Pressure and Temperature Effects on the Formation of Aminoacrylate Intermediates of Tyrosine Phenol-lyase Demonstrate Reaction Dynamics-Reference-Cited by-同舟云学术

Pressure and Temperature Effects on the Formation of Aminoacrylate Intermediates of Tyrosine Phenol-lyase Demonstrate Reaction Dynamics

Published:2019-12-19 Issue:3 Volume:10 Page:1692-1703
ISSN:2155-5435
Container-title:ACS Catalysis
language:en
Short-container-title:ACS Catal.

Author:

Phillips Robert S.¹²^ORCID,Craig Steven²,Kovalevsky Andrey³^ORCID,Gerlits Oksana⁴,Weiss Kevin³^ORCID,Iorgu Andreea I.⁵^ORCID,Heyes Derren J.⁵,Hay Sam⁵^ORCID

Affiliation:

1. Department of Chemistry, University of Georgia, Athens, Georgia 30602 United States

2. Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602, United States

3. Neutron Scattering Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee 37831-6475, United States

4. Tennessee Wesleyan University, Athens, Tennessee 37303, United States

5. Manchester Institute of Biotechnology and Department of Chemistry, The University of Manchester, Manchester M17DN, U.K.

Publisher

American Chemical Society (ACS)

Subject

Catalysis,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acscatal.9b03967

Reference40 articles.

1. Tyrosine Phenol Lyase

2. Synthesis of l-tyrosine from phenol and catalysed by tyrosine phenol-lyase

3. Threonine-124 and phenylalanine-448 in Citrobacter freundii tyrosine phenol-lyase are necessary for activity with l-tyrosine

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. 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

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