The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

EC 6.3.4.15     
Accepted name: biotin—[biotin carboxyl-carrier protein] ligase
Reaction: ATP + biotin + [biotin carboxyl-carrier protein]-L-lysine = AMP + diphosphate + [biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine
Other name(s): birA (gene name); HLCS (gene name); HCS1 (gene name); biotin-[acetyl-CoA carboxylase] synthetase; biotin-[acetyl coenzyme A carboxylase] synthetase; acetyl coenzyme A holocarboxylase synthetase; acetyl CoA holocarboxylase synthetase; biotin:apocarboxylase ligase; Biotin holoenzyme synthetase; biotin:apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] ligase (AMP-forming); biotin—[acetyl-CoA-carboxylase] ligase
Systematic name: biotin:apo-[carboxyl-carrier protein] ligase (AMP-forming)
Comments: The enzyme biotinylates a biotin carboxyl-carrier protein that is part of an acetyl-CoA carboxylase complex, enabling its subsequent carboxylation by EC 6.3.4.14, biotin carboxylase. The carboxyl group is eventually transferred to acetyl-CoA by EC 2.1.3.15, acetyl-CoA carboxytransferase. In some organisms the carrier protein is part of EC 6.4.1.2, acetyl-CoA carboxylase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37340-95-7
References:
1.  Landman, A.D. and Dakshinamurti, K. Acetyl-Coenzyme A carboxylase. Role of the prosthetic group in enzyme polymerization. Biochem. J. 145 (1975) 545–548. [PMID: 239688]
2.  Wilson, K.P., Shewchuk, L.M., Brennan, R.G., Otsuka, A.J. and Matthews, B.W. Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains. Proc. Natl. Acad. Sci. USA 89 (1992) 9257–9261. [DOI] [PMID: 1409631]
3.  Nenortas, E. and Beckett, D. Purification and characterization of intact and truncated forms of the Escherichia coli biotin carboxyl carrier subunit of acetyl-CoA carboxylase. J. Biol. Chem. 271 (1996) 7559–7567. [DOI] [PMID: 8631788]
[EC 6.3.4.15 created 1978, modified 2018]
 
 


Data © 2001–2024 IUBMB
Web site © 2005–2024 Andrew McDonald