Biotin— ligase | |||||||||
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Identifiers | |||||||||
EC no. | 6.3.4.15 | ||||||||
CAS no. | 37340-95-7 | ||||||||
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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In enzymology, a biotin— ligase (EC 6.3.4.15) is an enzyme that catalyzes the chemical reaction
- ATP + biotin + apo- AMP + diphosphate +
The 3 substrates of this enzyme are ATP, biotin, and apo-, whereas its 3 products are AMP, diphosphate, and acetyl-CoA:carbon-dioxide ligase (ADP-forming).
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds.
This enzyme participates in biotin metabolism. This protein may use the morpheein model of allosteric regulation.
Nomenclature
The systematic name of this enzyme class is biotin:apo- ligase (AMP-forming). Other names in common use include:
- biotin- synthetase,
- biotin- synthetase,
- acetyl coenzyme A holocarboxylase synthetase,
- acetyl CoA holocarboxylase synthetase,
- biotin:apocarboxylase ligase,
- biotin holoenzyme synthetase,
- and HCS.
References
- Selwood T, Jaffe EK (March 2012). "Dynamic dissociating homo-oligomers and the control of protein function". Arch. Biochem. Biophys. 519 (2): 131–43. doi:10.1016/j.abb.2011.11.020. PMC 3298769. PMID 22182754.
Further reading
- Landman AD, Darkshinamurti K (March 1975). "Acetyl-Coenzyme A carboxylase. Role of the prosthetic group in enzyme polymerization". Biochem. J. 145 (3): 545–8. doi:10.1042/bj1450545. PMC 1165255. PMID 239688.
Enzymes: CO CS and CN ligases (EC 6.1-6.3) | |
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6.1: Carbon-Oxygen | |
6.2: Carbon-Sulfur | |
6.3: Carbon-Nitrogen |
Enzymes | |
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Activity | |
Regulation | |
Classification | |
Kinetics | |
Types |
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