acilenzyme

Acilenzyme is a hypothetical enzyme family defined as catalysts of acyl transfer and hydrolysis involving acyl groups (R-C=O). In this framework, acilenzyme catalyzes the transfer of acyl groups from donors such as acyl-CoA, acyl-phosphates, or anhydrides to acceptors including alcohols, amines, sugars, or water, enabling ester and amide bond formation and cleavage.

Most proposed acilenzyme catalytic mechanisms involve a conserved nucleophile (often serine) that forms a transient acyl-enzyme intermediate, supported by a general base (histidine) and an acid (aspartate or another residue). Active-site pockets accommodate varied acyl chain lengths, and twin-substrate binding ensures coupling of transfer events. Structures, when solved, resemble hydrolases or acyltransferases with alpha/beta folds.

Within the hypothetical organisms, acilenzyme participates in lipid remodeling, detoxification of acyl-CoAs, and biosynthesis of esterified metabolites. Its activity can be regulated by coenzymes, pH, and allosteric effectors.

In synthetic biology and industrial chemistry, acilenzyme concepts inform design of biocatalysts for production of esters, amides, biodegradable polymers, and flavor compounds. Researchers use computational design and directed evolution to tailor substrate scope and stability. No consensus on natural occurrence; status is theoretical or experimental in early-stage studies.