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Function and structure relationships of a β‐1,2‐glucooligosaccharide‐degrading β‐glucosidase
Author(s) -
Ishiguro Rikuto,
Tanaka Nobukiyo,
Abe Koichi,
Nakajima Masahiro,
Maeda Takuma,
Miyanaga Akimasa,
Takahashi Yuta,
Sugimoto Naohisa,
Nakai Hiroyuki,
Taguchi Hayao
Publication year - 2017
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12911
Subject(s) - moiety , mutant , chemistry , bacteroides thetaiotaomicron , stereochemistry , hydrogen bond , biochemistry , biology , bacteroides , bacteria , genetics , molecule , organic chemistry , gene
BT _3567 protein, a putative β‐glucosidase from Bacteroides thetaiotaomicron , exhibits higher activity toward Sop 3–5 (Sop n , n: degree of polymerization of β‐1,2‐glucooligosaccharides) than toward Sop 2 , unlike a known β‐glucosidase from Listeria innocua which predominantly prefers Sop 2 . In the complex structure determined by soaking of a D286N mutant crystal with Sop 4 , a Sop 3 moiety was observed at subsites −1 to +2. The glucose moiety at subsite +2 forms a hydrogen bond with Asn81, which is replaced with Gly in the L. innocua β‐glucosidase. The K m values of the N81G mutant for Sop 3–5 are much higher than those of the wild‐type, suggesting that Asn81 contributes to the binding to substrates longer than Sop 3 .