Oxepin-CoA hydrolase

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Oxepin-CoA hydrolase
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EC no. 3.7.1.16
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Oxepin-CoA hydrolase (EC 3.7.1.16, paaZ (gene)) is an enzyme with systematic name 2-oxepin-2(3H)-ylideneacetyl-CoA hydrolyase. [1] [2] [3] [4] This enzyme catalyses the following chemical reaction

2-oxepin-2(3H)-ylideneacetyl-CoA + H2O 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde

The enzyme is present in bacteria Escherichia coli .

Related Research Articles

Propionyl-CoA is a coenzyme A derivative of propionic acid. It is composed of a 24 total carbon chain and its production and metabolic fate depend on which organism it is present in. Several different pathways can lead to its production, such as through the catabolism of specific amino acids or the oxidation of odd-chain fatty acids. It later can be broken down by propionyl-CoA carboxylase or through the methylcitrate cycle. In different organisms, however, propionyl-CoA can be sequestered into controlled regions, to alleviate its potential toxicity through accumulation. Genetic deficiencies regarding the production and breakdown of propionyl-CoA also have great clinical and human significance.

In enzymology, a 3-phenylpropanoate dioxygenase (EC 1.14.12.19) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">4-Hydroxyphenylacetate 3-monooxygenase</span> Class of enzymes

4-hydroxyphenylacetate 3-monooxygenase (EC 1.14.14.9) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">N-acetylglucosamine-6-phosphate deacetylase</span>

In enzymology, N-acetylglucosamine-6-phosphate deacetylase (EC 3.5.1.25), also known as GlcNAc-6-phosphate deacetylase or NagA, is an enzyme that catalyzes the deacetylation of N-acetylglucosamine-6-phosphate (GlcNAc-6-P) to glucosamine-6-phosphate (GlcN-6-P):

In enzymology, a N-succinylarginine dihydrolase (EC 3.5.3.23) is an enzyme that catalyzes the chemical reaction

In enzymology, a succinylglutamate desuccinylase (EC 3.5.1.96) is an enzyme that catalyzes the chemical reaction

In enzymology, a [acyl-carrier-protein] S-malonyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, an arginine N-succinyltransferase (EC 2.3.1.109) is an enzyme that catalyzes the chemical reaction

4-Hydroxy-3-methylbut-2-enyl diphosphate reductase (EC 1.17.1.2, isopentenyl-diphosphate:NADP+ oxidoreductase, LytB, (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase, HMBPP reductase, IspH, LytB/IspH) is an enzyme in the non-mevalonate pathway. It acts upon (E)-4-Hydroxy-3-methyl-but-2-enyl pyrophosphate (or "HMB-PP").

3,4-Dehydroadipyl-CoA semialdehyde dehydrogenase (NADP+) (EC 1.2.1.77, BoxD, 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase) is an enzyme with systematic name 3,4-didehydroadipyl-CoA semialdehyde:NADP+ oxidoreductase. This enzyme catalyses the following chemical reaction

3-(3-hydroxyphenyl)propanoate hydroxylase (EC 1.14.13.127, mhpA (gene)) is an enzyme with systematic name 3-(3-hydroxyphenyl)propanoate,NADH:oxygen oxidoreductase (2-hydroxylating). This enzyme catalyses the following chemical reaction

Phenylacetyl-CoA 1,2-epoxidase (EC 1.14.13.149, ring 1,2-phenylacetyl-CoA epoxidase, phenylacetyl-CoA monooxygenase, PaaAC, PaaABC(D)E) is an enzyme with systematic name phenylacetyl-CoA:oxygen oxidoreductase (1,2-epoxidizing). This enzyme catalyses the following chemical reaction

3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase (EC 1.17.1.7, paaZ (gene)) is an enzyme with systematic name 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde:NADP+ oxidoreductase. This enzyme catalyses the following chemical reaction

Putrescine aminotransferase (EC 2.6.1.82, putrescine-alpha-ketoglutarate transaminase, YgjG, putrescine:alpha-ketoglutarate aminotransferase, PAT, putrescine:2-oxoglutarate aminotransferase, putrescine transaminase) is an enzyme with systematic name butane-1,4-diamine:2-oxoglutarate aminotransferase. This enzyme catalyses the following chemical reaction

Propionate kinase is an enzyme with systematic name ATP:propanoate phosphotransferase. This enzyme catalyses the following chemical reaction

Signal peptidase I is an enzyme. This enzyme catalyses the following chemical reaction

2-hydroxy-6-oxonona-2,4-dienedioate hydrolase (EC 3.7.1.14, mhpC (gene)) is an enzyme with systematic name (2Z,4E)-2-hydroxy-6-oxona-2,4-dienedioate succinylhydrolase. This enzyme catalyses the following chemical reaction:

  1. (2Z,4E)-2-hydroxy-6-oxonona-2,4-diene-1,9-dioate + H2O (2Z)-2-hydroxypenta-2,4-dienoate + succinate
  2. (2Z,4E,7E)-2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioate + H2O (2Z)-2-hydroxypenta-2,4-dienoate + fumarate

2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA isomerase is an enzyme with systematic name 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA isomerase. This enzyme catalyses the following chemical reaction

Azoarcus evansii is a species of bacteria. Its type strain is KB 740T.

Phenylacetyl-CoA (C29H42N7O17P3S) is a form of acetyl-CoA formed from the condensation of the thiol group from coenzyme A with the carboxyl group of phenylacetic acid.

References

  1. ↑ Ferrández A, Miñambres B, García B, Olivera ER, Luengo JM, García JL, Díaz E (October 1998). "Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway". The Journal of Biological Chemistry. 273 (40): 25974–86. doi: 10.1074/jbc.273.40.25974 . PMID   9748275.
  2. ↑ Park SJ, Lee SY (September 2003). "Identification and characterization of a new enoyl coenzyme A hydratase involved in biosynthesis of medium-chain-length polyhydroxyalkanoates in recombinant Escherichia coli" (PDF). Journal of Bacteriology. 185 (18): 5391–7. doi:10.1128/jb.185.18.5391-5397.2003. PMC   193764 . PMID   12949091.
  3. ↑ Ismail W, El-Said Mohamed M, Wanner BL, Datsenko KA, Eisenreich W, Rohdich F, Bacher A, Fuchs G (July 2003). "Functional genomics by NMR spectroscopy. Phenylacetate catabolism in Escherichia coli". European Journal of Biochemistry. 270 (14): 3047–54. doi: 10.1046/j.1432-1033.2003.03683.x . PMID   12846838.
  4. ↑ Teufel R, Mascaraque V, Ismail W, Voss M, Perera J, Eisenreich W, Haehnel W, Fuchs G (August 2010). "Bacterial phenylalanine and phenylacetate catabolic pathway revealed". Proceedings of the National Academy of Sciences of the United States of America. 107 (32): 14390–5. doi: 10.1073/pnas.1005399107 . PMC   2922514 . PMID   20660314.
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