MOLECULAR EVOLUTION AND ZINC ION BINDING MOTIF OF LEUKOTRIENE-A4 HYDROLASE

被引：40

作者：

TOH, H ^{[1
]}

MINAMI, M ^{[1
]}

SHIMIZU, T ^{[1
]}

机构：

[1] UNIV TOKYO,FAC MED,DEPT PHYSIOL CHEM & NUTR,TOKYO 113,JAPAN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1990年 / 171卷 / 01期

关键词：

D O I：

10.1016/0006-291X(90)91379-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Leukotriene A4 (LTA4) hydrolase belongs to the aminopeptidase N family. In order to investigate the molecular evolution and physiological significance of LTA4 hydrolase, the enzymes belonging to the family were aligned and a phylogenetic tree was constructed. From the alignment, it was found that three residues involved in zinc binding and one residue of the active sites of aminopeptidases N were conserved in LTA4 hydrolase. In agreement with the observation, LTA4hydrolase is a zinc protein as determined by atomic absorption spectroscopy. © 1990.

引用

页码：216 / 221

页数：6

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