Phenylacetyl-CoA 1,2-epoxidase
| 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 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
- ↑ Teufel, R.; Mascaraque, V.; Ismail, W.; Voss, M.; Perera, J.; Eisenreich, W.; Haehnel, W.; Fuchs, G. (2010). "Bacterial phenylalanine and phenylacetate catabolic pathway revealed". Proc. Natl. Acad. Sci. USA. 107: 14390–14395. doi:10.1073/pnas.1005399107. PMC 2922514
. PMID 20660314. - ↑ Grishin, A.M.; Ajamian, E.; Zhang, L.; Cygler, M. (2010). "Crystallization and preliminary X-ray analysis of PaaAC, the main component of the hydroxylase of the Escherichia coli phenylacetyl-coenzyme A oxygenase complex". Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66 (Pt 9): 1045–1049. doi:10.1107/S174430911002748X. PMC 2935223. PMID 20823522.
- ↑ Grishin, A.M.; Ajamian, E.; Tao, L.; Zhang, L.; Menard, R.; Cygler, M. (2011). "Structural and functional studies of the Escherichia coli phenylacetyl-CoA monooxygenase complex". J. Biol. Chem. 286 (12): 10735–10743. doi:10.1074/jbc.M110.194423. PMC 3060524. PMID 21247899.
External links
- Phenylacetyl-CoA 1,2-epoxidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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