Function and structure relationships of a β-1,2-glucooligosaccharide-degrading β-glucosidase

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 Sop₂ , unlike a known β-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 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 Sop₃ .