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Description

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. Human genome contains the genes for two different ACCs - ACACA and ACACB. The activity of the enzyme is controlled by the reversible phosphorylation. The activities of the enzyme is inhibited if phosphorylated, the phosphorylation takes place when the hormones, glucagon or epinephrine bind 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 of the cell, 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.