Crystal Structures of Wild-Type and F448A Mutant Citrobacter freundii Tyrosine Phenol-Lyase Complexed with a Substrate and Inhibitors: Implications for the Reaction Mechanism-Reference-Cited by-同舟云学术

Crystal Structures of Wild-Type and F448A Mutant Citrobacter freundii Tyrosine Phenol-Lyase Complexed with a Substrate and Inhibitors: Implications for the Reaction Mechanism

Published:2018-09-27 Issue:43 Volume:57 Page:6166-6179
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Phillips Robert S.^ORCID,Craig Steven

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.8b00724

Reference35 articles.

1. Tyrosine Phenol Lyase

2. Syntheses of l-Tyrosine-Related Amino Acids by Tyrosine Phenol-lyase of Citrobacter intermedius

3. 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

4. Mechanistic deductions from kinetic isotope effects and pH studies of pyridoxal phosphate dependent carbon-carbon lyases: Erwinia herbicola and Citrobacter freundii tyrosine phenol-lyase

5. Stereochemistry and Mechanism of Reactions Catalyzed by Tyrosine Phenol-Lyase from Escherichia intermedia

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