The TIM-barrel fold: a versatile framework for efficient enzymes

被引：339

作者：

Wierenga, RK ^{[1
]}

机构：

[1] Univ Oulu, Bioctr, Oulu, Finland

[2] Univ Oulu, Dept Biochem, Oulu, Finland

来源：

FEBS LETTERS | 2001年 / 492卷 / 03期

关键词：

enolase; evolution; HisA; triosephosphate isomerase; TrpF; protein design;

D O I：

10.1016/S0014-5793(01)02236-0

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：

Recent studies on triosephosphate isomerase (TIM)-barrel enzymes highlight the remarkable versatility of the TIM-barrel scaffold. At least 15 distinct enzyme families use this framework to generate the appropriate active site geometry, always at the C-terminal end of the eight parallel beta -strands of the barrel. Sequence and structure comparisons now suggest that many of the TIM-barrel enzymes are evolutionarily related. Common structural properties of TIM-barrel enzymes are discussed. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：193 / 198

页数：6

共 49 条

[1] RETRACTED: Directed evolution of new catalytic activity using the α/β-barrel scaffold (Retracted article. See vol 417, pg 468, 2002) [J].