Biology:Phenylacetyl-CoA 1,2-epoxidase
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Short description: Class of enzymes
| Phenylacetyl-CoA 1,2-epoxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.14.13.149 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
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).[1][2][3] This enzyme catalyses the following chemical reaction
- phenylacetyl-CoA + NADPH + H+ + O2 [math]\displaystyle{ \rightleftharpoons }[/math] 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA + NADP+ + H2O
Phenylacetyl-CoA 1,2-epoxidase participates in catabolism of phenylacetate in Escherichia coli and Pseudomonas putida.
References
- ↑ "Bacterial phenylalanine and phenylacetate catabolic pathway revealed". Proceedings of the National Academy of Sciences of the United States of America 107 (32): 14390–5. August 2010. doi:10.1073/pnas.1005399107. PMID 20660314.
- ↑ "Crystallization and preliminary X-ray analysis of PaaAC, the main component of the hydroxylase of the Escherichia coli phenylacetyl-coenzyme A oxygenase complex". Acta Crystallographica Section F 66 (Pt 9): 1045–9. September 2010. doi:10.1107/S174430911002748X. PMID 20823522.
- ↑ "Structural and functional studies of the Escherichia coli phenylacetyl-CoA monooxygenase complex". The Journal of Biological Chemistry 286 (12): 10735–43. March 2011. doi:10.1074/jbc.M110.194423. PMID 21247899.
External links
- Phenylacetyl-CoA+1,2-epoxidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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