Structure-Function and Industrial Relevance of Bacterial Aminopeptidase P

Abstract

Aminopeptidase P (APPro, E.C 3.4.11.9) cleaves N-terminal amino acids from peptides and proteins where the penultimate residue is proline. This metal-ion-dependent enzyme shares a similar fold, catalytic mechanism, and substrate specificity with methionine aminopeptidase and prolidase. It adopts a canonical pita bread fold that serves as a structural basis for the metal-dependent catalysis and assembles as a tetramer in crystals. Similar to other metalloaminopeptidase, APPro requires metal ions for its maximal enzymatic activity, with manganese being the most preferred cation. Microbial aminopeptidase possesses unique characteristics compared with aminopeptidase from other sources, making it a great industrial enzyme for various applications. This review provides a summary of recent progress in the study of the structure and function of aminopeptidase P and describes its various applications in different industries as well as its significance in the environment.

Biochemical Characterisation and Structure Determination of a Novel Cold-Active Proline Iminopeptidase from the Psychrophilic Yeast, Glaciozyma antarctica PI12

“…Proline iminopeptidase (PIP, prolyl aminopeptidase; EC 3.4.11.5) is a unique exopeptidase that catalyses the cleavage of proline from N-terminal peptides [13]. The presence of prolines in polypeptides renders the polypeptides resistant to other proteases [14]. Proline iminopeptidases are known to be involved in the hydrolysis of peptides or proteins, but their biological functions are still unclear.…”