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Literature summary for 3.2.1.20 extracted from
- Molecular and biochemical characterization of alpha-glucosidase and alpha-mannosidase and their clustered genes from the thermoacidophilic archaeon Picrophilus torridus (2006), J. Bacteriol., 188, 7123-7131.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene aglA, expression analysis and mapping of transcription start sites, the gene is clustered in the genome and shows colinear orientation and a small intergenic space with gene manA encoding alpha-mannosidase, the genes are independently transcribed, both producing leaderless mRNA, phylogenetic tree, overexpression in Escherichia coli strain BL21, subcloning in Escherichia coli strain XL-1 Blue | Picrophilus torridus |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 72000 | - |
6 * 72000, recombinant AglA, SDS-PAGE | Picrophilus torridus |
| 440000 | - |
recombinant AglA, gel filtration | Picrophilus torridus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| maltose + H2O | Picrophilus torridus | probable physiological role of the enzyme in the utilization of exogenous glycoproteins and/or in the turnover of the organisms own glycoproteins, overview | alpha-D-glucose + D-glucose | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Picrophilus torridus | Q6L2X4 | strain DSM 9790, gene aglA | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant AglA 39.3fold from Escherichia coli strain BL21 by heat treatment for 15 min at 67°C, hydrophobic interaction and anion exchange chromatography, and gel filtration in presence of 150 mM NaCl | Picrophilus torridus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| additional information | 60°C is the optimal, 67°C the maximal growth temperature | Picrophilus torridus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-nitrophenyl alpha-D-glucopyranoside + H2O | low activity | Picrophilus torridus | 4-nitrophenol + alpha-D-glucose | - |
? | |
| dextrin 10 + H2O | 27% of the activity with maltose | Picrophilus torridus | alpha-D-glucose | - |
? | |
| maltohexaose + H2O | - |
Picrophilus torridus | maltopentaose + D-glucose | - |
? | |
| maltopentaose + H2O | - |
Picrophilus torridus | alpha-D-glucose + ? | - |
? | |
| maltose + H2O | probable physiological role of the enzyme in the utilization of exogenous glycoproteins and/or in the turnover of the organisms own glycoproteins, overview | Picrophilus torridus | alpha-D-glucose + D-glucose | - |
? | |
| maltose + H2O | preferred substrate, the enzyme shows strict glucose substrate specificity hydrolyzing maltose, as well as longer alpha-1,4-linked maltooligosaccharides | Picrophilus torridus | alpha-D-glucose + D-glucose | - |
? | |
| maltotetraose + H2O | 54% of the activity with maltose | Picrophilus torridus | alpha-D-glucose | - |
? | |
| maltotriose + H2O | - |
Picrophilus torridus | maltose + alpha-D-glucose | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| hexamer | 6 * 72000, recombinant AglA, SDS-PAGE | Picrophilus torridus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AglA | - |
Picrophilus torridus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 87 | - |
recombinant AglA | Picrophilus torridus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 100 | - |
15 min, inactivation | Picrophilus torridus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5 | - |
- |
Picrophilus torridus |
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