Cloned (Comment) | Organism |
---|---|
gene malA, DNA and amino acid sequence analysis, phylogenetic tree, overexpression of wild-type and selenomethionine-labeled enzyme in Escherichia coli strain NF1830 | Saccharolobus solfataricus |
Crystallization (Comment) | Organism |
---|---|
purified recombinant wild-type and selenomethionine-labeled enzyme, hanging drop vapour diffusion method, hexameric crystal form, X-ray diffraction structure determination and analysis of the different crystal forms at 2.5 A resolution, structure modelling of domains, full-length enzyme, and active site | Saccharolobus solfataricus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics | Saccharolobus solfataricus | |
2 | - |
4-nitrophenyl alpha-D-glucopyranoside | pH 4.5, 85°C, recombinant enzyme | Saccharolobus solfataricus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
470000 | - |
recombinant enzyme, native PAGE | Saccharolobus solfataricus |
480000 | - |
recombinant enzyme, gel filtration | Saccharolobus solfataricus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
maltose + H2O | Saccharolobus solfataricus | - |
alpha-D-glucose + D-glucose | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharolobus solfataricus | P0CD66 | gene malA | - |
Purification (Comment) | Organism |
---|---|
recombinant wild-type and selenomethionine-labeled enzyme from Escherichia coli strain NF1830 by ammonium sulfate fractionation, ion exchange chromatography, and gel filtration | Saccharolobus solfataricus |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
maltotetraose + 3 H2O = 4 alpha-D-glucose | substrate recognition and catalytic mechanism, active site structure, residues R400, D87, W284, M321, F327 are involved in formation of the +1 subsite in the GH31 alpha-glucosidase substrate binding | Saccharolobus solfataricus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-nitrophenyl alpha-D-glucopyranoside + H2O | - |
Saccharolobus solfataricus | 4-nitrophenol + alpha-D-glucose | - |
? | |
maltose + H2O | - |
Saccharolobus solfataricus | alpha-D-glucose + D-glucose | - |
? | |
maltose + H2O | preferred substrate, Asp251 and Trp284 interact with the position 6 OH group of the substrate | Saccharolobus solfataricus | alpha-D-glucose + D-glucose | - |
? | |
additional information | substrate specificity, overview | Saccharolobus solfataricus | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
hexamer | domain structure analysis, quarternary organization, comparison to alpha-xylosidase Yic1 | Saccharolobus solfataricus |
More | monomer fold, overview | Saccharolobus solfataricus |
Synonyms | Comment | Organism |
---|---|---|
AG | - |
Saccharolobus solfataricus |
MalA | - |
Saccharolobus solfataricus |
More | the enzyme belongs to the glycoside hydrolase family 31, GH31 | Saccharolobus solfataricus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
85 | - |
assay at | Saccharolobus solfataricus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
33 | - |
4-nitrophenyl alpha-D-glucopyranoside | pH 4.5, 85°C, recombinant enzyme | Saccharolobus solfataricus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
4.5 | - |
assay at | Saccharolobus solfataricus |