Enzyme

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EC Tree
     1. Oxidoreductases
        1.1 Acting on the CH-OH group of donors
            1.1.1 With NAD+ or NADP+ as acceptor
ID:1.1.1.36
Description:Acetoacetyl-CoA reductase.
Prosite: PDOC00060;
PDB:
PDBScop
Cath: 3.40.50.720;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.1.1.36
BRENDA Enzyme Link: BRENDA 1.1.1.36
KEGG Enzyme Link: KEGG1.1.1.36
BioCyc Enzyme Link: BioCyc 1.1.1.36
ExPASy Enzyme Link: ExPASy1.1.1.36
EC2PDB Enzyme Link: EC2PDB 1.1.1.36
ExplorEnz Enzyme Link: ExplorEnz 1.1.1.36
PRIAM enzyme-specific profiles Link: PRIAM 1.1.1.36
IntEnz Enzyme Link: IntEnz 1.1.1.36
MEDLINE Enzyme Link: MEDLINE 1.1.1.36
MSA:

1.1.1.36;

Phylogenetic Tree:

1.1.1.36;

Uniprot:
M-CSA:
RHEA:45796 (3R)-hydroxybutanoyl-CoA + NADP(+) = acetoacetyl-CoA + H(+) + NADPH
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[OH;+0:4].[*:5]-[c;H0;+0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[n+;H0:10](-[*:11]):[cH;+0:12]:1>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:4].[*:5]-[C;H0;+0:6]1=[CH;+0:12]-[N;H0;+0:10](-[*:11])-[CH;+0:9]=[CH;+0:8]-[CH2;+0:7]-1
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Crystal structure of (R)-3-hydroxybutyryl-CoA dehydrogenase PhaB from Ralstonia eutropha.Kim J, Chang JH, Kim EJ, Kim KJ2014 Jan 1724211201
Directed evolution and structural analysis of NADPH-dependent Acetoacetyl Coenzyme A (Acetoacetyl-CoA) reductase from Ralstonia eutropha reveals two mutations responsible for enhanced kinetics.Matsumoto K, Tanaka Y, Watanabe T, Motohashi R, Ikeda K, Tobitani K, Yao M, Tanaka I, Taguchi S2013 Oct23913421

RHEA:22256 a (3R)-hydroxyacyl-CoA + NADP(+) = a 3-oxoacyl-CoA + H(+) + NADPH
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[OH;+0:4].[*:5]-[c;H0;+0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[n+;H0:10](-[*:11]):[cH;+0:12]:1>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:4].[*:5]-[C;H0;+0:6]1=[CH;+0:12]-[N;H0;+0:10](-[*:11])-[CH;+0:9]=[CH;+0:8]-[CH2;+0:7]-1
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Crystal structure of (R)-3-hydroxybutyryl-CoA dehydrogenase PhaB from Ralstonia eutropha.Kim J, Chang JH, Kim EJ, Kim KJ2014 Jan 1724211201
Directed evolution and structural analysis of NADPH-dependent Acetoacetyl Coenzyme A (Acetoacetyl-CoA) reductase from Ralstonia eutropha reveals two mutations responsible for enhanced kinetics.Matsumoto K, Tanaka Y, Watanabe T, Motohashi R, Ikeda K, Tobitani K, Yao M, Tanaka I, Taguchi S2013 Oct23913421
Binary structure of the two-domain (3R)-hydroxyacyl-CoA dehydrogenase from rat peroxisomal multifunctional enzyme type 2 at 2.38 A resolution.Haapalainen AM, Koski MK, Qin YM, Hiltunen JK, Glumoff T2003 Jan12517343