Computational approaches to predict binding interactions between mammalian tyrosinases and (S)-(+)-decursin and its analogues as potent inhibitors

Jung, Sang Won; Lee, Kyeong; Cho, Art E.

doi:10.1039/c6ra09365e

Cited by 3 publications

(1 citation statement)

References 44 publications

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“…Crystal structure alignment and protein 3D structure visualization and editing were performed using PyMOL software (Meng et al, 2016 ). The predicted structural proteins were docked with pyruvate and PPA using Schrodinger software (Jung et al, 2016 ).…”

Section: Methodsmentioning

confidence: 99%

Biological characterization of D‐lactate dehydrogenase responsible for high‐yield production of D‐phenyllactic acid in Sporolactobacillus inulinus

Park

Seong

Kim

et al. 2022

Microbial Biotechnology

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PLA (3‐D‐phenyllactic acid) is an ideal antimicrobial and immune regulatory compound present in honey and fermented foods. Sporolactobacillus inulinus is regarded as a potent D‐PLA producer that reduces phenylpyruvate (PPA) with D‐lactate dehydrogenases. In this study, PLA was produced by whole‐cell bioconversion of S. inulinus ATCC 15538. Three genes encoding D‐lactate dehydrogenase (d‐ldh1, d‐ldh2, and d‐ldh3) were cloned and expressed in Escherichia coli BL21 (DE3), and their biochemical and structural properties were characterized. Consequently, a high concentration of pure D‐PLA (47 mM) was produced with a high conversion yield of 88%. Among the three enzymes, D‐LDH1 was responsible for the efficient conversion of PPA to PLA with kinetic parameters of Km (0.36 mM), kcat (481.10 s−1), and kcat/Km (1336.39 mM−1 s−1). In silico structural analysis and site‐directed mutagenesis revealed that the Ile307 in D‐LDH1 is a key residue for excellent PPA reduction with low steric hindrance at the substrate entrance. This study highlights that S. inulinus ATCC 15538 is an excellent PLA producer, equipped with a highly specific and efficient D‐LDH1 enzyme.

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Section: Methodsmentioning

confidence: 99%

Biological characterization of D‐lactate dehydrogenase responsible for high‐yield production of D‐phenyllactic acid in Sporolactobacillus inulinus

Park

Seong

Kim

et al. 2022

Microbial Biotechnology

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Melanins as Sustainable Resources for Advanced Biotechnological Applications

et al. 2020

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Melanins are a class of biopolymers that are widespread in nature and have diverse origins, chemical compositions, and functions. Their chemical, electrical, optical, and paramagnetic properties offer opportunities for applications in materials science, particularly for medical and technical uses. This review focuses on the application of analytical techniques to study melanins in multidisciplinary contexts with a view to their use as sustainable resources for advanced biotechnological applications, and how these may facilitate the achievement of the United Nations Sustainable Development Goals.

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

Lee

Park

Yoo

et al. 2019

Enzyme and Microbial Technology

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Computational approaches to predict binding interactions between mammalian tyrosinases and (S)-(+)-decursin and its analogues as potent inhibitors

Abstract: Using computational methods, we elucidated the binding modes of (S)-(+)-decursin with mouse and human tyrosinases, and thereby provided insight to new tyrosinase inhibitors.

Cited by 3 publications

References 44 publications

Biological characterization of D‐lactate dehydrogenase responsible for high‐yield production of D‐phenyllactic acid in Sporolactobacillus inulinus

Biological characterization of D‐lactate dehydrogenase responsible for high‐yield production of D‐phenyllactic acid in Sporolactobacillus inulinus

Melanins as Sustainable Resources for Advanced Biotechnological Applications

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

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