Enzyme

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EC Tree
     6. Ligases
        6.2 Forming carbon-sulfur bonds
            6.2.1 Acid-thiol ligases
ID:6.2.1.1
Description:Acetate--CoA ligase.
Alternative Name: Acyl-activating enzyme.
Acetyl-CoA synthetase.
Acetyl-CoA synthase.
Acetyl-activating enzyme.
Acetate thiokinase.
Prosite: PDOC00427;
PDB:
PDBScop
Cath: 3.30.300.30;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 6.2.1.1
BRENDA Enzyme Link: BRENDA 6.2.1.1
KEGG Enzyme Link: KEGG6.2.1.1
BioCyc Enzyme Link: BioCyc 6.2.1.1
ExPASy Enzyme Link: ExPASy6.2.1.1
EC2PDB Enzyme Link: EC2PDB 6.2.1.1
ExplorEnz Enzyme Link: ExplorEnz 6.2.1.1
PRIAM enzyme-specific profiles Link: PRIAM 6.2.1.1
IntEnz Enzyme Link: IntEnz 6.2.1.1
MEDLINE Enzyme Link: MEDLINE 6.2.1.1
MSA:

6.2.1.1;

Phylogenetic Tree:

6.2.1.1;

Uniprot:
M-CSA:
RHEA:23176 acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate
RULE(radius=1) [*:1]-[P;H0;+0:2](=[*:3])(-[*:4])-[O;H0;+0:5]-[*:6].[*:7]-[SH;+0:8].[*:9]=[C;H0;+0:10](-[*:11])-[OH;+0:12]>>[*:6]-[OH;+0:5].[*:1]-[P;H0;+0:2](=[*:3])(-[*:4])-[OH;+0:12].[*:7]-[S;H0;+0:8]-[C;H0;+0:10](=[*:9])-[*:11]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Molecular cloning of rat acss3 and characterization of mammalian propionyl-CoA synthetase in the liver mitochondrial matrix.Yoshimura Y, Araki A, Maruta H, Takahashi Y, Yamashita H2017 Mar 128003429
Molecular characterization of human acetyl-CoA synthetase, an enzyme regulated by sterol regulatory element-binding proteins.Luong A, Hannah VC, Brown MS, Goldstein JL2000 Aug 2510843999