Biotin carboxylase

From Wikipedia, the free encyclopedia

This is an old revision of this page, as edited by BU RoBOT (talk | contribs) at 15:24, 10 August 2016 (→‎Further reading: Sort into more specific stub template based on presence in Category:EC 6.3 or subcategories (Task 25)). The present address (URL) is a permanent link to this revision, which may differ significantly from the current revision.

biotin carboxylase
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 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

  1. ^ 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