Biotin carboxylase

Biotin carboxylase
Biotin carboxylase homodimer, E.Coli
Identifiers
EC no.6.3.4.14
CAS no.9075-71-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
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
SymbolBiotin_carb_C
PfamPF02785
InterProIPR005482
SCOP21dv1 / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

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 three substrates of this enzyme are ATP, biotin-carboxyl-carrier protein (BCCP), and CO2, whereas its three products are ADP, phosphate, and carboxybiotin-carboxyl-carrier protein.

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 ATP-grasp enzyme participates in fatty acid biosynthesis. This enzyme participates in fatty acid biosynthesis by providing one of the catalytic functions of the Acetyl-CoA carboxylase complex. As previously mentioned, after the carboxybiotin product is formed, the carboxyltransferase unit of the complex will transfer the activated carboxy group from BCCP to Acetyl-CoA, forming a malonate analog known as malonyl-CoA. Malonyl-CoA serves as the primary carbon donor in fatty acid biosynthesis, followed by a series of reduction and dehydration reactions to remove the acyl group.