Is chorismate mutase a prototypic entropy trap? Activation parameters for the Bacillus subtilis enzyme

被引:105
作者
Kast, P
AsifUllah, M
Hilvert, D
机构
[1] Scripps Res Inst, DEPT CHEM, LA JOLLA, CA 92037 USA
[2] SCRIPPS RES INST, DEPT MOLEC BIOL, LA JOLLA, CA 92037 USA
基金
美国国家卫生研究院;
关键词
D O I
10.1016/0040-4039(96)00338-3
中图分类号
O62 [有机化学];
学科分类号
070303 ; 081704 ;
摘要
Chorismate mutase is thought to accelerate the chorismate-to-prephenate rearrangement in part by significantly lowering the entropy barrier for the reaction. We have determined the activation parameters for the well-characterized Bacillus subtilis chorismate mutase and find that Delta S double dagger (-9.1 +/- 1.2 eu) is nearly as unfavorable as the activation entropy for the uncatalyzed process. Our results suggest that chorismate mutase catalysts show greater mechanistic versatility than commonly believed. Copyright (C) 1996 Elsevier Science Ltd.
引用
收藏
页码:2691 / 2694
页数:4
相关论文
共 30 条
[1]   SECONDARY TRITIUM ISOTOPE EFFECTS AS PROBES OF THE ENZYMIC AND NON-ENZYMIC CONVERSION OF CHORISMATE TO PREPHENATE [J].
ADDADI, L ;
JAFFE, EK ;
KNOWLES, JR .
BIOCHEMISTRY, 1983, 22 (19) :4494-4501
[2]   TRANSITION-STATE STABILIZATION AND ENZYMIC CATALYSIS - KINETIC AND MOLECULAR-ORBITAL STUDIES OF REARRANGEMENT OF CHORISMATE TO PREPHENATE [J].
ANDREWS, PR ;
SMITH, GD ;
YOUNG, IG .
BIOCHEMISTRY, 1973, 12 (18) :3492-3498
[3]   REARRANGEMENT OF CHORISMATE TO PREPHENATE - USE OF CHORISMATE MUTASE INHIBITORS TO DEFINE TRANSITION-STATE STRUCTURE [J].
ANDREWS, PR ;
CAIN, EN ;
RIZZARDO, E ;
SMITH, GD .
BIOCHEMISTRY, 1977, 16 (22) :4848-4852
[4]   CONTROLLABLE ALTERATION OF CELL GENOTYPE IN BACTERIAL CULTURES USING AN EXCISION VECTOR [J].
BALAKRISHNAN, R ;
BACKMAN, K .
GENE, 1988, 67 (01) :97-103
[5]   BINDING OF A HIGH-ENERGY SUBSTRATE CONFORMER IN ANTIBODY CATALYSIS [J].
CAMPBELL, AP ;
TARASOW, TM ;
MASSEFSKI, W ;
WRIGHT, PE ;
HILVERT, D .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1993, 90 (18) :8663-8667
[6]   CRYSTAL-STRUCTURES OF THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS-SUBTILIS AND ITS COMPLEX WITH A TRANSITION-STATE ANALOG [J].
CHOOK, YM ;
KE, HM ;
LIPSCOMB, WN .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1993, 90 (18) :8600-8603
[7]   THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS-SUBTILIS - STRUCTURE DETERMINATION OF CHORISMATE MUTASE AND ITS COMPLEXES WITH A TRANSITION-STATE ANALOG AND PREPHENATE, AND IMPLICATIONS FOR THE MECHANISM OF THE ENZYMATIC-REACTION [J].
CHOOK, YM ;
GRAY, JV ;
KE, HM ;
LIPSCOMB, WN .
JOURNAL OF MOLECULAR BIOLOGY, 1994, 240 (05) :476-500
[8]  
CONNELLY JA, 1987, METHOD ENZYMOL, V142, P422
[9]  
Connors K. A., 1990, CHEM KINETICS STUDY, P187
[10]   THE UNCATALYZED CLAISEN REARRANGEMENT OF CHORISMATE TO PREPHENATE PREFERS A TRANSITION-STATE OF CHAIRLIKE GEOMETRY [J].
COPLEY, SD ;
KNOWLES, JR .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1985, 107 (18) :5306-5308