Cryoenzymology: enzyme action in slow motion.

Abstract:

:Knowledge of the existence and structure of intermediates on the reaction pathway is necessary before specific details of the mechanism may be successfully resolved. However, enzymatic catalysis is an extremely fast process. This rapidity of enzyme-catalyzed reactions and the short life times of intermediates represent a major problem in studying the dynamic processes which occur during catalysis, as they prevent the accumulation of intermediates under normal conditions for concentrations and time periods required by most high-resolution structural methods. Therefore, a method that would utilize specific substrates but would permit the detection and characterization of intermediates was highly desired. As one of the approaches to overcome this problem the use of cryoenzymology to allow the accumulation and stabilization of intermediates at very low temperatures was proposed. This review describes the contribution of Prof. Anthony L. Fink to cryoenzymology and shows how his work shaped this exciting area.

journal_name

Curr Protein Pept Sci

authors

Dunn BM,Uversky VN

doi

10.2174/138920309789351958

subject

Has Abstract

pub_date

2009-10-01 00:00:00

pages

408-15

issue

5

eissn

1389-2037

issn

1875-5550

pii

CPPS-7

journal_volume

10

pub_type

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