Cytosolic beta-Glucosidase (GBA3)

Glycosidase probably involved in the intestinal absorption and metabolism of dietary flavonoid glycosides. Able to hydrolyze a broad variety of glycosides including phytoestrogens, flavonols, flavones, flavanones and cyanogens. Possesses beta-glycosylceramidase activity and may be involved in a nonlysosomal catabolic pathway of glycosylceramide.

Cytosolic beta-Glucosidase (GBA3) Related Areas

Enzyme>>Carbohydrate Metabolism Enzymes>>GBA3

Cytosolic beta-Glucosidase (GBA3) Alternative Names

GBA3, CBGL1, cytosolic beta-glucosidase, GLUC, KLrP, MGC104276, MGC126878 [Homo sapiens]

Summaries for Cytosolic beta-Glucosidase (GBA3)

Entrez Gene summary for Cytosolic beta-Glucosidase (GBA3):

GBA3, or cytosolic beta-glucosidase (EC 3.2.1.21), is a predominantly liver enzyme that efficiently hydrolyzes beta-D-glucoside and beta-D-galactoside, but not any known physiologic beta-glycoside, suggesting that it may be involved in detoxification of plant glycosides (de Graaf et al., 2001 [PubMed 11389701]). GBA3 also has significant neutral glycosylceramidase activity (EC 3.2.1.62), suggesting that it may be involved in a nonlysosomal catabolic pathway of glucosylceramide metabolism (Hayashi et al., 2007 [PubMed 17595169]).

OMIM - description for Cytosolic beta-Glucosidase (GBA3):

Using synthetic glucosylceramide, Hayashi et al. (2007) showed that KLRP had neutral glycosylceramidase activity in cytosolic fractions of several vertebrate tissues and in human fibroblasts. Knockdown of endogenous KLRP in human embryonic kidney cells increased the cellular level of glucosylceramide. Purified recombinant human KLRP showed maximum glycosylceramidase activity at pH 6 to 7. KLRP also hydrolyzed glucosylsphingosine and, less efficiently, galactosylceramide and galactosylsphingosine. Mutation of glu165 and glu373 of KLRP to asp reduced glycosylceramidase activity, and mutation of these residues to gly eliminated glycosylceramidase activity.

Wikipedia summary for Cytosolic beta-Glucosidase (GBA3):

Cytosolic beta-glucosidase, also known as cytosolic beta-glucosidase-like protein 1, is a beta-glucosidase (EC 3.2.1.21) enzyme that in humans is encoded by the GBA3 gene

Human Cytosolic beta-Glucosidase (GBA3) Protein General Information

 

• Protein names: Recommended name: Cytosolic beta-glucosidase
• Sequence length: 469 AA.
• Sequence similarities: Belongs to the glycosyl hydrolase 1 family. Klotho subfamily.
• Post-translational modification: The N-terminus is blocked
• Catalytic activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
• Subcellular location: Cytoplasm › cytosol
• Enzyme regulation: Inhibited by 2,4-dinitrophenyl-2-fluoro-2-deoxy-beta-D-glucopyranoside and sodium taurocholate.
• Biophysicochemical properties: Kinetic parameters: KM=40 µM for 4-methylumbelliferyl-beta-D-glucopyranoside Ref.2 Ref.3 KM=50 µM for 4-methylumbelliferyl-beta-D-galactopyranoside KM=370 µM for 4-nitrophenyl-beta-D-fucopyranoside KM=570 µM for 4-nitrophenyl-alpha-D-arabinopyranoside KM=1.76 mM for 4-nitrophenyl-beta-D-glucopyranoside KM=3.14 mM for 4-nitrophenyl-beta-D-galactopyranoside KM=1.58 mM for 4-nitrophenyl-beta-D-xylopyranoside KM=52.6 mM for 4-nitrophenyl-beta-L-arabinopyranoside KM=35 µM for genistein-7-glucoside KM=118 µM for daidzein-7-glucoside KM=31.8 µM for quercetin-4'-glucoside KM=42.2 µM for quercetin-7-glucoside KM=21.5 µM for apigenin-7-glucoside KM=10 µM for luteolin-4'-glucoside KM=50 µM for luteolin-7-glucoside KM=432 µM for naringenin-7-glucoside KM=253 µM for eriodictyol-7-glucoside Vmax=10 µmol/min/mg enzyme toward 4-nitrophenyl-beta-D-glucopyranoside Vmax=1.73 µmol/min/mg enzyme toward genistein-7-glucoside Vmax=2.75 µmol/min/mg enzyme toward daidzein-7-glucoside Vmax=1.19 µmol/min/mg enzyme toward quercetin-4'-glucoside Vmax=0.77 µmol/min/mg enzyme toward quercetin-7-glucoside Vmax=1.30 µmol/min/mg enzyme toward apigenin-7-glucoside Vmax=1.30 µmol/min/mg enzyme toward luteolin-4'-glucoside Vmax=2.85 µmol/min/mg enzyme toward luteolin-7-glucoside Vmax=0.93 µmol/min/mg enzyme toward naringenin-7-glucoside Vmax=0.90 µmol/min/mg enzyme toward eriodictyol-7-glucoside pH dependence: Optimum pH is 6.5. Active from pH 5 to 7.5. Activity decreases sharply with increasing acidity and is less than 4% at pH 4. Temperature dependence: Optimum temperature is 50 degrees Celsius. Stable more than 24 hours at 37 degrees Celsius. Loses activity at 58 degrees Celsius.

General information above from UniProt

Function for Cytosolic beta-Glucosidase (GBA3) Protein

UniProtKB:

Glycosidase probably involved in the intestinal absorption and metabolism of dietary flavonoid glycosides. Able to hydrolyze a broad variety of glycosides including phytoestrogens, flavonols, flavones, flavanones and cyanogens. Possesses beta-glycosylceramidase activity and may be involved in a nonlysosomal catabolic pathway of glycosylceramide.

Genatlas:

• hydrolyzing beta-D glucoside and beta-D galactoside but any known physiologic beta-glucoside, suggesting that it may be involved in the detoxification of plant glycosides
• Cytosolic beta-Glucosidase (GBA3) also has a significant neutral glycosylceramidase activity, suggesting that it may be involved in a nonlysosomal catabolic pathway of glucosylceramide metabolism
• Cytosolic beta-Glucosidase (GBA3) is probably involved in the intestinal absorption and metabolism of dietary flavonoid glycosides

Homology for human Cytosolic beta-Glucosidase (GBA3)

• homolog to dog GBA3 (87.8pc)