Metallo-beta-lactamase domain-containing protein 2 (MBLAC2)

Metallo-beta-lactamase domain-containing protein 2 (MBLAC2) is a human enzyme that belongs to the metallo-beta-lactamase (MBL) superfamily, sharing a conserved αββα-fold structure and a metal-binding catalytic site, typically coordinating zinc ions. MBLAC2 is a zinc-dependent hydrolase with acyl-CoA thioesterase activity, meaning it hydrolyzes long-chain fatty acyl-CoA substrates, contributing to fatty acid metabolic processes and lipid regulation in the cell. Uniquely, MBLAC2 is S-palmitoylated and found on cellular membranes, interacting with specific acyltransferases such as zDHHC20 and possibly influencing substrate protein palmitoylation—but its exact physiological and disease relevance remains to be fully established. MBLAC2 is detected in the endoplasmic reticulum and plasma membrane and may be functionally linked to the regulation of lipid metabolism. No approved drugs currently target MBLAC2, and no major safety concerns have been linked to inhibition or modulation of this enzyme.

Other names

Acyl-coenzyme A thioesterase MBLAC2Acyl-CoA thioesterase MBLAC2Beta-lactamase MBLAC2Palmitoyl-coenzyme A thioesterase MBLAC2DKFZp686P15118MGC46734

No drugs target MBLAC2 in clinical use; mechanism would be expected hydrolase inhibition if developed