PROTEIN MOTIFS .4. THE STRUCTURE AND EVOLUTION OF ALPHA/BETA BARREL PROTEINS

被引：156

作者：

REARDON, D

FARBER, GK

机构：

[1] Department of Biochemistry, Pennsylvania State University, University Park

[2] Department of Biochemistry, 108 Althouse Laboratory, Pennsylvania State University, University Park

来源：

FASEB JOURNAL | 1995年 / 9卷 / 07期

关键词：

TIM BARREL; MOLECULAR EVOLUTION;

D O I：

10.1096/fasebj.9.7.7737457

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：

Roughly 10% of all known enzyme structures have an alpha/beta barrel domain. The members of this large family of proteins catalyze very different types of reactions. Such diversity of function has made this family a target for protein engineering. The evolutionary history of this family has been the subject of vigorous debate. In this paper, arguments are made to support the divergence of all members of this family from a common ancestor. Because of the lack of strong sequence homology, the ancestral molecule must be very old. A hypothesis concerning the relationship between chemical mechanism and evolutionary history is discussed. Evidence is presented to suggest that convergent molecular evolution occurs when there is only one energetically reasonable pathway for a chemical reaction.

引用

页码：497 / 503

页数：7

共 42 条

[1] ISOTOPIC EXCHANGE PLUS SUBSTRATE AND INHIBITION-KINETICS OF D-XYLOSE ISOMERASE DO NOT SUPPORT A PROTON-TRANSFER MECHANISM [J].