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• W2918137312 endingPage "44" @default.
• W2918137312 startingPage "37" @default.
• W2918137312 abstract "2-Hydroxy acid dehydrogenases (2-HADHs) have been implicated in the synthesis of 2-hydroxy acids from 2-oxo acids that are used in wide areas of industry. d-lactate dehydrogenases (d-LDHs), a subfamily of 2-HADH, have been utilized to this purpose, yet they exhibited relatively low catalytic activity to the 2-oxo acids with large functional groups at C3. In this report, four putative 2-HADHs from Oenococcus oeni, Weissella confusa, Weissella koreensis and Pediococcus claussenii were examined for activity on phenylpyruvate (PPA), a substrate to 3-phenyllactic acid (PLA) with a C3 phenyl group. The 2-HADH from P. claussenii was found to have the highest kcat/Km on PPA with 1,348.03 s−1 mM−1 among the four enzymes with higher substrate preference for PPA than pyruvate. Sequential, structural and mutational analysis of the enzyme revealed that it belonged to the d-LDH family, and phenylalanine at the position 51 was the key residue for the PPA binding to the active site via hydrophobic interaction, whereas in the 2-HADHs from O. oeni and W. confusa the hydrophilic tyrosine undermined the interaction. Because phenyllactate is a potential precursor for pharmaceutical compounds, antibiotics and biopolymers, the enzyme could increase the efficiency of bio-production of valuable chemicals. This study suggests a structural basis for the high substrate preference of the 2-HADH, and further engineering possibilities to synthesize versatile 2-hydroxy acids." @default.
• W2918137312 created "2019-03-02" @default.
• W2918137312 creator A5003715831 @default.
• W2918137312 creator A5057591539 @default.
• W2918137312 creator A5062892784 @default.
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• W2918137312 date "2019-06-01" @default.
• W2918137312 modified "2023-10-18" @default.
• W2918137312 title "A novel d-2-hydroxy acid dehydrogenase with high substrate preference for phenylpyruvate originating from lactic acid bacteria: Structural analysis on the substrate specificity" @default.
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• W2918137312 doi "https://doi.org/10.1016/j.enzmictec.2019.02.008" @default.
• W2918137312 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30885323" @default.
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