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1. Oxidoreductases

1.3 Acting on the CH-CH group of donors

1.3.8 With a flavin as acceptor

ID:

1.3.8.8

Description:

Long-chain-acyl-CoA dehydrogenase.

Prosite:

PDOC00070;

PDB:

PDB	Scop

Cath:

1.10.540.10; 1.20.140.10; 2.40.110.10;

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UniProtKB Enzyme Link:	UniProtKB 1.3.8.8
BRENDA Enzyme Link:	BRENDA 1.3.8.8
KEGG Enzyme Link:	KEGG1.3.8.8
BioCyc Enzyme Link:	BioCyc 1.3.8.8
ExPASy Enzyme Link:	ExPASy1.3.8.8
EC2PDB Enzyme Link:	EC2PDB 1.3.8.8
ExplorEnz Enzyme Link:	ExplorEnz 1.3.8.8
PRIAM enzyme-specific profiles Link:	PRIAM 1.3.8.8
IntEnz Enzyme Link:	IntEnz 1.3.8.8
MEDLINE Enzyme Link:	MEDLINE 1.3.8.8

RHEA:17721	a long-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = a long-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]
RULE(radius=1)	[:1]-[CH2;+0:2]-[CH2;+0:3]-[:4].[:5]:[c;H0;+0:6]1:[n;H0;+0:7]:[:8]:[:9]:[n;H0;+0:10](-[:11]):[c;H0;+0:12]-1:[n;H0;+0:13]:[:14].[H+;H0:15]>>[:1]-[CH;+0:2]=[CH;+0:3]-[:4].[:5]:[c;H0;+0:6]1:[c;H0;+0:12](:[nH;+0:13]:[:14])-[N;H0;+0:10](-[:11])-[:9]:[:8]-[NH;+0:7]-1
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Core-to-Core	More

Title	Authors	Date	PubMed ID
Identification of the catalytic base in long chain acyl-CoA dehydrogenase.	Djordjevic S, Dong Y, Paschke R, Frerman FE, Strauss AW, Kim JJ	1994 Apr 12	8155643
Acyl coenzyme A dehydrogenases and electron-transferring flavoprotein from beef hart mitochondria.	Hall CL, Heijkenskjöld L, Bártfai T, Ernster L, Kamin H	1976 Dec	1015826
Purification and characterization of short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases from rat liver mitochondria. Isolation of the holo- and apoenzymes and conversion of the apoenzyme to the holoenzyme.	Ikeda Y, Okamura-Ikeda K, Tanaka K	1985 Jan 25	3968063