Divergent evolution in the enolase superfamily: the interplay of mechanism and specificity

被引：164

作者：

Gerlt, JA ^{[1
]}

Babbitt, PC

Rayment, I

机构：

[1] Univ Illinois, Dept Biochem, Urbana, IL 61801 USA

[2] Univ Illinois, Dept Chem, Urbana, IL 61801 USA

[3] Univ Calif San Francisco, Dept Biopharmaceut Sci, San Francisco, CA 94143 USA

[4] Univ Calif San Francisco, Dept Pharmaceut Chem, San Francisco, CA 94143 USA

[5] Univ Wisconsin, Dept Biochem, Madison, WI 53705 USA

来源：

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | 2005年 / 433卷 / 01期

关键词：

enolase superfamily; divergent evolution;

D O I：

10.1016/j.abb.2004.07.034

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：

The members of the mechanistically diverse enolase superfamily catalyze different overall reactions. Each shares a partial reaction in which an active site base abstracts the alpha-proton of the carboxylate substrate to generate an enolate anion intermediate that is stabilized by coordination to the essential Mg2+ ion; the intermediates are then directed to different products in the different active sites. In this minireview, our current understanding of structure/function relationships in the divergent members of the superfamily is reviewed, and the use of this knowledge for our future studies is proposed. (C) 2004 Published by Elsevier Inc.

引用

页码：59 / 70

页数：12

共 53 条

[1] The structure of 3-methylaspartase from Clostridium tetanomorphum functions via the common enolase chemical step
Asuncion, M
Blankenfeldt, W
Barlow, JN
Gani, D
Naismith, JH
[J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (10) : 8306 - 8311
[2] FUNCTIONALLY DIVERSE ENZYME SUPERFAMILY THAT ABSTRACTS THE ALPHA-PROTONS OF CARBOXYLIC-ACIDS
BABBITT, PC
MRACHKO, GT
HASSON, MS
HUISMAN, GW
KOLTER, R
RINGE, D
PETSKO, GA
KENYON, GL
GERLT, JA
[J]. SCIENCE, 1995, 267 (5201) : 1159 - 1161
[3] The enolase superfamily: A general strategy for enzyme-catalyzed abstraction of the alpha-protons of carboxylic acids
Babbitt, PC
Hasson, MS
Wedekind, JE
Palmer, DRJ
Barrett, WC
Reed, GH
Rayment, I
Ringe, D
Kenyon, GL
Gerlt, JA
[J]. BIOCHEMISTRY, 1996, 35 (51) : 16489 - 16501
[4] Understanding enzyme superfamilies - Chemistry as the fundamental determinant in the evolution of new catalytic activities
Babbitt, PC
Gerlt, JA
[J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (49) : 30591 - 30594
[5] BABBITT PC, UNPUB
[6] Mandelate racemase in pieces: Effective concentrations of enzyme functional groups in the transition state
Bearne, SL
Wolfenden, R
[J]. BIOCHEMISTRY, 1997, 36 (07) : 1646 - 1656
[7] UTILIZATION OF D-GALACTONATE AND D-2-OXO-3-DEOXYGALACTONATE BY ESCHERICHIA-COLI-K-12 - BIOCHEMICAL AND GENETIC STUDIES
COOPER, RA
[J]. ARCHIVES OF MICROBIOLOGY, 1978, 118 (02) : 199 - 206
[8] DEUTERIUM-GALACTONATE UTILIZATION BY ENTERIC BACTERIA - CATABOLIC PATHWAY IN ESCHERICHIA-COLI
DEACON, J
COOPER, RA
[J]. FEBS LETTERS, 1977, 77 (02) : 201 - 205
[9] Evolution of enzymatic activities in the enolase superfamily:: Crystal structure of (D)-glucarate dehydratase from Pseudomonas putida
Gulick, AM
Palmer, DRJ
Babbitt, PC
Gerlt, JA
Rayment, I
[J]. BIOCHEMISTRY, 1998, 37 (41) : 14358 - 14368
[10] Evolution of enzymatic activities in the enolase superfamily:: Crystallographic and mutagenesis studies of the reaction catalyzed by D-glucarate dehydratase from Escherichia coli
Gulick, AM
Hubbard, BK
Gerlt, JA
Rayment, I
[J]. BIOCHEMISTRY, 2000, 39 (16) : 4590 - 4602

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