Mutation of βGln114 to Ala Alters the Stabilities of Allosteric States in Tryptophan Synthase Catalysis-Reference-Cited by-同舟云学术

Mutation of βGln114 to Ala Alters the Stabilities of Allosteric States in Tryptophan Synthase Catalysis

Published:2021-10-01 Issue:42 Volume:60 Page:3173-3186
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Ghosh Rittik K.¹,Hilario Eduardo²,Liu Viktoriia²,Wang Yangyang²,Niks Dimitri¹,Holmes Jacob B.²,Sakhrani Varun V.²,Mueller Leonard J.²^ORCID,Dunn Michael F.¹

Affiliation:

1. Department of Biochemistry, University of California, Riverside, California 92521, United States

2. Department of Chemistry, University of California, Riverside, California 92521, United States

Funder

Division of Chemistry

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.1c00383

Reference66 articles.

1. A genomic overview of pyridoxal‐phosphate‐dependent enzymes

2. Synthesis and Characterization of Allosteric Probes of Substrate Channeling in the Tryptophan Synthase Bienzyme Complex,

3. Tryptophan Synthase: Structure, Function, and Subunit Interaction

4. On the nature of allosteric transitions: A plausible model

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