A novel d-2-hydroxy acid dehydrogenase with high substrate preference for phenylpyruvate originating from lactic acid bacteria: Structural analysis on the substrate specificity-Reference-Cited by-同舟云学术

A novel d-2-hydroxy acid dehydrogenase with high substrate preference for phenylpyruvate originating from lactic acid bacteria: Structural analysis on the substrate specificity

Published:2019-06 Issue: Volume:125 Page:37-44
ISSN:0141-0229
Container-title:Enzyme and Microbial Technology
language:en
Short-container-title:Enzyme and Microbial Technology

Author:

Lee Hoe-Suk^ORCID,Park Jisu,Yoo Young Je,Yeon Young Joo

Funder

Ministry of Science and ICT

Publisher

Elsevier BV

Subject

Applied Microbiology and Biotechnology,Biochemistry,Biotechnology,Bioengineering

Reference44 articles.

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2. A new chemo-enzymatic route to chiral 2-hydroxy-4-phenylbutyrates by combining lactonase-mediated resolution with hydrogenation over Pd/C;Chen;Chem. Commun. (Camb.),2010

3. Kinetic resolution of 2-hydroxybutanoate racemic mixtures by NAD-independent L-lactate dehydrogenase;Gao;Bioresour. Technol.,2011

4. Highly stereoselective biosynthesis of (R)-alpha-hydroxy carboxylic acids through rationally re-designed mutation of D-lactate dehydrogenase;Zheng;Sci. Rep.,2013

5. Recent research on 3-phenyllactic acid, a broad-spectrum antimicrobial compound;Mu;Appl. Microbiol. Biotechnol.,2012

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