CATH Classification

Domain Context

CATH Clusters

Superfamily 2-enoyl-CoA Hydratase; Chain A, domain 1
Functional Family Acetyl-CoA carboxylase 1

Enzyme Information
Biotin carboxylase.
based on mapping to UniProt Q00955
ATP + [biotin carboxyl-carrier protein]-biotin-N(6)-L-lysine + hydrogencarbonate- = ADP + phosphate + [biotin carboxyl-carrier protein]- carboxybiotin-N(6)-L-lysine.
-!- This enzyme, part of an acetyl-CoA carboxylase complex, acts on a biotin carboxyl-carrier protein (BCCP) that has been biotinylated by EC -!- 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 catalyzes the transfer of the carboxyl group from biotin to acetyl-CoA (see EC
Acetyl-CoA carboxylase.
based on mapping to UniProt Q00955
ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate + malonyl-CoA.
-!- This enzyme is a multi-domain polypeptide that catalyzes three different activities - a biotin carboxyl-carrier protein (BCCP), a biotin carboxylase that catalyzes the transfer of a carboxyl group from hydrogencarbonate to the biotin molecule carried by the carrier protein, and the transfer of the carboxyl group from biotin to acetyl-CoA, forming malonyl-CoA. -!- In some organisms these activities are catalyzed by separate enzymes (see EC and EC -!- The carboxylation of the carrier protein requires ATP, while the transfer of the carboxyl group to acetyl-CoA does not.

UniProtKB Entries (1)

Saccharomyces cerevisiae S288C
Acetyl-CoA carboxylase

PDB Structure

External Links
Primary Citation
Discovery of spirocyclic-diamine inhibitors of mammalian acetyl CoA-carboxylase.
Kung, D.W., Griffith, D.A., Esler, W.P., Vajdos, F.F., Mathiowetz, A.M., Doran, S.D., Amor, P.A., Bagley, S.W., Banks, T., Cabral, S., Ford, K., Garcia-Irizarry, C.N., Landis, M.S., Loomis, K., McPherson, K., Niosi, M., Rockwell, K.L., Rose, C., Smith, A.C., Southers, J.A., Tapley, S., Tu, M., Valentine, J.J.