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Results 1 - 7 of 7
EC Number
General Information
Commentary
Reference
evolution
the enzyme belongs to the glycosyl hydrolase family 1, GH1
evolution
the enzyme belongs to the glycosyl hydrolase family 1, GH1. Members of the GH-1 family share a common catalytic mechanism and exhibit similar structural folds, including a (beta/alpha)8 TIM-barrel
metabolism
the enzyme is involved in the metabolic pathway of lactose in Lactobacillus gasseri, overview; the enzyme is involved in the metabolic pathway of lactose in Lactobacillus gasseri, overview
more
conserved residues S427, Lys435, and Tyr437 act as gatekeepers in a phosphate-binding loop and play important roles in phosphate recognition, homology structure modelling, overview
more
structure comparisons, active center and substrate specificity, overview
more
the overall structure of enzyme BglA-2 adopts a typical (beta/alpha)8 TIM-barrel, with the active site located at the center of the convex surface of the beta-barrel. Residues Tyr126, Tyr303, and Trp338, at subsite +1 of BglA-2 determine substrate specificity with respect to 1,4-linked 6-phospho-beta-glucosides. Residues Ser424, Lys430, and Tyr432 of BglA-2 play important roles in the hydrolytic selectivity toward phosphorylated rather than non-phosphorylated compounds, comparative structural analysis. Tryptophan versus a methionine/alanine residue at subsite -1 may contribute to the catalytic and substrate selectivity with respect to structurally similar 6-phospho-beta-galactosidases and 6-phospho-beta-glucosidases assigned to the GH-1 family
physiological function
the enzyme SPy1599 is involved in the intracellular degradation of 6-phosphoglycosides, which are likely to originate from import through one of the organism's many phosphoenolpyruvate phosphotransfer systems
Results 1 - 7 of 7