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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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Main Authors: Omar, Muhamad Nadzmi, Abd Rahman, Raja Noor Zaliha Raja, Muhd Noor, Noor Dina, Latip, Wahhida, Knight, Victor Feizal, Mohamad Ali, Mohd Shukuri
Format: Article
Published: MDPI AG 2021
Online Access:http://psasir.upm.edu.my/id/eprint/95190/
https://www.mdpi.com/2073-4344/11/10/1157
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spelling my.upm.eprints.951902023-04-06T07:58:00Z http://psasir.upm.edu.my/id/eprint/95190/ Structure-function and industrial relevance of bacterial aminopeptidase P Omar, Muhamad Nadzmi Abd Rahman, Raja Noor Zaliha Raja Muhd Noor, Noor Dina Latip, Wahhida Knight, Victor Feizal Mohamad Ali, Mohd Shukuri 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. MDPI AG 2021-09-26 Article PeerReviewed 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 https://www.mdpi.com/2073-4344/11/10/1157 10.3390/catal11101157
institution Universiti Putra Malaysia
building UPM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Putra Malaysia
content_source UPM Institutional Repository
url_provider http://psasir.upm.edu.my/
description 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.
format Article
author Omar, Muhamad Nadzmi
Abd Rahman, Raja Noor Zaliha Raja
Muhd Noor, Noor Dina
Latip, Wahhida
Knight, Victor Feizal
Mohamad Ali, Mohd Shukuri
spellingShingle Omar, Muhamad Nadzmi
Abd Rahman, Raja Noor Zaliha Raja
Muhd Noor, Noor Dina
Latip, Wahhida
Knight, Victor Feizal
Mohamad Ali, Mohd Shukuri
Structure-function and industrial relevance of bacterial aminopeptidase P
author_facet Omar, Muhamad Nadzmi
Abd Rahman, Raja Noor Zaliha Raja
Muhd Noor, Noor Dina
Latip, Wahhida
Knight, Victor Feizal
Mohamad Ali, Mohd Shukuri
author_sort Omar, Muhamad Nadzmi
title Structure-function and industrial relevance of bacterial aminopeptidase P
title_short Structure-function and industrial relevance of bacterial aminopeptidase P
title_full Structure-function and industrial relevance of bacterial aminopeptidase P
title_fullStr Structure-function and industrial relevance of bacterial aminopeptidase P
title_full_unstemmed Structure-function and industrial relevance of bacterial aminopeptidase P
title_sort structure-function and industrial relevance of bacterial aminopeptidase p
publisher MDPI AG
publishDate 2021
url http://psasir.upm.edu.my/id/eprint/95190/
https://www.mdpi.com/2073-4344/11/10/1157
_version_ 1762839463007879168
score 13.211869

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