Anti-acetyl CoA Carboxylase Antibody, clone 7D2.2

Acetyl-CoA carboxylase (ACC) is a biotin-dependent enzyme that catalyzes carboxylation of acetyl-CoA to produce malonyl-CoA through its two catalytic activities, biotin carboxylase (BC) and carboxyltransferase (CT). ACC is a multi-subunit enzyme in most prokaryotes, whereas it is a large, multi-domain enzyme in most eukaryotes. The activity of ACC can be controlled at the transcriptional level as well as by small molecule modulators and covalent modification. The human genome contains the genes for two different ACCs - ACACA and ACACB. The activity of the enzyme is controlled by reversible phosphorylation. The activity of the enzyme is inhibited if phosphorylated; the phosphorylation takes place when the hormone glucagon or epinephrine binds to the receptors or the energy status of the cell is low, leading to the activation of the AMP-activated protein kinase. The presence of fatty acid inhibits the activities of the enzyme. When insulin binds to its receptors, it activates a phosphatase to dephosphorylate the enzyme; the activities of the acetyl-CoA carboxylase is thus enhanced. Acetyl-CoA carboxylase has recently become a target in the design of new anti-obesity and antibiotic drugs.