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: | , , , , , |
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| Format: | Article |
| Published: |
MDPI AG
2021
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| Online Access: | http://psasir.upm.edu.my/id/eprint/95190/ https://www.mdpi.com/2073-4344/11/10/1157 |
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