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.
Highlights
Enzymes from bacteria and other microorganisms have received a lot of interest resulting from their widespread use in various industrial sectors because of their stability, catalytic activity, ease of production, and optimization compared with other plant and animal enzymes [1]
A study carried out in 2002 suggested that low concentrations of aminopeptidase P could be a predisposing factor for the angioedema development in patients treated with angiotensin-converting enzyme (ACE) inhibitors
This review shows that aminopeptidase P has significant properties that would make this enzyme be capable of cleaving peptides containing proline as a second residue and could play an important role in the regulation of biological activity
Summary
Enzymes from bacteria and other microorganisms have received a lot of interest resulting from their widespread use in various industrial sectors because of their stability, catalytic activity, ease of production, and optimization compared with other plant and animal enzymes [1]. In contrast to other metalloaminopeptidases, APPro is a cytoplasmic aminopeptidase and recognizes a restricted scissile Xaa–Pro bond of the polypeptide or protein substrates that may be related to virulence-related phenotypes or other biological activities beyond the ability to degrade proteins in general [24] This enzyme is encoded by pepP genes that are one of the critical virulence-associated genes identified through a Pseudomonas aeruginosa-Caernohaditis elegans infection model [25]. APPro has been found and characterized from diverse sources, including bacteria, fungi, plants, and from the tissues of several mammalian species This enzyme is thought to have a role in a number of important biological processes; for example, hormone regulation in mammals and terminal degradation of proline-containing peptides and proteins or organophosphate compounds in bacteria [26]. The crystal structures of bacterial APPros from Escherichia coli and Pseudomonas aeruginosa are used as examples to demonstrate the similarities and differences in their 3D structure
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