Site-Directed Mutagenesis of Tyrosine-71 to Phenylalanine in Citrobacter freundii Tyrosine Phenol-Lyase: Evidence for Dual Roles of Tyrosine-71 as a General Acid Catalyst in the Reaction Mechanism and in Cofactor Binding-Reference-Cited by-同舟云学术

Site-Directed Mutagenesis of Tyrosine-71 to Phenylalanine in Citrobacter freundii Tyrosine Phenol-Lyase: Evidence for Dual Roles of Tyrosine-71 as a General Acid Catalyst in the Reaction Mechanism and in Cofactor Binding

Published:1995-09-26 Issue:38 Volume:34 Page:12276-12283
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Chen Hao Yuan,Demidkina Tatyana V.,Phillips Robert S.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00038a023

Reference41 articles.

1. Three-dimensional structure of tyrosine phenol-lyase

2. Bemasconi, C. F. (1976) Relaxation Kinetics, pp51-72, Academic Press, New York.

3. Appendix 6. Mass values for amino acid residues in peptides

4. Tyrosine-48 Is the Proton Donor and Histidine-110 Directs Substrate Stereochemical Selectivity in the Reduction Reaction of Human Aldose Reductase: Enzyme Kinetics and Crystal Structure of the Y48H Mutant Enzyme

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