| EC Tree |
| 6. Ligases |
| 6.3 Forming carbon-nitrogen bonds |
| 6.3.4 Other carbon-nitrogen ligases |
| ID: | 6.3.4.15 |
|---|---|
| Description: | Biotin--[biotin carboxyl-carrier protein] ligase. |
| Alternative Name: |
Biotin--protein ligase. Biotin--[acetyl-CoA-carboxylase] ligase. Biotin--[acetyl-CoA carboxylase] synthetase. Acetyl-CoA carboxylase biotin holoenzyme synthetase. |
| Cath: | 1.10.10.10; 3.30.930.10; 2.30.30.10; 2.30.30.100; |
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 6.3.4.15 |
| BRENDA Enzyme Link: | BRENDA 6.3.4.15 |
| KEGG Enzyme Link: | KEGG6.3.4.15 |
| BioCyc Enzyme Link: | BioCyc 6.3.4.15 |
| ExPASy Enzyme Link: | ExPASy6.3.4.15 |
| EC2PDB Enzyme Link: | EC2PDB 6.3.4.15 |
| ExplorEnz Enzyme Link: | ExplorEnz 6.3.4.15 |
| PRIAM enzyme-specific profiles Link: | PRIAM 6.3.4.15 |
| IntEnz Enzyme Link: | IntEnz 6.3.4.15 |
| MEDLINE Enzyme Link: | MEDLINE 6.3.4.15 |
| RHEA:11756 | ATP + biotin + L-lysyl-[protein] = AMP + diphosphate + H(+) + N(6)-biotinyl-L-lysyl-[protein] |
| RULE(radius=1) | [*:1]-[C;H0;+0:2](=[*:3])-[OH;+0:4].[*:5]-[NH2;+0:6].[*:7]-[O;H0;+0:8]-[P;H0;+0:9](-[*:10])(=[*:11])-[*:12]>>[*:1]-[C;H0;+0:2](=[*:3])-[NH;+0:6]-[*:5].[*:7]-[OH;+0:8].[*:10]-[P;H0;+0:9](=[*:11])(-[*:12])-[OH;+0:4] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Purification and characterization of intact and truncated forms of the Escherichia coli biotin carboxyl carrier subunit of acetyl-CoA carboxylase. | Nenortas E, Beckett D | 1996 Mar 29 | 8631788 |
| Kinetics of biotinyl-5'-adenylate synthesis catalyzed by the Escherichia coli repressor of biotin biosynthesis and the stability of the enzyme-product complex. | Xu Y, Beckett D | 1994 Jun 14 | 8003500 |
| Purification and properties of the biotin repressor. A bifunctional protein. | Eisenberg MA, Prakash O, Hsiung SC | 1982 Dec 25 | 6129246 |
| Mechanisms Governing Precise Protein Biotinylation. | Sternicki LM, Wegener KL, Bruning JB, Booker GW, Polyak SW | 2017 May | 28268045 |
| Active site conformational changes upon reaction intermediate biotinyl-5'-AMP binding in biotin protein ligase from Mycobacterium tuberculosis. | Ma Q, Akhter Y, Wilmanns M, Ehebauer MT | 2014 Jul | 24723382 |
| Structural and functional studies of the biotin protein ligase from Aquifex aeolicus reveal a critical role for a conserved residue in target specificity. | Tron CM, McNae IW, Nutley M, Clarke DJ, Cooper A, Walkinshaw MD, Baxter RL, Campopiano DJ | 2009 Mar 20 | 19385043 |
| Corepressor-induced organization and assembly of the biotin repressor: a model for allosteric activation of a transcriptional regulator. | Weaver LH, Kwon K, Beckett D, Matthews BW | 2001 May 22 | 11353844 |