ID: | 6.2.1.18 |
---|---|
Description: | Citrate--CoA ligase. |
Cath: | 3.30.1490.20; 3.30.470.110; 3.30.470.20; 3.40.50.720; 3.40.50.261; |
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Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.UniProtKB Enzyme Link: | UniProtKB 6.2.1.18 |
BRENDA Enzyme Link: | BRENDA 6.2.1.18 |
KEGG Enzyme Link: | KEGG6.2.1.18 |
BioCyc Enzyme Link: | BioCyc 6.2.1.18 |
ExPASy Enzyme Link: | ExPASy6.2.1.18 |
EC2PDB Enzyme Link: | EC2PDB 6.2.1.18 |
ExplorEnz Enzyme Link: | ExplorEnz 6.2.1.18 |
PRIAM enzyme-specific profiles Link: | PRIAM 6.2.1.18 |
IntEnz Enzyme Link: | IntEnz 6.2.1.18 |
MEDLINE Enzyme Link: | MEDLINE 6.2.1.18 |
RHEA:21472 | ATP + citrate + CoA = (3S)-citryl-CoA + ADP + phosphate |
RULE(radius=1) | [*:1]-[C;H0;+0:2](=[*:3])-[OH;+0:4].[*:5]-[SH;+0:6].[*:7]=[P;H0;+0:8](-[*:9])(-[*:10])-[O;H0;+0:11]-[*:12]>>[*:12]-[OH;+0:11].[*:5]-[S;H0;+0:6]-[C;H0;+0:2](-[*:1])=[*:3].[*:7]=[P;H0;+0:8](-[*:9])(-[*:10])-[OH;+0:4] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Isolation of enzymically active fragments formed by limited proteolysis of ATP citrate lyase. | Lill U, Schreil A, Eggerer H | 1982 Jul | 6749502 |
A novel enzyme, citryl-CoA synthetase, catalysing the first step of the citrate cleavage reaction in Hydrogenobacter thermophilus TK-6. | Aoshima M, Ishii M, Igarashi Y | 2004 May | 15101981 |