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UniProt functional annotation for Q09LY5 | ||
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| UniProt code: Q09LY5. |
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| Organism: | |
Geobacillus stearothermophilus (Bacillus stearothermophilus). |
| Taxonomy: | |
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus. |
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| Function: | |
Alpha-glucuronidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. It catalyzes the cleavage of alpha-1,2-glycosidic bond of the 4-O-methyl-D-glucuronic acid side chain of xylan and releases 4- O-methylglucuronic acid from xylan. {ECO:0000269|PubMed:11358519}. |
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| Catalytic activity: | |
Reaction=Hydrolysis of (1->2)-alpha-D-(4-O-methyl)glucuronosyl links in the main chain of hardwood xylans.; EC=3.2.1.131; |
| Activity regulation: | |
The metal cations Ni(2+), K(+) and Zn(2+) show some inhibition of the activity, and Ag(+), Hg(2+) and Cu(2+) shows very significant inhibition even at relatively low ion concentrations. {ECO:0000269|PubMed:11358519}. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=0.2 mM for aldotetraouronic acid (at 55 degrees Celsius) {ECO:0000269|PubMed:11358519}; Vmax=42 umol/min/ug enzyme with aldotetraouronic acid as substrate (at 55 degrees Celsius) {ECO:0000269|PubMed:11358519}; pH dependence: Optimum pH is 5.5-6. It retains about 40% of its activity at pH 4.5 and 7.5. {ECO:0000269|PubMed:11358519}; Temperature dependence: Optimum temperature is 65 degrees Celsius. The enzyme is stable up to 70 degrees Celsius and lost 70% of its activity at 75 degrees Celsius. {ECO:0000269|PubMed:11358519}; |
| Subunit: | |
Homodimer. {ECO:0000269|PubMed:11358519, ECO:0000269|PubMed:14573597}. |
| Similarity: | |
Belongs to the glycosyl hydrolase 67 family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.