Structure-Function and Industrial Relevance of Bacterial Aminopeptidase P

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 c...

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Bibliographic Details
Published in:Catalysts 2021-10, Vol.11 (10), p.1157
Main Authors: Omar, Muhamad Nadzmi, Raja Abd Rahman, Raja Noor Zaliha, Muhd Noor, Noor Dina, Latip, Wahhida, Knight, Victor Feizal, Ali, Mohd Shukuri Mohamad
Format: Article
Language:English
Subjects:
Amino acids
Bacteria
Binding sites
Catalysis
Catalysts
Chemical reactions
Crystal structure
E coli
Enzymes
Genes
Mammals
Manganese
Metal ions
Methionine
Microorganisms
Peptides
Polypeptides
Proline
Proteins
Substrates
Virulence
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Description
Summary: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.
ISSN:2073-4344
2073-4344
DOI:10.3390/catal11101157