Critical Role of Substrate Conformational Change in the Proton Transfer Process Catalyzed by 4-Oxalocrotonate Tautomerase-Reference-Cited by-同舟云学术

Critical Role of Substrate Conformational Change in the Proton Transfer Process Catalyzed by 4-Oxalocrotonate Tautomerase

Published:2009-02-03 Issue:7 Volume:131 Page:2687-2698
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Ruiz-Pernía J. Javier¹,Garcia-Viloca Mireia¹,Bhattacharyya Sudeep¹,Gao Jiali¹,Truhlar Donald G.¹,Tuñón Iñaki¹

Affiliation:

1. Departament de Química Física, Universitat de València, València 46100, Spain, Institut de Biotecnologia i de Biomedicina and Departament de Química, Universitat Autònoma de Barcelona, Barcelona 08193, Spain, and Department of Chemistry and Supercomputing Institute, University of Minnesota, Minneapolis, Minnesota 55455-0431

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja8087423

Reference101 articles.

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

2. 4-Oxalocrotonate Tautomerase: pH Dependence of Catalysis and pKa Values of Active Site Residues

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

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

5. Physically associated enzymes produce and metabolize 2-hydroxy-2,4-dienoate, a chemically unstable intermediate formed in catechol metabolism via meta cleavage in Pseudomonas putida

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