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Kang, Yue-Gyu The Korean Society of Plant Pathology 2000 Plant Pathology Journal Vol.16 No.4
In disease surveys from 1986 ti 1998, disease incidence of tobacco black shank was gradually increased in burley tobacco from 1996. To study the causes of the disease occurrence, one hundred and fourteen isolates of Phytophthora parasitica var. nicotianae (Ppn) were collected from burley tobacco-growing areas in the southern part of Korea during 1996-1997, and tested in vitro for meatlaxyl sensitivity which was determined by measuring the mycelial growth on corn meal agar (CMA) amended with metalaxyl. Of the tested isolates, 78.1% showed sensitive to metalaxyl, having $\textrm{ED}_{50}$ values less than 1.0 $\mu\textrm{g}/$\textrm{ml}, while 1.7% was resistant weth $\textrm{ED}_{50}$ greater than 100 $\mu\textrm{g}/$\textrm{ml}. Ppn isolates from three provinces, Chungnam, Chonbuk and Chonnam showed similar distributions of metalaxyl sensitivity. Metalaxyl-resistant isolates were not significantly different from metalaxyl-sensitive ones in mycelial growth rate, chlamydospore formation capacity and size of the spore, and pathogenicity on tobacco plant (cv. Burley 21). These results suggest that the metalaxyl-resistant Ppn in burley tobacco may be one of the major factors to cause the higher occurrence of the tobacco black shank in the burley tobacco-growing area.
( Hyun Gyu Choi ),( Yu Mi Park ),( Yue Lu ),( Hyeun Wook Chang ),( Minkyun Na ),( Seung Ho Lee ) 영남대학교 약품개발연구소 2014 영남대학교 약품개발연구소 연구업적집 Vol.24 No.0
The stem and root barks of Ulmus davidiana var. japonica (Ulmaceae) have been used to treat inflammatory diseases including mastitis, rhinitis, sinusitis, and enteritis. In an ongoing study focused on the discovery of natural anti-inflammatory compounds from natural products, a methanol extract of the stem and root barks of U. davidiana var. japonica showed anti-inflammatory activities. Activity-guided fractionation of the methanol extract yielded a new trihydroxy fatty acid, 9,12,13-trihydroxyoctadeca-10(Z),15(Z)-dienoic acid (1), and a known compound, pinellic acid (2). These two trihydroxy fatty acids 1 and 2 inhibited prostaglandin D₂ production with IC values of 25.8 and 40.8μM, respectively. These results suggest that 9,12,13-trihydroxyoctadeca-10(Z),15(Z)-dienoic acid (1) and pinellic acid (2) are among the anti-inflammatory principles in this medicinal plant. Copyright ⓒ 2012 John Wiley & Sons, Ltd.
Xiong, Shang-Ling,Lim, Gyu Tae,Yin, Shang-Jun,Lee, Jinhyuk,Si, Yue-Xiu,Yang, Jun-Mo,Park, Yong-Doo,Qian, Guo-Ying Elsevier 2019 INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES Vol.121 No.-
<P><B>Abstract</B></P> <P>Pyrogallol is naturally found in aquatic plant and has been proposed as a substrate of tyrosinase. In this study, we evaluated the dual effect of pyrogallol on tyrosinase as an inhibitor in the presence of L‑DOPA simultaneously via integrating methods of enzyme kinetics and computational molecular dynamics (MD) simulations. Pyrogallol was found to be a reversible inhibitor of tyrosinase in the presence of L‑DOPA and its induced mechanism was the parabolic non-competitive inhibition type (<I>IC</I> <SUB>50</SUB> = 0.772 ± 0.003 mM and <I>K</I> <SUB>i</SUB> = 0.529 ± 0.022 mM). Kinetic measurements by real-time interval assay showed that pyrogallol induced rapid inactivation process composing with slight activations at the low dose. Spectrofluorimetry studies showed that pyrogallol mainly induced regional changes in the active site of tyrosinase accompanying with hydrophobic disruption at high dose. The computational MD simulations further revealed that pyrogallol could interact with several residues near the tyrosinase active site pocket such as HIS61, HIS85, HIS259, ASN260, HIS263, VAL283, and ALA296. Our study provides insight into the mechanism by which hydroxyl group composing pyrogallol inhibit tyrosinase and pyrogallol is a potential natural anti-pigmentation agent.</P>
Zheng, Li,Lee, Jinhyuk,Yue, Li-Mei,Lim, Gyu Tae,Yang, Jun-Mo,Ye, Zhuo-Ming,Park, Yong-Doo Elsevier 2018 International journal of biological macromolecules Vol.112 No.-
<P><B>Abstract</B></P> <P>In this study we conducted serial kinetic studies integrated with computational simulations to judge the inhibitory effect of pyrogallol on α-glucosidase, due to the association between this enzyme and the treatment of type 2 diabetes. As a result, we found that pyrogallol bound to the active site of α-glucosidase, interacting with several key residues, such as ASP68, MET69, TYR71, PHE157, PHE158, PHE177, GLN181, HIS348, ASP349, ASP406, VAL407, ASP408, ARG439, and ARG443, which was predicted by performing a protein-ligand docking simulation. Subsequently, we evaluated the inhibitory effect of pyrogallol on α-glucosidase, and found that it induced a mixed type of inhibition in a reversible and quick-binding manner. The relevant kinetic parameters were evaluated to be: <I>IC</I> <SUB>50</SUB> =0.72±0.051mM; <I>K</I> <SUB>i</SUB> =0.37±0.018mM. A tertiary conformational change was synchronized with pyrogallol inhibition and modulation of the shape of the active site was correspondingly observed. Our study provides insight into the functional inhibitory role of pyrogallol, which results from its triple-hydroxyl groups interacting with the active site of α-glucosidase. We suggest that compounds similar to pyrogallol (phenolic hydroxyl compounds) which target the key residues of the active site of α-glucosidase could be potential agents for α-glucosidase inhibition.</P>
Xiong, Shang-Ling,Yue, Li-Mei,Lim, Gyu Tae,Yang, Jun-Mo,Lee, Jinhyuk,Park, Yong-Doo Elsevier 2018 INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES Vol.113 No.-
<P><B>Abstract</B></P> <P>Inhibition of α-glucosidase is directly associated with treatment of type 2 diabetes. In this regard, we conducted enzyme kinetics integrated with computational docking simulation to assess the inhibitory effect of raspberry ketone (RK) on α-glucosidase. RK bound to the active site of α-glucosidase and interacted with several key residues such as ASP68, TYR71, HIS111, PHE157, PHE158, PHE177, GLN181, ASP214, THR215, ASP349, ASP408, and ARG439, as detected by protein-ligand docking simulation. Subsequently, we confirmed the action of RK on α-glucosidase as the non-competitive type of inhibition in a reversible and rapidly binding manner. The relevant kinetic parameters were <I>IC</I> <SUB>50</SUB> =6.17±0.46mM and <I>K</I> <SUB> <I>i</I> </SUB> =7.939±0.211mM. Regarding the structure-activity relationship, the higher concentration of RK induced slight modulation of the shape of the active site as monitored by hydrophobic exposure. The tertiary conformational change was linked to RK inhibition, and mostly involved regional changes of the active site. Our study provides insight into the functional role of RK due to its structural property of a hydroxyphenyl ring that interacts with the active site of α-glucosidase. We suggest that similar hydroxyphenyl ring compounds targeting the key residues of the active site might be potential α-glucosidase inhibitors.</P>