Biotin carboxylase
In enzymology, a biotin carboxylase (EC 6.3.4.14) is an enzyme that catalyzes the chemical reaction
- ATP + biotin-carboxyl-carrier protein + CO2 ADP + phosphate + carboxybiotin-carboxyl-carrier protein
| biotin carboxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 6.3.4.14 | ||||||||
| CAS number | 9075-71-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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| Biotin carboxylase C-terminal domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structure of biotin carboxylase domain of acetyl-coenzyme a carboxylase from saccharomyces cerevisiae in complex with soraphen a | |||||||||
| Identifiers | |||||||||
| Symbol | Biotin_carb_C | ||||||||
| Pfam | PF02785 | ||||||||
| InterPro | IPR005482 | ||||||||
| SCOP2 | 1dv1 / SCOPe / SUPFAM | ||||||||
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The 3 substrates of this enzyme are ATP, biotin-carboxyl-carrier protein, and CO2, whereas its 3 products are ADP, phosphate, and carboxybiotin-carboxyl-carrier protein.
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. The systematic name of this enzyme class is biotin-carboxyl-carrier-protein:carbon-dioxide ligase (ADP-forming). This enzyme is also called biotin carboxylase (component of acetyl CoA carboxylase). This enzyme participates in fatty acid biosynthesis.
A C-terminal conserved domain within this enzyme contains most of the active site residues.[1]
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1BNC, 1DV1, 1DV2, 2GPS, and 2GPW.
References
- Waldrop, G. L.; Rayment, I.; Holden, H. M. (1994). "Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase". Biochemistry. 33 (34): 10249–10256. doi:10.1021/bi00200a004. PMID 7915138.
Further reading
- Dimroth P, Guchhait RB, Stoll E, Lane MD (1970). "Enzymatic carboxylation of biotin: molecular and catalytic properties of a component enzyme of acetyl CoA carboxylase". Proc. Natl. Acad. Sci. U.S.A. 67 (3): 1353–60. Bibcode:1970PNAS...67.1353D. doi:10.1073/pnas.67.3.1353. PMC 283359. PMID 4922289.