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Publication Abstract from PubMed

BT_3567 protein, a putative beta-glucosidase from Bacteroides thetaiotaomicron, exhibits higher activity toward Sop3-5 (Sopn , n: degree of polymerization of beta-1,2-glucooligosaccharides) than toward Sop2 , unlike a known beta-glucosidase from Listeria innocua which predominantly prefers Sop2 . In the complex structure determined by soaking of a D286N mutant crystal with Sop4 , a Sop3 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 beta-glucosidase. The Km values of the N81G mutant for Sop3-5 are much higher than those of the wild-type, suggesting that Asn81 contributes to the binding to substrates longer than Sop3 .

Function and structure relationships of a beta-1,2-glucooligosaccharide-degrading beta-glucosidase.,Ishiguro R, Tanaka N, Abe K, Nakajima M, Maeda T, Miyanaga A, Takahashi Y, Sugimoto N, Nakai H, Taguchi H FEBS Lett. 2017 Dec;591(23):3926-3936. doi: 10.1002/1873-3468.12911. Epub 2017, Nov 24. PMID:29131329^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.