Abstract
Various aminopeptidases belong to the M1 aminopeptidase family. They are all zinc dependent enzymes playing important roles in several biological processes such as regulation of blood pressure under both physiological and pathological conditions, and the angiogenesis and metastasis of tumor, etc. They all have the highly conserved HEXXH(X)18E zinc-binding and GAMEN motifs essential for enzyme activities. In this review, the current situation regarding the biochemical characteristics, biological functions and inhibitors of three important members of these enzymes, aminopeptidase A, aminopeptidase N and aminopeptidase B are summarized.
Keywords: aminopeptidase A, aminopeptidase B, aminopeptidase N, renin–angiotensin system, hypertension, angiogenesis, metastasis.
Current Protein & Peptide Science
Title:The Characteristics, Functions and Inhibitors of Three Aminopeptidases Belonging to the M1 Family
Volume: 13 Issue: 5
Author(s): Yepeng Luan, Chunhua Ma, Yan Wang, Hao Fang and Wenfang Xu
Affiliation:
Keywords: aminopeptidase A, aminopeptidase B, aminopeptidase N, renin–angiotensin system, hypertension, angiogenesis, metastasis.
Abstract: Various aminopeptidases belong to the M1 aminopeptidase family. They are all zinc dependent enzymes playing important roles in several biological processes such as regulation of blood pressure under both physiological and pathological conditions, and the angiogenesis and metastasis of tumor, etc. They all have the highly conserved HEXXH(X)18E zinc-binding and GAMEN motifs essential for enzyme activities. In this review, the current situation regarding the biochemical characteristics, biological functions and inhibitors of three important members of these enzymes, aminopeptidase A, aminopeptidase N and aminopeptidase B are summarized.
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Cite this article as:
Luan Yepeng, Ma Chunhua, Wang Yan, Fang Hao and Xu Wenfang, The Characteristics, Functions and Inhibitors of Three Aminopeptidases Belonging to the M1 Family, Current Protein & Peptide Science 2012; 13 (5) . https://dx.doi.org/10.2174/138920312802430554
DOI https://dx.doi.org/10.2174/138920312802430554 |
Print ISSN 1389-2037 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5550 |
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