ID: | 3.1.2.16 |
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Description: | Citrate-lyase deacetylase. |
Alternative Name: |
Citrate lyase deacetylase. Acetyl-S-(acyl-carrier protein) enzyme thioester hydrolase. [Citrate-(pro-3S)-lyase] thiolesterase. [Citrate-(pro-3S)-lyase] thioesterase. |
Cath: | 1.10.287.2470; 3.20.20.60; 3.40.1080.10; |
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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 3.1.2.16 |
BRENDA Enzyme Link: | BRENDA 3.1.2.16 |
KEGG Enzyme Link: | KEGG3.1.2.16 |
BioCyc Enzyme Link: | BioCyc 3.1.2.16 |
ExPASy Enzyme Link: | ExPASy3.1.2.16 |
EC2PDB Enzyme Link: | EC2PDB 3.1.2.16 |
ExplorEnz Enzyme Link: | ExplorEnz 3.1.2.16 |
PRIAM enzyme-specific profiles Link: | PRIAM 3.1.2.16 |
IntEnz Enzyme Link: | IntEnz 3.1.2.16 |
MEDLINE Enzyme Link: | MEDLINE 3.1.2.16 |
RHEA:13657 | acetyl-[citrate lyase ACP] + H2O = acetate + H(+) + holo-[citrate lyase ACP] |
RULE(radius=1) | [*:1]-[S;H0;+0:2]-[C;H0;+0:3](=[*:4])-[*:5].[OH2;+0:6]>>[*:1]-[SH;+0:2].[*:4]=[C;H0;+0:3](-[*:5])-[OH;+0:6] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Citrate lyase deacetylase of Rhodopseudomonas gelatinosa. Isolation of the enzyme and studies on the inhibition by L-glutamate. | Giffhorn F, Rode H, Kuhn A, Gottschalk G | 1980 Oct | 7460909 |