Biotin carboxylase
Biotin carboxylase C-terminal domain |
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crystal structure of biotin carboxylase domain of acetyl-coenzyme a carboxylase from saccharomyces cerevisiae in complex with soraphen a |
Identifiers |
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Symbol |
Biotin_carb_C |
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Pfam |
PF02785 |
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InterPro |
IPR005482 |
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SCOP |
1dv1 |
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SUPERFAMILY |
1dv1 |
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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
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
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| 6.1: Carbon-Oxygen | |
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| 6.2: Carbon-Sulfur | |
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| 6.3: Carbon-Nitrogen | |
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