls, but different from rates determined for cells from control rats 4h later. Administration of dexamethasone phosphate increased the activity of tryptophan 2,3-dioxygenase (EC 1.13.11.11) 7-8-fold, and the flux through the kynurenine pathway 3-4-fold, in cells from bot

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34

Emelyanova, Elena V., Sudarsu V. Ramanaiah, Nataliya V. Prisyazhnaya, et al. "The Contribution of Actinobacteria to the Degradation of Chlorinated Compounds: Variations in the Activity of Key Degradation Enzymes." Microorganisms 11, no. 1 (2023): 141. http://dx.doi.org/10.3390/microorganisms11010141.

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Bacteria make a huge contribution to the purification of the environment from toxic stable pollutants of anthropogenic and natural origin due to the diversity of their enzyme systems. For example, the ability to decompose 3-chlorobenzoate (3CBA) by the four representative genera of Actinobacteria, such as Rhodococcus, Gordonia, Microbacterium, and Arthrobacter, was studied. In most cases, the formation of 4-chlorocatechol as the only key intermediate during the decomposition of 3CBA was observed. However, Rhodococcus opacus strain 1CP was an exception, whose cells decomposed 3CBA via both 3-ch

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Miyazawa, Daisuke, Gouri Mukerjee-Dhar, Minoru Shimura, Takashi Hatta, and Kazuhide Kimbara. "Genes for Mn(II)-dependent NahC and Fe(II)-dependent NahH located in close proximity in the thermophilic naphthalene and PCB degrader, Bacillus sp. JF8: cloning and characterization." Microbiology 150, no. 4 (2004): 993–1004. http://dx.doi.org/10.1099/mic.0.26858-0.

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A 10 kb DNA fragment was isolated using a DNA probe derived from the N-terminal amino acid sequence of the extradiol dioxygenase purified from naphthalene-grown Bacillus sp. JF8, a thermophilic naphthalene and polychlorinated biphenyl degrader. The cloned DNA fragment had six open reading frames, designated nahHLOMmocBnahC based on sequence homology, of which the products NahH_JF8 and NahC_JF8 were extradiol dioxygenases. Although NahC_JF8 and NahH_JF8 exhibit low homology to known extradiol dioxygenases, the active-site residues and metal ion ligands are conserved. The presence of Mn(II) in c

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36

Jin, Xin-Yu, Kui Wang, Pan-Xiu Zhang, and Fei Ye. "Synthesis, Characterization, and Molecular Docking Studies of 3-Hydroxy-2-(1-methyl-3- (trifluoromethyl)-1H-pyrazole-4-carbonyl)cyclohex-2-en-1-ones." INDIAN JOURNAL OF HETEROCYCLIC CHEMISTRY 34, no. 02 (2024): 141. http://dx.doi.org/10.59467/ijhc.2024.34.141.

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Three new 3-hydroxy-2-(1-methyl-3-(trifluoromethyl)-1H-pyrazole-4-carbonyl)cyclohex-2-en-1-ones (4a-c) were synthesized using aromatic formic acid as starting material. The structures of the compounds were confirmed by spectral (infrared, proton nuclear magnetic resonance, carbon-13 nuclear magnetic resonance, and HRMS) data. The molecular docking studies of the compounds were carried out to predict the possible 4-hydroxyphenylpyruvate dioxygenase (HPPD) inhibitory activity. All the compounds exhibited activity in HPPD inhibitory.. KEYWORDS :4-Hydroxyphenylpyruvate dioxygenase inhibitory, Mole

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Fischer, Frank, Stefan Künne та Susanne Fetzner. "Bacterial 2,4-Dioxygenases: New Members of the α/β Hydrolase-Fold Superfamily of Enzymes Functionally Related to Serine Hydrolases". Journal of Bacteriology 181, № 18 (1999): 5725–33. http://dx.doi.org/10.1128/jb.181.18.5725-5733.1999.

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ABSTRACT 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase (Qdo) fromPseudomonas putida 33/1 and 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase (Hod) fromArthrobacter ilicis Rü61a catalyze an N-heterocyclic-ring cleavage reaction, generatingN-formylanthranilate and N-acetylanthranilate, respectively, and carbon monoxide. Amino acid sequence comparisons between Qdo, Hod, and a number of proteins belonging to the α/β hydrolase-fold superfamily of enzymes and analysis of the similarity between the predicted secondary structures of the 2,4-dioxygenases and the known secondary structure of haloalkane deha

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38

Kasai, Daisuke, Eiji Masai, Keisuke Miyauchi, Yoshihiro Katayama, and Masao Fukuda. "Characterization of the 3-O-Methylgallate Dioxygenase Gene and Evidence of Multiple 3-O-Methylgallate Catabolic Pathways in Sphingomonas paucimobilis SYK-6." Journal of Bacteriology 186, no. 15 (2004): 4951–59. http://dx.doi.org/10.1128/jb.186.15.4951-4959.2004.

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ABSTRACT Sphingomonas paucimobilis SYK-6 is able to grow on various lignin-derived biaryls as the sole source of carbon and energy. These compounds are degraded to vanillate and syringate by the unique and specific enzymes in this strain. Vanillate and syringate are converted to protocatechuate (PCA) and 3-O-methylgallate (3MGA), respectively, by the tetrahydrofolate-dependent O-demethylases. Previous studies have suggested that these compounds are further degraded via the PCA 4,5-cleavage pathway. However, our subsequent analysis of the ligB insertion mutant, which encodes the β subunit of PC

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Bubinas, Audrius, Gražina Giedraitytė, Lilija Kalėdienė, Ona Nivinskiene, and Rita Butkiene. "Degradation of naphthalene by thermophilic bacteria via a pathway, through protocatechuic acid." Open Life Sciences 3, no. 1 (2008): 61–68. http://dx.doi.org/10.2478/s11535-007-0042-x.

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AbstractA number of thermophilic bacteria capable of utilizing naphthalene as a sole source of carbon were isolated from a high-temperature oilfield in Lithuania. These isolates were able to utilize several other aromatic compounds, such as anthracene, benzene, phenol, benzene-1, 3-diol, protocatechuic acid as well. Thermophilic isolate G27 ascribed to Geobacillus genus was found to have a high aromatic compound degrading capacity. Spectrophotometric determination of enzyme activities in cell-free extracts revealed that the last aromatic ring fission enzyme in naphthalene biotransformation by

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Zeng, Dao-Bing, and Shi-Chun Lu. "Function of indoleamine 2, 3-dioxygenase in viral infection." World Chinese Journal of Digestology 16, no. 8 (2008): 879. http://dx.doi.org/10.11569/wcjd.v16.i8.879.

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Jia, Lining, Puxun Tian, and Chenguang Ding. "Immunoregulatory effects of indoleamine 2, 3-dioxygenase in transplantation." Transplant Immunology 21, no. 1 (2009): 18–22. http://dx.doi.org/10.1016/j.trim.2009.01.004.

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42

Su, Chang, Peng Zhang, Jianwen Liu, and Yiou Cao. "Erianin inhibits indoleamine 2, 3-dioxygenase –induced tumor angiogenesis." Biomedicine & Pharmacotherapy 88 (April 2017): 521–28. http://dx.doi.org/10.1016/j.biopha.2017.01.090.

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Liu, Jiangxin, Jian Ren, Kun Yang, Shuang Chen, Xinni Yang, and Qin-Shi Zhao. "Discovery and biological evaluation of tanshinone derivatives as potent dual inhibitors of indoleamine 2, 3-dioxygenase 1 and tryptophan 2, 3-dioxygenase." European Journal of Medicinal Chemistry 235 (May 2022): 114294. http://dx.doi.org/10.1016/j.ejmech.2022.114294.

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44

Sophi, R., and Rayan Faisal. "Distribution of biphenyl degraders in soil samples in Mosul-Iraq." UNEC journal of engineering and applied sciences 3, no. 1 (2023): 21–32. http://dx.doi.org/10.61640/ujeas.2023.1203.

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This work aimed to study the distribution of biphenyl degrading isolates from different soils in Nineveh governorate. Fifty five soil samples were collected from reeds soil, sandy soil, landfill soil, oil refinery soil, agricultural soil, sulfur station soil, garden soil, and sewage contaminated soil. Nine isolates were diagnosed based on their cultural characteristics and 16S rRNA gene sequence. Five isolates belonged to Rhodococcus, and the other four were diagnosed as Extensimonas perlucida, Achromobacter sp., Microbacterium barkeri, and Pseudomonas luteola. The sequences were submitted to

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Hintner, Jan-Peter, Christa Lechner, Ulrich Riegert, et al. "Direct Ring Fission of Salicylate by a Salicylate 1,2-Dioxygenase Activity from Pseudaminobacter salicylatoxidans." Journal of Bacteriology 183, no. 23 (2001): 6936–42. http://dx.doi.org/10.1128/jb.183.23.6936-6942.2001.

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ABSTRACT In cell extracts of Pseudaminobacter salicylatoxidans strain BN12, an enzymatic activity was detected which converted salicylate in an oxygen-dependent but NAD(P)H-independent reaction to a product with an absorbance maximum at 283 nm. This metabolite was isolated, purified, and identified by mass spectrometry and 1H and 13C nuclear magnetic resonance spectroscopy as 2-oxohepta-3,5-dienedioic acid. This metabolite could be formed only by direct ring fission of salicylate by a 1,2-dioxygenase reaction. Cell extracts from P. salicylatoxidans also oxidized 5-aminosalicylate, 3-, 4-, and

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46

Bruland, Nadine, Jan Hendrik Wübbeler, and Alexander Steinbüchel. "3-Mercaptopropionate Dioxygenase, a Cysteine Dioxygenase Homologue, Catalyzes the Initial Step of 3-Mercaptopropionate Catabolism in the 3,3-Thiodipropionic Acid-degrading BacteriumVariovorax paradoxus." Journal of Biological Chemistry 284, no. 1 (2008): 660–72. http://dx.doi.org/10.1074/jbc.m806762200.

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47

Suenaga, Hikaru, Takahito Watanabe, Mika Sato, Ngadiman, and Kensuke Furukawa. "Alteration of Regiospecificity in Biphenyl Dioxygenase by Active-Site Engineering." Journal of Bacteriology 184, no. 13 (2002): 3682–88. http://dx.doi.org/10.1128/jb.184.13.3682-3688.2002.

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ABSTRACT Biphenyl dioxygenase (Bph Dox) is responsible for the initial dioxygenation step during the metabolism of biphenyl. The large subunit (BphA1) of Bph Dox plays a crucial role in the determination of the substrate specificity of biphenyl-related compounds, including polychlorinated biphenyls (PCBs). Based on crystallographic analyses of naphthalene dioxygenase (B. Kauppi, K. Lee, E. Carredano, R. E. Parales, D. T. Gibson, H. Eklund, and S. Ramaswamy, Structure 6:571-586, 1998), we developed a three-dimensional model of KF707 BphA1 of Pseudomonas pseudoalcaligenes KF707. Based on structu

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48

Wang, Yifan, Kathy Fange Liu, Yu Yang, Ian Davis, and Aimin Liu. "Observing 3-hydroxyanthranilate-3,4-dioxygenase in action through a crystalline lens." Proceedings of the National Academy of Sciences 117, no. 33 (2020): 19720–30. http://dx.doi.org/10.1073/pnas.2005327117.

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The synthesis of quinolinic acid from tryptophan is a critical step in the de novo biosynthesis of nicotinamide adenine dinucleotide (NAD+) in mammals. Herein, the nonheme iron-based 3-hydroxyanthranilate-3,4-dioxygenase responsible for quinolinic acid production was studied by performing time-resolvedin crystalloreactions monitored by UV-vis microspectroscopy, electron paramagnetic resonance (EPR) spectroscopy, and X-ray crystallography. Seven catalytic intermediates were kinetically and structurally resolved in the crystalline state, and each accompanies protein conformational changes at the

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Joseph, P., S. N. Srinivasan, and A. P. Kulkarni. "Purification and partial characterization of lipoxygenase with dual catalytic activities from human term placenta." Biochemical Journal 293, no. 1 (1993): 83–91. http://dx.doi.org/10.1042/bj2930083.

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Lipoxygenase possessing dual catalytic activities, i.e. dioxygenase and hydroperoxidase, was purified from the cytosols of term placentas from non-smoking women. Concanavalin A affinity chromatography followed by phenyl-Sepharose CL-4B chromatography resulted in the separation of one hydrophobic and one non-hydrophobic isoenzyme. The concanavalin A-purified enzyme was used in all subsequent experiments. The dioxygenase activity of the enzyme exhibited a Vmax. of 204.37 +/- 17.66 nmol/min per mg of protein and a Km of 0.79 mM for linoleic acid. The involvement of dioxygen in enzymic linoleic ac

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Fortin, Pascal D., Andy T. F. Lo, María-Amparo Haro, Stefan R. Kaschabek, Walter Reineke, and Lindsay D. Eltis. "Evolutionarily Divergent Extradiol Dioxygenases Possess Higher Specificities for Polychlorinated Biphenyl Metabolites." Journal of Bacteriology 187, no. 2 (2005): 415–21. http://dx.doi.org/10.1128/jb.187.2.415-421.2005.

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ABSTRACT The reactivities of four evolutionarily divergent extradiol dioxygenases towards mono-, di-, and trichlorinated (triCl) 2,3-dihydroxybiphenyls (DHBs) were investigated: 2,3-dihydroxybiphenyl dioxygenase (EC 1.13.11.39) from Burkholderia sp. strain LB400 (DHBDLB400), DHBDP6-I and DHBDP6-III from Rhodococcus globerulus P6, and 2,2′,3-trihydroxybiphenyl dioxygenase from Sphingomonas sp. strain RW1 (THBDRW1). The specificity of each isozyme for particular DHBs differed by up to 3 orders of magnitude. Interestingly, the K m app values of each isozyme for the tested polychlorinated DHBs wer

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