CATH Domain 4wz8B03

CATH Classification

Level	CATH Code	Description
	3	Alpha Beta
	3.90	Alpha-Beta Complex
	3.90.226	2-enoyl-CoA Hydratase; Chain A, domain 1
	3.90.226.10	2-enoyl-CoA Hydratase; Chain A, domain 1

Domain Context

CATH Clusters

Superfamily	2-enoyl-CoA Hydratase; Chain A, domain 1
Functional Family	acetyl-CoA carboxylase isoform X2

Enzyme Information

6.3.4.14

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 6.3.4.15. -!- 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 6.4.1.2).

6.4.1.2

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 6.3.4.14 and EC 2.1.3.15). -!- The carboxylation of the carrier protein requires ATP, while the transfer of the carboxyl group to acetyl-CoA does not.

UniProtKB Entries (1)

Q00955

ACAC_YEAST

Saccharomyces cerevisiae S288C

Acetyl-CoA carboxylase

PDB Structure

PDB	4WZ8
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism
Primary Citation	Decreasing the Rate of Metabolic Ketone Reduction in the Discovery of a Clinical Acetyl-CoA Carboxylase Inhibitor for the Treatment of Diabetes. Griffith, D.A., Kung, D.W., Esler, W.P., Amor, P.A., Bagley, S.W., Beysen, C., Carvajal-Gonzalez, S., Doran, S.D., Limberakis, C., Mathiowetz, A.M., McPherson, K., Price, D.A., Ravussin, E., Sonnenberg, G.E., Southers, J.A., Sweet, L.J., Turner, S.M., Vajdos, F.F. J.Med.Chem.