| ID: | 3.1.2.3 |
|---|---|
| Description: | Succinyl-CoA hydrolase. |
| Alternative Name: |
Succinyl-CoA acylase. |
Click one PDB to see exact 3D structure provided by NGL.
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 3.1.2.3 |
| BRENDA Enzyme Link: | BRENDA 3.1.2.3 |
| KEGG Enzyme Link: | KEGG3.1.2.3 |
| BioCyc Enzyme Link: | BioCyc 3.1.2.3 |
| ExPASy Enzyme Link: | ExPASy3.1.2.3 |
| EC2PDB Enzyme Link: | EC2PDB 3.1.2.3 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.1.2.3 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.1.2.3 |
| IntEnz Enzyme Link: | IntEnz 3.1.2.3 |
| MEDLINE Enzyme Link: | MEDLINE 3.1.2.3 |
| RHEA:11516 | H2O + succinyl-CoA = CoA + H(+) + succinate |
| RULE(radius=1) | [*:1]-[C;H0;+0:2](=[*:3])-[S;H0;+0:4]-[*:5].[OH2;+0:6]>>[*:1]-[C;H0;+0:2](=[*:3])-[OH;+0:6].[*:5]-[SH;+0:4] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Succinyl and acetyl coenzyme a deacylases. | GERGELY J, HELE P, RAMAKRISHNAN CV | 1952 Sep | 12999747 |
| Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs. | Hunt MC, Rautanen A, Westin MA, Svensson LT, Alexson SE | 2006 Sep | 16940157 |
| The identification of a succinyl-CoA thioesterase suggests a novel pathway for succinate production in peroxisomes. | Westin MA, Hunt MC, Alexson SE | 2005 Nov 18 | 16141203 |