EC number:2.1.3.15
Enzyme
Download| EC Tree |
| 2. Transferases |
| 2.1 Transferring one-carbon groups |
| 2.1.3 Carboxy- and carbamoyltransferases |
| ID: | 2.1.3.15 |
|---|---|
| Description: | Acetyl-CoA carboxytransferase. |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 2.1.3.15 |
| BRENDA Enzyme Link: | BRENDA 2.1.3.15 |
| KEGG Enzyme Link: | KEGG2.1.3.15 |
| BioCyc Enzyme Link: | BioCyc 2.1.3.15 |
| ExPASy Enzyme Link: | ExPASy2.1.3.15 |
| EC2PDB Enzyme Link: | EC2PDB 2.1.3.15 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.1.3.15 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.1.3.15 |
| IntEnz Enzyme Link: | IntEnz 2.1.3.15 |
| MEDLINE Enzyme Link: | MEDLINE 2.1.3.15 |
| RHEA:54728 | acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein] |
| RULE(radius=1) | [*:1]-[CH3;+0:2].[*:3]-[N;H0;+0:4](-[*:5])-[C;H0;+0:6](=[*:7])-[*:8]>>[*:1]-[CH2;+0:2]-[C;H0;+0:6](=[*:7])-[*:8].[*:3]-[NH;+0:4]-[*:5] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| The structure of the carboxyltransferase component of acetyl-coA carboxylase reveals a zinc-binding motif unique to the bacterial enzyme. | Bilder P, Lightle S, Bainbridge G, Ohren J, Finzel B, Sun F, Holley S, Al-Kassim L, Spessard C, Melnick M, Newcomer M, Waldrop GL | 2006 Feb 14 | 16460018 |
| Characterization of a bifunctional archaeal acyl coenzyme A carboxylase. | Chuakrut S, Arai H, Ishii M, Igarashi Y | 2003 Feb | 12533469 |
| A tale of two functions: enzymatic activity and translational repression by carboxyltransferase. | Meades G Jr, Benson BK, Grove A, Waldrop GL | 2010 Mar | 19965770 |
| Identification and characterization of the first class of potent bacterial acetyl-CoA carboxylase inhibitors with antibacterial activity. | Freiberg C, Brunner NA, Schiffer G, Lampe T, Pohlmann J, Brands M, Raabe M, Häbich D, Ziegelbauer K | 2004 Jun 18 | 15066985 |