Electrostatic interactions dominate the catalytic contribution of arg39 in 4-oxalocrotonate tautomerase

Norman Metanis; Ashraf Brik; Philip E Dawson; Ehud Keinan

doi:10.1021/ja0463841

Electrostatic interactions dominate the catalytic contribution of arg39 in 4-oxalocrotonate tautomerase

J Am Chem Soc. 2004 Oct 13;126(40):12726-7. doi: 10.1021/ja0463841.

Authors

Norman Metanis¹, Ashraf Brik, Philip E Dawson, Ehud Keinan

Affiliation

¹ Department of Chemistry and Institute of Catalysis Science and Technology, Technion-Israel Institute of Technology, Technion City, Haifa 32000 Israel.

PMID: 15469238
DOI: 10.1021/ja0463841

Abstract

The synthesis and kinetic parameters of a comprehensive set of 4-OT analogues with arginine (X = NH2+) to citrulline (X = O) substitutions at positions 11, 39, and 61 are reported. These data suggest that the main contribution of Arg39' ' to catalysis is by electrostatic stabilization of the anionic transition state leading to intermediate 2, and not by hydrogen bonding.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

Amino Acid Substitution
Arginine / chemistry*
Arginine / metabolism*
Catalysis
Circular Dichroism
Citrulline / chemistry
Citrulline / metabolism
Isomerases / chemistry*
Isomerases / metabolism*
Kinetics
Protein Folding
Static Electricity

Substances

Citrulline
Arginine
4-oxalocrotonate tautomerase
Isomerases