3.2.1.86: 6-phospho-beta-glucosidase
This is an abbreviated version!
For detailed information about 6-phospho-beta-glucosidase, go to the full flat file.
Word Map on EC 3.2.1.86
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3.2.1.86
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phosphotransferase
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beta-glucoside
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arbutin
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salicin
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phosphoenolpyruvate-dependent
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antiterminator
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beta-glucoside-specific
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mortiferum
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phospho-beta-galactosidase
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turanose
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palatinose
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glycosylhydrolase
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trehalulose
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leucrose
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p-nitrophenyl-alpha-d-glucopyranoside
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maltulose
- 3.2.1.86
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phosphotransferase
- beta-glucoside
- arbutin
- salicin
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phosphoenolpyruvate-dependent
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antiterminator
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beta-glucoside-specific
- mortiferum
- phospho-beta-galactosidase
- turanose
- palatinose
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glycosylhydrolase
- trehalulose
- leucrose
- p-nitrophenyl-alpha-d-glucopyranoside
- maltulose
Reaction
Synonyms
6-phospho-alpha-glucosidase, 6-phospho-beta-glucosidase, AscB protein, bgl-2, BglA, BglA-2, BglA3, bglD, BglT, CelD, Cellobiose-6-phosphate hydrolase, Gan1D, LacG1, LacG2, More, P-beta-glc, PalH, Pbgl25-217, phospho-alpha-glucosidase, phospho-beta-glucosidase, phospho-beta-glucosidase A, phosphocellobiase, SPD_0247, SPy1599
ECTree
3.2.1.86 6-phospho-beta-glucosidaseAdvanced search results
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results (General Information
General Information on EC 3.2.1.86 - 6-phospho-beta-glucosidase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
malfunction
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an enzyme deletion mutant shows reduced 6-phospho-glucosidase activity and is attenuated in growth on cellobiose and hyaluronic acid compared to the growth of wild type. Mutant-infected mice survive significantly longer than the wild-type-infected cohort, and the colony counts of the mutant are lower than those of the wild type in the lungs. The enzyme deletion mutant is also severely impaired in attachment to an abiotic surface
metabolism
physiological function
additional information
evolution
the enzyme belongs to the glycosyl hydrolase family 1, GH1
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
evolution
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the enzyme belongs to the glycosyl hydrolase family 1, GH1
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metabolism
the enzyme is involved in the metabolic pathway of lactose in Lactobacillus gasseri, overview
metabolism
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the enzyme is involved in the metabolic pathway of lactose in Lactobacillus gasseri, overview
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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
physiological function
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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
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additional information
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
additional information
structure comparisons, active center and substrate specificity, overview
additional information
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structure comparisons, active center and substrate specificity, overview
additional information
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
additional information
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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
additional information
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structure comparisons, active center and substrate specificity, overview
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