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Insights into Enzymic Catalysis from Studies on Dihydrofolate Reductases

Insights into Enzymic Catalysis from Studies on Dihydrofolate Reductases Summary The role of DHFR in the maintenance of cellular DNA has sparked wide interest in the structure and dynamics of this enzyme. Kinetic studies of specific amino acid replacements on the enzyme isolated from E. coli has proved useful in the detailing of hydrophobic and ionic interactions both proximal and distal to the site of chemical transformation (e. g. Phe-31, Leu-54 and Arg-44). Despite the low sequence homology shared by the E. coli and L. easei enzymes, the free energy profiles are surprisingly comparable. This probably is the result of the high degree of structural similarity of the active site surfaces, but the deleterious effects of subtle replacements (e. g. Leu-54-Ile) at strictly conserved amino acids underscore the latters unique role in attaining the required catalytic efficiency for the enzyme. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Pteridines de Gruyter

Insights into Enzymic Catalysis from Studies on Dihydrofolate Reductases

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Publisher
de Gruyter
Copyright
Copyright © 1989 by the
ISSN
0933-4807
eISSN
2195-4720
DOI
10.1515/pteridines.1989.1.1.37
Publisher site
See Article on Publisher Site

Abstract

Summary The role of DHFR in the maintenance of cellular DNA has sparked wide interest in the structure and dynamics of this enzyme. Kinetic studies of specific amino acid replacements on the enzyme isolated from E. coli has proved useful in the detailing of hydrophobic and ionic interactions both proximal and distal to the site of chemical transformation (e. g. Phe-31, Leu-54 and Arg-44). Despite the low sequence homology shared by the E. coli and L. easei enzymes, the free energy profiles are surprisingly comparable. This probably is the result of the high degree of structural similarity of the active site surfaces, but the deleterious effects of subtle replacements (e. g. Leu-54-Ile) at strictly conserved amino acids underscore the latters unique role in attaining the required catalytic efficiency for the enzyme.

Journal

Pteridines – de Gruyter

Published: Feb 1, 1989

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