enzymeadenylate

Enzymeadenylate is not a standard, widely used name in biochemistry. In many contexts, it may refer to enzymes that catalyze adenylation, the transfer or creation of an adenylyl (AMP) group on a substrate. Depending on the context, enzymeadenylate activity may describe two related but distinct reactions: AMPylation, in which an adenylate group is transferred from ATP to a target molecule, and activation of substrates by adenylation during biosynthesis, forming adenylated intermediates such as aminoacyl-AMP.

Mechanistically, AMP transfer to a substrate typically requires ATP as the donor and divalent metal cofactors such as Mg2+. In AMPylation, enzymes known as AMP-transferases or Fic-domain proteins catalyze the transfer of AMP to residues on proteins or other substrates, modulating their function. In nonribosomal peptide synthetase (NRPS) and polyketide synthase (PKS) pathways, adenylation domains activate carboxylate substrates by forming aminoacyl-AMP intermediates before subsequent transfer to carrier proteins.

Structurally, enzymes associated with adenylation often bind ATP in nucleotide-binding pockets and share motifs common to adenylate-forming enzymes. They may belong to several superfamilies, including those dedicated to AMP transfer or to substrate activation for biosynthetic assembly lines.

Biological roles include regulation of protein activity through AMPylation, signaling via cyclic nucleotides, and the activation steps in the biosynthesis of natural products. The term appears mainly in annotations or discussions of enzyme function; when possible, it is better to use more specific terms such as AMP transferases, AMPylases, or adenylation domains to avoid ambiguity.