Precursor Structure of Cephalosporin Acylase: Insights into Auto-Proteolytic Activation in a New N-Terminal Hydrolase Family

Autocatalytic proteolytic cleavage is a frequently observed post-translational modification in proteins. Cephalosporin acylase (CA) is a recently identified member of the Nterminal hydrolase family that is activated from an inactive precursor by autoproteolytic processing, generating a new N-terminal residue, which is either a Ser or a Thr[1]. The N-terminal Ser or Thr becomes a nucleophilic catalytic center for intramolecular and intermolecular amide cleavages. The gene structure of the open reading frame of CAs generally consist of a signal peptide followed by the α-subunit, a spacer sequence, and the β-subunit, which are all translated into a single polypeptide chain, the CA precursor. The precursor is post-translationally modified into an active heterodimeric enzyme with α- and β-subunits, first by intramolecular cleavage and second, by intermolecular cleavage.

Abstract licence: CC BY

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