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Structure-function and industrial relevance of bacterial aminopeptidase P


Omar, Muhamad Nadzmi and Abd Rahman, Raja Noor Zaliha Raja and Muhd Noor, Noor Dina and Latip, Wahhida and Knight, Victor Feizal and Mohamad Ali, Mohd Shukuri (2021) Structure-function and industrial relevance of bacterial aminopeptidase P. Catalysts, 11 (10). art. no. 1157. pp. 1-14. ISSN 2073-4344


Aminopeptidase P (APPro, E.C 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.

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Official URL or Download Paper: https://www.mdpi.com/2073-4344/11/10/1157

Additional Metadata

Item Type: Article
Divisions: Faculty of Biotechnology and Biomolecular Sciences
DOI Number: https://doi.org/10.3390/catal11101157
Publisher: MDPI AG
Keywords: Bacterial aminopeptidase P; Structure; Manganese; Industrial applications; Environment
Depositing User: Ms. Che Wa Zakaria
Date Deposited: 06 Apr 2023 07:58
Last Modified: 06 Apr 2023 07:58
Altmetrics: http://www.altmetric.com/details.php?domain=psasir.upm.edu.my&doi=10.3390/catal11101157
URI: http://psasir.upm.edu.my/id/eprint/95190
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