Structure of lactate oxidase from <scp> <i>Enterococcus hirae</i> </scp> revealed new aspects of active site loop function: Product‐inhibition mechanism and oxygen gatekeeper-Reference-Cited by-同舟云学术

Structure of lactate oxidase from Enterococcus hirae revealed new aspects of active site loop function: Product‐inhibition mechanism and oxygen gatekeeper

Published:2022-09-21 Issue:10 Volume:31 Page:
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Hiraka Kentaro¹²^ORCID,Yoshida Hiromi³^ORCID,Tsugawa Wakako¹,Asano Ryutaro¹,La Belle Jeffrey T.²,Ikebukuro Kazunori¹,Sode Koji⁴^ORCID

Affiliation:

1. Department of Biotechnology and Life Science, Graduate School of Engineering Tokyo University of Agriculture and Technology Tokyo Japan

2. College of Science, Engineering and Technology Grand Canyon University Phoenix Arizona USA

3. Department of Basic Life Science, Faculty of Medicine Kagawa University Kagawa Japan

4. Joint Department of Biomedical Engineering The University of North Carolina at Chapel Hill and North Carolina State University Chapel Hill North Carolina USA

Funder

Japan Society for the Promotion of Science

Japan Student Services Organization

Nakatani Foundation for Advancement of Measuring Technologies in Biomedical Engineering

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/pro.4434

Reference70 articles.

1. The 2.1 Å structure ofAerococcus viridansL-lactate oxidase (LOX)

2. Crystallographic study on the interaction of l-lactate oxidase with pyruvate at 1.9 Å resolution

3. L-lactate oxidase and L-lactate monooxygenase: Mechanistic variations on a common structural theme

4. Conformational flexibility related to enzyme activity: evidence for a dynamic active-site gatekeeper function of Tyr215 in Aerococcus viridans lactate oxidase

5. Speeding up the product release: a second-sphere contribution from Tyr191 to the reactivity ofl-lactate oxidase revealed in crystallographic and kinetic studies of site-directed variants

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1. Activation of L-lactate oxidase by the formation of enzyme assemblies through liquid–liquid phase separation;Scientific Reports;2023-01-25