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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| Format: | Article |
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MDPI AG
2021
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| author | Omar, Muhamad Nadzmi Abd Rahman, Raja Noor Zaliha Raja Muhd Noor, Noor Dina Latip, Wahhida Knight, Victor Feizal Mohamad Ali, Mohd Shukuri |
| 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 |
| collection | UPM |
| 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. |
| first_indexed | 2024-03-06T11:00:53Z |
| format | Article |
| id | upm.eprints-95190 |
| institution | Universiti Putra Malaysia |
| last_indexed | 2024-03-06T11:00:53Z |
| publishDate | 2021 |
| publisher | MDPI AG |
| record_format | dspace |
| spelling | 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 |
| 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 |
| title | 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_short | Structure-function and industrial relevance of bacterial aminopeptidase P |
| title_sort | structure function and industrial relevance of bacterial aminopeptidase p |
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