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Ligand binding energy and enzyme efficiency from reductions in protein dynamics.

Abstract：

:Tetrameric rabbit muscle glyceraldehyde 3-phosphate dehydrogenase (GAPDH; EC 1.2.1.12) binds successively four molecules of its cofactor (NAD+) with affinities of ca 10(11) M(-1), 10(9) M(-1), 10(7) M(-1), and 10(5) M(-1). The reduction in the dynamics of the protein is greatest upon binding the first NAD+ molecule. Smaller reductions then occur upon binding the second and third NAD+ molecules, and the fourth NAD+ molecule binds without dynamic change. Reduction of the GAPDH dynamics, with consequent improvements in its internal bonding, can account for the increase in NAD+ binding affinity from 10(5) M(-1) to 10(11) M(-1). Evidence is provided that comparable fractions of the binding energy of other ligands, and of the catalytic efficiency of enzymes, may be derived in the same way.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Williams DH,Zhou M,Stephens E

doi

10.1016/j.jmb.2005.11.015

keywords:

subject

Has Abstract

pub_date

2006-01-27 00:00:00

pages

760-7

issue

4

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(05)01401-4

journal_volume

355

pub_type

杂志文章

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