ExplorEnz: EC 6.3.4.14

Your query returned 1 entry. Printable version

6.3.4.14

Accepted name:

biotin carboxylase

Reaction:

ATP + [biotin carboxyl-carrier protein]-biotin-N⁶-L-lysine + hydrogencarbonate- = ADP + phosphate + [biotin carboxyl-carrier protein]-carboxybiotin-N⁶-L-lysine

Other name(s):

accC (gene name); biotin-carboxyl-carrier-protein:carbon-dioxide ligase (ADP-forming)

Systematic name:

[biotin carboxyl-carrier protein]-biotin-N⁶-L-lysine:hydrogencarbonate ligase (ADP-forming)

Comments:

This enzyme, part of an acetyl-CoA carboxylase complex, acts on a biotin carboxyl-carrier protein (BCCP) that has been biotinylated by EC 6.3.4.15, biotin—[biotin carboxyl-carrier protein] ligase. In some organisms the enzyme is part of a multi-domain polypeptide that also includes the carrier protein (e.g. mycobacteria). Yet in other organisms (e.g. mammals) this activity is included in a single polypeptide that also catalyses the transfer of the carboxyl group from biotin to acetyl-CoA (see EC 6.4.1.2, acetyl-CoA carboxylase).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9075-71-2

References:

1.	Dimroth, P., Guchhait, R.B., Stoll, E. and Lane, M.D. Enzymatic carboxylation of biotin: molecular and catalytic properties of a component enzyme of acetyl CoA carboxylase. Proc. Natl. Acad. Sci. USA 67 (1970) 1353–1360. [DOI] [PMID: 4922289]
2.	Norman, E., De Smet, K.A., Stoker, N.G., Ratledge, C., Wheeler, P.R. and Dale, J.W. Lipid synthesis in mycobacteria: characterization of the biotin carboxyl carrier protein genes from Mycobacterium leprae and M. tuberculosis. J. Bacteriol. 176 (1994) 2525–2531. [DOI] [PMID: 7909542]
3.	Janiyani, K., Bordelon, T., Waldrop, G.L. and Cronan, J.E., Jr. Function of Escherichia coli biotin carboxylase requires catalytic activity of both subunits of the homodimer. J. Biol. Chem. 276 (2001) 29864–29870. [DOI] [PMID: 11390406]
4.	Chou, C.Y., Yu, L.P. and Tong, L. Crystal structure of biotin carboxylase in complex with substrates and implications for its catalytic mechanism. J. Biol. Chem. 284 (2009) 11690–11697. [DOI] [PMID: 19213731]
5.	Broussard, T.C., Pakhomova, S., Neau, D.B., Bonnot, R. and Waldrop, G.L. Structural analysis of substrate, reaction intermediate, and product binding in Haemophilus influenzae biotin carboxylase. Biochemistry 54 (2015) 3860–3870. [DOI] [PMID: 26020841]

[EC 6.3.4.14 created 1976, modified 2014, modified 2018]