AcetylCoAsta

AcetylCoAsta is a hypothetical enzyme proposed to act as an acetyltransferase that uses acetyl-CoA as the acetyl donor to modify a range of substrates. The name blends acetyl-CoA with the standard enzyme-suffix -sta, following conventions used for acetyltransferases in some model systems.

Proposed mechanism: The enzyme binds acetyl-CoA in a conserved pocket and transfers the acetyl group to a recipient molecule, producing CoA and an acetylated product. In models where acetylCoAsta operates, substrates may include amines, alcohols, or small metabolites, thereby linking acetyl-CoA flux to downstream biosynthetic or regulatory pathways. The enzyme is often predicted to have a GNAT-like catalytic core, with a conserved residue acting as a general base.

Distribution and evidence: The concept arises from comparative genomics and proteomics where sequences with modest similarity to known acetyltransferases appear in several bacteria and eukaryotes; in some studies, recombinant proteins show acetyltransferase activity in vitro, but in vivo function remains unconfirmed.

Biological role: Potentially contributes to regulation of acetyl-CoA pools, post-translational modification of proteins, or modification of metabolic intermediates; could play a role in responses to nutrient status or stress.

Nomenclature and status: Because acetylCoAsta is not widely recognized as a distinct, validated enzyme, some databases group related activities under broader acetyltransferase families rather than as a separate entity. The term is used mainly in speculative or preliminary reports and may be superseded by more precise names if proven.

See also acetyltransferase, GNAT family, acetyl-CoA.