Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Choi, I.D.; Kim, H.Y.; Choi, Y.J.
    Gene cloning and characterization of alpha-glucuronidase of Bacillus stearothermophilus No. 236 (2000), Biosci. Biotechnol. Biochem., 64, 2530-2537.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.139 expression in Escherichia coli Geobacillus stearothermophilus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.139 Ag+ 1 mM, 58% inhibition Geobacillus stearothermophilus
3.2.1.139 Cu2+ 1 mM, complete inhibition Geobacillus stearothermophilus
3.2.1.139 Hg2+ 1 mM, complete inhibition Geobacillus stearothermophilus
3.2.1.139 Mn2+ 1 mM, 78% inhibition Geobacillus stearothermophilus
3.2.1.139 Pb2+ 1 mM, 53% inhibition Geobacillus stearothermophilus
3.2.1.139 Zn2+ 1 mM, 43% inhibition Geobacillus stearothermophilus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.139 0.78
-
 2-O-alpha-(4-O-methyl-alpha-D-glucopyranosyluronic)-D-xylobiose 40°C, pH 6.5 Geobacillus stearothermophilus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.139 intracellular
-
 Geobacillus stearothermophilus 5622
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.139 77000
-
 2 * 77000, SDS-PAGE Geobacillus stearothermophilus
3.2.1.139 78156
-
 2 * 78156, calculated from sequence Geobacillus stearothermophilus
3.2.1.139 161000
-
 gel filtration Geobacillus stearothermophilus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.139 additional information Geobacillus stearothermophilus the enzyme is involved in hydrolysis of xylan. Presence of endoxylanase is critical for efficient alpha-glucuronidase activity, and efficient alpha-glucuronidase activity is essential for the complete hydrolysis of intact xylan ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.139 Geobacillus stearothermophilus
-
 No. 236
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.139 15.3
-
 hydrolysis of 2-O-alpha-(4-O-methyl-alpha-D-glucopyranosyluronic)-D-xylobiose Geobacillus stearothermophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.139 2-O-alpha-(4-O-methyl-alpha-D-glucopyranosyluronic)-D-xylobiose + H2O i.e. aldotriouronic acid Geobacillus stearothermophilus 4-O-methylglucuronic acid + D-xylobiose
-
 ?
3.2.1.139 aldobiouronic acid + H2O
-
 Geobacillus stearothermophilus ?
-
 ?
3.2.1.139 aldotetraouronic acid + H2O
-
 Geobacillus stearothermophilus ?
-
 ?
3.2.1.139 additional information the enzyme is involved in hydrolysis of xylan. Presence of endoxylanase is critical for efficient alpha-glucuronidase activity, and efficient alpha-glucuronidase activity is essential for the complete hydrolysis of intact xylan Geobacillus stearothermophilus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.139 dimer 2 * 77000, SDS-PAGE Geobacillus stearothermophilus
3.2.1.139 dimer 2 * 78156, calculated from sequence Geobacillus stearothermophilus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.139 40
-
-
 Geobacillus stearothermophilus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.139 45
-
 4 h, 20% loss of activity Geobacillus stearothermophilus
3.2.1.139 50
-
 half-life: 50 min Geobacillus stearothermophilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.139 6.5
-
-
 Geobacillus stearothermophilus

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.2.1.139 Geobacillus stearothermophilus calculated from sequence
-
 5.34