THE SUBUNIT INTERFACES OF OLIGOMERIC ENZYMES ARE CONSERVED TO A SIMILAR EXTENT TO THE OVERALL PROTEIN SEQUENCES

被引：61

作者：

GRISHIN, NV ^{[1
]}

PHILLIPS, MA ^{[1
]}

机构：

[1] UNIV TEXAS,SW MED CTR,DEPT PHARMACOL,DALLAS,TX 75230

来源：

PROTEIN SCIENCE | 1994年 / 3卷 / 12期

关键词：

MOLECULAR EVOLUTION; OLIGOMERIC ENZYME; SUBUNIT INTERFACE;

D O I：

10.1002/pro.5560031231

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：

It is well established that, within families of homologous enzymes, amino acid residues that are involved in the chemistry of the reaction are highly conserved. To determine if residues at the subunit interface of oligomeric enzymes with shared active sites are also conserved, comparative analysis of five enzyme families was undertaken. For the chosen enzyme families, sequence data were available for a large number of proteins and a three-dimensional structure was known for at least two members of each family. The analysis indicates that the subunit interface and the hydrophobic core of proteins from all five families have diverged to a similar extent to the overall protein sequences.

引用

页码：2455 / 2458

页数：4

共 33 条

[31] X-RAY STRUCTURE OF LIPOAMIDE DEHYDROGENASE FROM AZOTOBACTER-VINELANDII DETERMINED BY A COMBINATION OF MOLECULAR AND ISOMORPHOUS REPLACEMENT TECHNIQUES [J].