M379A Mutant Tyrosine Phenol‐lyase from <i>Citrobacter freundii</i> Has Altered Conformational Dynamics-Reference-Cited by-同舟云学术

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M379A Mutant Tyrosine Phenol‐lyase from Citrobacter freundii Has Altered Conformational Dynamics

Published:2022-05-24 Issue:13 Volume:23 Page:
ISSN:1439-4227
Container-title:ChemBioChem
language:en
Short-container-title:ChemBioChem

Author:

Phillips Robert S.¹²^ORCID,Jones Benjamin³,Nash Sarah⁴

Affiliation:

1. Department of Chemistry University of Georgia Athens Georgia 30602 USA

2. Department of Biochemistry and Molecular Biology University of Georgia Athens Georgia 30602 USA

3. Department of Biological Engineering University of Georgia Athens Georgia 30602 USA

4. Department of Biology University of Georgia Athens Georgia 30602 USA

Funder

National Institute of General Medical Sciences

Publisher

Wiley

Subject

Organic Chemistry,Molecular Biology,Molecular Medicine,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/cbic.202200028

Reference36 articles.

1. Tyrosine Phenol Lyase

2. Reactions of O-acyl-l-serines with tryptophanase, tyrosine phenol-lyase, and tryptophan synthase

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. Enzymatic preparation of L-tyrosine and 3,4-dihydroxyphenyl-L-alanine

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

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