Electrostatic Interactions Dominate the Catalytic Contribution of Arg39 in 4-Oxalocrotonate Tautomerase-Reference-Cited by-同舟云学术

Electrostatic Interactions Dominate the Catalytic Contribution of Arg39 in 4-Oxalocrotonate Tautomerase

Published:2004-09-18 Issue:40 Volume:126 Page:12726-12727
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Metanis Norman¹,Brik Ashraf¹,Dawson Philip E.¹,Keinan Ehud¹

Affiliation:

1. Department of Chemistry and Institute of Catalysis Science and Technology, TechnionIsrael Institute of Technology, Technion City, Haifa 32000 Israel, and Departments of Molecular Biology and Cell Biology and Chemistry and The Skaggs Institute of Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja0463841

Reference19 articles.

1. The 4-oxalocrotonate tautomerase family of enzymes: how nature makes new enzymes using a β–α–β structural motif

2. Chemical and enzymic ketonization of 2-hydroxymuconate, a conjugated enol

3. Kinetic, Stereochemical, and Structural Effects of Mutations of the Active Site Arginine Residues in 4-Oxalocrotonate Tautomerase

4. Ketonization of 2-hydroxy-2,4-pentadienoate by 4-oxalocrotonate tautomerase: implications for the stereochemical course and the mechanism

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