How can enzymes be so efficient?

被引：32

作者：

Williams, DH ^{[1
]}

Stephens, E ^{[1
]}

Zhou, M ^{[1
]}

机构：

[1] Univ Cambridge, Dept Chem, Cambridge CB2 1EW, England

来源：

CHEMICAL COMMUNICATIONS | 2003年 / 16期

关键词：

D O I：

10.1039/b305544m

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Dudley nWilliams and his colleagues discuss how ligands can gain binding energy to their receptors, and substrate transition states to their enzymes, by tightening the protein structures, with a decrease in their dynamic behaviour.

引用

页码：1973 / 1976

页数：4

共 19 条

[1] An illustration of the expression of cooperative binding energy in arrays of non-covalent interactions [J].

Bardsley, B ;

Williams, DH .

CHEMICAL COMMUNICATIONS, 1998, (21) :2305-2306

[2] THE DEVELOPMENT OF A SIMPLE EMPIRICAL SCORING FUNCTION TO ESTIMATE THE BINDING CONSTANT FOR A PROTEIN LIGAND COMPLEX OF KNOWN 3-DIMENSIONAL STRUCTURE [J].

BOHM, HJ .

JOURNAL OF COMPUTER-AIDED MOLECULAR DESIGN, 1994, 8 (03) :243-256

[3] Direct measurement of the uncatalyzed rate of hydrolysis of a peptide bond [J].

Bryant, RAR ;

Hansen, DE .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1996, 118 (23) :5498-5499

[4] Structural studies of the streptavidin binding loop [J].

Freitag, S ;

LeTrong, I ;

Klumb, L ;

Stayton, PS ;

Stenkamp, RE .

PROTEIN SCIENCE, 1997, 6 (06) :1157-1166

[5] The maximal affinity of ligands [J].

Kuntz, ID ;

Chen, K ;

Sharp, KA ;

Kollman, PA .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (18) :9997-10002

[6] The stereochemical mechanism of the cooperative effects in hemoglobin revisited [J].

Perutz, MF ;

Wilkinson, AJ ;

Paoli, M ;

Dodson, GG .

ANNUAL REVIEW OF BIOPHYSICS AND BIOMOLECULAR STRUCTURE, 1998, 27 :1-34

[7] Rates of uncatalyzed peptide bond hydrolysis in neutral solution and the transition state affinities of proteases [J].

Radzicka, A ;

Wolfenden, R .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1996, 118 (26) :6105-6109

[8] A PROFICIENT ENZYME [J].

RADZICKA, A ;

WOLFENDEN, R .

SCIENCE, 1995, 267 (5194) :90-93

[9] Temperature effects on the catalytic efficiency, rate enhancement, and transition state affinity of cytidine deaminase, and the thermodynamic consequences for catalysis of removing a substrate "anchor" [J].

Snider, MJ ;

Gaunitz, S ;

Ridgway, C ;

Short, SA ;

Wolfenden, R .

BIOCHEMISTRY, 2000, 39 (32) :9746-9753

[10] The lesser "burden borne" by o-succinylbenzoate synthase:: An "easy" reaction involving a carboxylate carbon acid [J].

Taylor, EA ;

Palmer, DRJ ;

Gerlt, JA .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2001, 123 (24) :5824-5825

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