Enzyme

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     1. Oxidoreductases
        1.2 Acting on the aldehyde or oxo group of donors
            1.2.1 With NAD+ or NADP+ as acceptor
ID:1.2.1.18
Description:Malonate-semialdehyde dehydrogenase (acetylating).
Cath: 3.40.605.10; 3.40.309.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.2.1.18
BRENDA Enzyme Link: BRENDA 1.2.1.18
KEGG Enzyme Link: KEGG1.2.1.18
BioCyc Enzyme Link: BioCyc 1.2.1.18
ExPASy Enzyme Link: ExPASy1.2.1.18
EC2PDB Enzyme Link: EC2PDB 1.2.1.18
ExplorEnz Enzyme Link: ExplorEnz 1.2.1.18
PRIAM enzyme-specific profiles Link: PRIAM 1.2.1.18
IntEnz Enzyme Link: IntEnz 1.2.1.18
MEDLINE Enzyme Link: MEDLINE 1.2.1.18
MSA:

1.2.1.18;

Phylogenetic Tree:

1.2.1.18;

Uniprot:
M-CSA:
RHEA:22992 3-oxopropanoate + CoA + NAD(+) = acetyl-CoA + CO2 + NADH
RULE(radius=1) [*:1]-[SH;+0:2].[*:3]-[c;H0;+0:4]1:[cH;+0:5]:[cH;+0:6]:[cH;+0:7]:[n+;H0:8](-[*:9]):[cH;+0:10]:1.[*:11]=[CH;+0:12]-[CH2;+0:13]-[C;H0;+0:14](=[*:15])-[OH;+0:16]>>[*:3]-[C;H0;+0:4]1=[CH;+0:10]-[N;H0;+0:8](-[*:9])-[CH;+0:7]=[CH;+0:6]-[CH2;+0:5]-1.[*:1]-[S;H0;+0:2]-[C;H0;+0:12](=[*:11])-[CH3;+0:13].[*:15]=[C;H0;+0:14]=[O;H0;+0:16]
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References

TitleAuthorsDatePubMed ID
Mechanistic characterization of the MSDH (methylmalonate semialdehyde dehydrogenase) from Bacillus subtilis.Stines-Chaumeil C, Talfournier F, Branlant G2006 Apr 116332250

RHEA:22988 3-oxopropanoate + CoA + NADP(+) = acetyl-CoA + CO2 + NADPH
RULE(radius=1) [*:1]-[SH;+0:2].[*:3]-[c;H0;+0:4]1:[cH;+0:5]:[cH;+0:6]:[cH;+0:7]:[n+;H0:8](-[*:9]):[cH;+0:10]:1.[*:11]=[C;H0;+0:12](-[OH;+0:13])-[CH2;+0:14]-[CH;+0:15]=[*:16]>>[*:3]-[C;H0;+0:4]1=[CH;+0:10]-[N;H0;+0:8](-[*:9])-[CH;+0:7]=[CH;+0:6]-[CH2;+0:5]-1.[*:1]-[S;H0;+0:2]-[C;H0;+0:15](=[*:16])-[CH3;+0:14].[*:11]=[C;H0;+0:12]=[O;H0;+0:13]
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