Linkage between dynamics and catalysis in a thermophilic-mesophilic enzyme pair.

Abstract:

:A fundamental question is how enzymes can accelerate chemical reactions. Catalysis is not only defined by actual chemical steps, but also by enzyme structure and dynamics. To investigate the role of protein dynamics in enzymatic turnover, we measured residue-specific protein dynamics in hyperthermophilic and mesophilic homologs of adenylate kinase during catalysis. A dynamic process, the opening of the nucleotide-binding lids, was found to be rate-limiting for both enzymes as measured by NMR relaxation. Moreover, we found that the reduced catalytic activity of the hyperthermophilic enzyme at ambient temperatures is caused solely by a slower lid-opening rate. This comparative and quantitative study of activity, structure and dynamics revealed a close link between protein dynamics and catalytic turnover.

journal_name

Nat Struct Mol Biol

authors

Wolf-Watz M,Thai V,Henzler-Wildman K,Hadjipavlou G,Eisenmesser EZ,Kern D

doi

10.1038/nsmb821

keywords:

subject

Has Abstract

pub_date

2004-10-01 00:00:00

pages

945-9

issue

10

eissn

1545-9993

issn

1545-9985

pii

nsmb821

journal_volume

11

pub_type

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