Fenilacetil-KoA dehidrogenaza
Izgled
Fenilacetil-KoA dehidrogenaza | |||||||||
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Identifikatori | |||||||||
EC broj | 1.17.5.1 | ||||||||
CAS broj | 210756-43-7 | ||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Fenilacetil-KoA dehidrogenaza (EC 1.17.5.1, fenilacetil-KoA:akceptor oksidoreduktaza) je enzim sa sistematskim imenom fenilacetil-KoA:hinon oksidoreduktaza.[1][2] Ovaj enzim katalizuje sledeću hemijsku reakciju:
Enzim iz Thauera aromatičnaa je vezan za membranu i sadrži molibden-gvožđe-sumporni motiv. Enzim je specifičan za fenilacetil-KoA kao supstrat.
- ↑ Rhee, S.K. and Fuchs, G. (1999). „Phenylacetyl-CoA:acceptor oxidoreductase, a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica”. Eur. J. Biochem. 262: 507-515. PMID 10336636.
- ↑ Schneider, S. and Fuchs, G. (1998). „Phenylacetyl-CoA:acceptor oxidoreductase, a new α-oxidizing enzyme that produces phenylglyoxylate. Assay, membrane localization, and differential production in Thauera aromatica”. Arch. Microbiol. 169: 509-516. PMID 9575237.
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