| EC Tree |
| 2. Transferases |
| 2.8 Transferring sulfur-containing groups |
| 2.8.3 CoA-transferases |
| ID: | 2.8.3.10 |
|---|---|
| Description: | Citrate CoA-transferase. |
| Cath: | 1.10.287.2470; 3.20.20.60; 3.40.1080.10; |
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 2.8.3.10 |
| BRENDA Enzyme Link: | BRENDA 2.8.3.10 |
| KEGG Enzyme Link: | KEGG2.8.3.10 |
| BioCyc Enzyme Link: | BioCyc 2.8.3.10 |
| ExPASy Enzyme Link: | ExPASy2.8.3.10 |
| EC2PDB Enzyme Link: | EC2PDB 2.8.3.10 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.8.3.10 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.8.3.10 |
| IntEnz Enzyme Link: | IntEnz 2.8.3.10 |
| MEDLINE Enzyme Link: | MEDLINE 2.8.3.10 |
| RHEA:19405 | acetyl-CoA + citrate = (3S)-citryl-CoA + acetate |
| RULE(radius=1) | [C:1][S:2][C:3](=[O:4])[C:5].[O:10][C:11](=[O:12])[C:13]>>[O:10][C:3](=[O:4])[C:5].[C:1][S:2][C:11](=[O:12])[C:13] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Characterization of the isolated transferase subunit of citrate lyase as a CoA-Transferase. Evidence against a covalent enzyme-substrate intermediate. | Dimroth P, Loyal R, Eggerer H | 1977 Nov 1 | 336371 |