Enzyme

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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:1.3.8.1
Description:Short-chain acyl-CoA dehydrogenase.
Alternative Name: Unsaturated acyl-CoA reductase.
Short-chain acyl CoA dehydrogenase.
Butyryl dehydrogenase.
Butanoyl-CoA dehydrogenase.
Prosite: PDOC00070;
PDB:
PDBScop
Cath: 1.10.540.10; 1.20.140.10; 2.40.110.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.3.8.1
BRENDA Enzyme Link: BRENDA 1.3.8.1
KEGG Enzyme Link: KEGG1.3.8.1
BioCyc Enzyme Link: BioCyc 1.3.8.1
ExPASy Enzyme Link: ExPASy1.3.8.1
EC2PDB Enzyme Link: EC2PDB 1.3.8.1
ExplorEnz Enzyme Link: ExplorEnz 1.3.8.1
PRIAM enzyme-specific profiles Link: PRIAM 1.3.8.1
IntEnz Enzyme Link: IntEnz 1.3.8.1
MEDLINE Enzyme Link: MEDLINE 1.3.8.1
MSA:

1.3.8.1;

Phylogenetic Tree:

1.3.8.1;

Uniprot:
M-CSA:
RHEA:47196 a short-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = a short-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
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
The protein coded by the PP2216 gene of Pseudomonas putida KT2440 is an acyl-CoA dehydrogenase that oxidises only short-chain aliphatic substrates.McMahon B, Gallagher ME, Mayhew SG2005 Sep 116024185
Structure and mechanism of action of the acyl-CoA dehydrogenases.Thorpe C, Kim JJ1995 Jun7601336
The purification and properties of ox liver short-chain acyl-CoA dehydrogenase.Shaw L, Engel PC1984 Mar 16712627
Studies on the fatty acid oxidizing system of animal tissues. IV. The prosthetic group of butyryl coenzyme A dehydrogenase.MAHLER HR1954 Jan13130522
Studies on the fatty acid oxidizing system of animal tissues. III. Butyryl coenzyme A dehydrogenase.GREEN DE, MII S, MAHLER HR, BOCK RM1954 Jan13130521

RHEA:24004 butanoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E)-butenoyl-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
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Isolation and expression of a cDNA encoding the precursor for a novel member (ACADSB) of the acyl-CoA dehydrogenase gene family.Rozen R, Vockley J, Zhou L, Milos R, Willard J, Fu K, Vicanek C, Low-Nang L, Torban E, Fournier B1994 Nov 157698750
Structure and mechanism of action of the acyl-CoA dehydrogenases.Thorpe C, Kim JJ1995 Jun7601336
The purification and properties of ox liver short-chain acyl-CoA dehydrogenase.Shaw L, Engel PC1984 Mar 16712627
Identification and characterization of new long chain acyl-CoA dehydrogenases.He M, Pei Z, Mohsen AW, Watkins P, Murdoch G, Van Veldhoven PP, Ensenauer R, Vockley J2011 Apr21237683
Studies on the fatty acid oxidizing system of animal tissues. IV. The prosthetic group of butyryl coenzyme A dehydrogenase.MAHLER HR1954 Jan13130522
Studies on the fatty acid oxidizing system of animal tissues. III. Butyryl coenzyme A dehydrogenase.GREEN DE, MII S, MAHLER HR, BOCK RM1954 Jan13130521