Identification and characterization of extracellular GH3 β-glucosidase from the pink snow mold fungus, Microdochium nivale

被引:0
作者
Ota, Tomoya [1 ]
Saburi, Wataru [1 ]
Jewell, Linda Elizabeth [2 ]
Hsiang, Tom [3 ]
Imai, Ryozo [4 ]
Mori, Haruhide [1 ]
机构
[1] Hokkaido Univ, Res Fac Agr, Sapporo, Japan
[2] Agr & Agrifood Canada, St John, NF, Canada
[3] Univ Guelph, Sch Environm Sci, Guelph, ON, Canada
[4] Natl Agr & Food Res Org, Inst Agrobiol Sci, Tsukuba, Japan
关键词
Microdochium nivale; beta-glucosidase; glycoside hydrolase family 3; substrate specificity; transglucosylation; SUBSTRATE-SPECIFICITY; CRYSTAL-STRUCTURES; GLYCOSIDE; INDUCTION; CELLULASE; ALIGNMENT; BLOOD;
D O I
10.1093/bbb/zbad044
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Glycoside hydrolase family 3 (GH3) beta-glucosidase exists in many filamentous fungi. In phytopathogenic fungi, it is involved in fungal growth and pathogenicity. Microdochium nivale is a severe phytopathogenic fungus of grasses and cereals and is the causal agent of pink snow mold, but its beta-glucosidase has not been identified. In this study, a GH3 beta-glucosidase of M. nivale (MnBG3A) was identified and characterized. Among various p-nitrophenyl beta-glycosides, MnBG3A showed activity on d-glucoside (pNP-Glc) and slight activity on d-xyloside. In the pNP-Glc hydrolysis, substrate inhibition occurred (K-is = 1.6 m m), and d-glucose caused competitive inhibition (K-i = 0.5 m m). MnBG3A acted on beta-glucobioses with beta 1-3, -6, -4, and -2 linkages, in descending order of k(cat)/K-m. In contrast, the regioselectivity for newly formed products was limited to beta 1-6 linkage. MnBG3A has similar features to those of beta-glucosidases from Aspergillus spp., but higher sensitivity to inhibitory effects.
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页码:707 / 716
页数:10
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