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Literature summary extracted from
- Deciphering the molecular basis of the broad substrate specificity of alpha-glucosidase from Bacillus sp. SAM1606 (2003), J. Biochem., 134, 543-550.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.2.1.10 | expression of wild-type and mutant enzymes in Escherichia coli strain W3110 | Bacillus sp. (in: Bacteria) |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.2.1.10 | N342T | site-directed mutagenesis, reduced activity with isomaltose, altered substrate specificity | Bacillus sp. (in: Bacteria) |
| 3.2.1.10 | P273G | site-directed mutagenesis, increased activity with trehalose, reduced activity with isomaltose, altered substrate specificity | Bacillus sp. (in: Bacteria) |
| 3.2.1.10 | P273G/N342T | site-directed mutagenesis, reduced activity with isomaltose, altered substrate specificity | Bacillus sp. (in: Bacteria) |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.2.1.10 | 2 | - |
trehalose | mutant P273G/N342T, pH 7.2, 35°C | Bacillus sp. (in: Bacteria) |  |
| 3.2.1.10 | 5.3 | - |
isomaltose | wild-type enzyme, pH 7.2, 35°C | Bacillus sp. (in: Bacteria) | |
| 3.2.1.10 | 13 | - |
isomaltose | mutant N342T, pH 7.2, 35°C | Bacillus sp. (in: Bacteria) | |
| 3.2.1.10 | 14 | - |
isomaltose | mutant P273G, pH 7.2, 35°C | Bacillus sp. (in: Bacteria) | |
| 3.2.1.10 | 14 | - |
trehalose | mutant P273G, pH 7.2, 35°C | Bacillus sp. (in: Bacteria) | |
| 3.2.1.10 | 20 | - |
isomaltose | mutant P273G/N342T, pH 7.2, 35°C | Bacillus sp. (in: Bacteria) | |
| 3.2.1.10 | 320 | - |
trehalose | wild-type enzyme, pH 7.2, 35°C | Bacillus sp. (in: Bacteria) | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.10 | additional information | Bacillus sp. (in: Bacteria) | evolutionary connection to other alpha-glucosidases in comparison of amino acid sequence and substrate specificity, overview, the alpha-glucosidase, EC 3.2.1.20, of Bacillus sp. strain SAM1606 shows 192fold enhanced activity with trehalose by mutations P273G and T342N | ? | - |
? | |
| 3.2.1.10 | additional information | Bacillus sp. (in: Bacteria) SAM1606 | evolutionary connection to other alpha-glucosidases in comparison of amino acid sequence and substrate specificity, overview, the alpha-glucosidase, EC 3.2.1.20, of Bacillus sp. strain SAM1606 shows 192fold enhanced activity with trehalose by mutations P273G and T342N | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.2.1.10 | Bacillus sp. (in: Bacteria) | - |
- |
- |
| 3.2.1.10 | Bacillus sp. (in: Bacteria) SAM1606 | - |
- |
- |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.10 | additional information | - |
- |
Bacillus sp. (in: Bacteria) |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.10 | 4-nitrophenyl 1-O-alpha-D-glucopyranoside + H2O | - |
Bacillus sp. (in: Bacteria) | 4-nitrophenol + alpha-D-glucopyranose | - |
? | |
| 3.2.1.10 | 4-nitrophenyl 1-O-alpha-D-glucopyranoside + H2O | - |
Bacillus sp. (in: Bacteria) SAM1606 | 4-nitrophenol + alpha-D-glucopyranose | - |
? | |
| 3.2.1.10 | isomaltose + H2O | - |
Bacillus sp. (in: Bacteria) | ? | - |
? | |
| 3.2.1.10 | isomaltose + H2O | - |
Bacillus sp. (in: Bacteria) SAM1606 | ? | - |
? | |
| 3.2.1.10 | additional information | evolutionary connection to other alpha-glucosidases in comparison of amino acid sequence and substrate specificity, overview, the alpha-glucosidase, EC 3.2.1.20, of Bacillus sp. strain SAM1606 shows 192fold enhanced activity with trehalose by mutations P273G and T342N | Bacillus sp. (in: Bacteria) | ? | - |
? | |
| 3.2.1.10 | additional information | enzyme is highly specific for alpha-1,6-linkages | Bacillus sp. (in: Bacteria) | ? | - |
? | |
| 3.2.1.10 | additional information | evolutionary connection to other alpha-glucosidases in comparison of amino acid sequence and substrate specificity, overview, the alpha-glucosidase, EC 3.2.1.20, of Bacillus sp. strain SAM1606 shows 192fold enhanced activity with trehalose by mutations P273G and T342N | Bacillus sp. (in: Bacteria) SAM1606 | ? | - |
? | |
| 3.2.1.10 | additional information | enzyme is highly specific for alpha-1,6-linkages | Bacillus sp. (in: Bacteria) SAM1606 | ? | - |
? | |
| 3.2.1.10 | trehalose + H2O | - |
Bacillus sp. (in: Bacteria) | ? | - |
? | |
| 3.2.1.10 | trehalose + H2O | - |
Bacillus sp. (in: Bacteria) SAM1606 | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.2.1.10 | dextrin 6-alpha-glucanohydrolase | - |
Bacillus sp. (in: Bacteria) |
| 3.2.1.10 | More | enzyme belongs to the family 13 of glycosyl hydrolases | Bacillus sp. (in: Bacteria) |
| 3.2.1.10 | O16G | - |
Bacillus sp. (in: Bacteria) |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.10 | 35 | - |
assay at | Bacillus sp. (in: Bacteria) |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.10 | 7.2 | - |
assay at | Bacillus sp. (in: Bacteria) |
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