Background:Streptococcus pneumoniae BgaC is a GH-35 -galactosidase of specific activity toward (1,3)-linked galactose and N-acetylglucosamine. Results: Three aromatic residues, Trp-240, Trp-243, and Tyr-455, determine the substrate specificity of BgaC. Conclusion: BgaC and other GH-35 -galactosidases adopt a similar domain organization and catalytic mechanism. Significance: Provided is the first structural insight into the substrate specificity of -galactosidase toward the (1,3)-linked galactosyl bond.
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