EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.4.1.25 | D293A | site-directed mutagenesis of the active site nucleophile, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme | Thermus thermophilus |
2.4.1.25 | D293N | site-directed mutagenesis of the active site nucleophile, the D293N mutation reduces the pH stability of the enzyme, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme | Thermus thermophilus |
2.4.1.25 | D294S | site-directed mutagenesis, the mutant shows highly reduced kcat and reduced activity with malto-oligomers compared to the wild-type enzyme | Thermus thermophilus |
2.4.1.25 | D395A | site-directed mutagenesis of the active site transition stabilizer, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme | Thermus thermophilus |
2.4.1.25 | D395N | site-directed mutagenesis of the active site transition stabilizer, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme | Thermus thermophilus |
2.4.1.25 | E340A | site-directed mutagenesis of the active site general acid/base catalyst, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme | Thermus thermophilus |
2.4.1.25 | E340Q | site-directed mutagenesis of the active site general acid/base catalyst, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme | Thermus thermophilus |
2.4.1.25 | F366L | site-directed mutagenesis, the mutant shows reduced kcat compared and reduced activity with malto-oligomers compared to the wild-type enzyme | Thermus thermophilus |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.4.1.25 | acarbose | a strong mixed inhibitor with almost equal competitive and uncompetitive binding constants, acarbose is both bound in the active site and at another site | Thermus thermophilus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.4.1.25 | additional information | - |
additional information | kinetics of wild-type and mutant enzymes at pH 6.5 and 70°C, overview | Thermus thermophilus |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
2.4.1.25 | 59337 | - |
x * 59337, sequence calculation | Thermus thermophilus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.4.1.25 | additional information | Thermus thermophilus | Thermus thermophilus AMase is among the most efficient 4-alpha-glucanotransferases in the alpha-amylase superfamily | ? | - |
? | |
2.4.1.25 | additional information | Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | Thermus thermophilus AMase is among the most efficient 4-alpha-glucanotransferases in the alpha-amylase superfamily | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.4.1.25 | Thermus thermophilus | O87172 | - |
- |
2.4.1.25 | Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | O87172 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.4.1.25 | maltoheptaose + maltoheptaose | - |
Thermus thermophilus | ? | - |
? | |
2.4.1.25 | maltoheptaose + maltoheptaose | - |
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | ? | - |
? | |
2.4.1.25 | maltohexaose + maltohexaose | - |
Thermus thermophilus | ? | - |
? | |
2.4.1.25 | maltohexaose + maltohexaose | - |
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | ? | - |
? | |
2.4.1.25 | maltopentaose + maltopentaose | - |
Thermus thermophilus | ? | - |
? | |
2.4.1.25 | maltopentaose + maltopentaose | - |
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | ? | - |
? | |
2.4.1.25 | maltotetraose + maltotetraose | - |
Thermus thermophilus | ? | - |
? | |
2.4.1.25 | maltotriose + maltotriose | - |
Thermus thermophilus | glucose + maltooligosaccharides | - |
? | |
2.4.1.25 | additional information | Thermus thermophilus AMase is among the most efficient 4-alpha-glucanotransferases in the alpha-amylase superfamily | Thermus thermophilus | ? | - |
? | |
2.4.1.25 | additional information | substrates are maltooligomers, trimer to heptamer, substrate binding mechanism and structure, modeling. The active site contains at least seven substrate binding sites, subsites -2 and +3 favoring substrate binding and subsites -3 and +2 do not, substrate specificity, overview | Thermus thermophilus | ? | - |
? | |
2.4.1.25 | additional information | Thermus thermophilus AMase is among the most efficient 4-alpha-glucanotransferases in the alpha-amylase superfamily | Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | ? | - |
? | |
2.4.1.25 | additional information | substrates are maltooligomers, trimer to heptamer, substrate binding mechanism and structure, modeling. The active site contains at least seven substrate binding sites, subsites -2 and +3 favoring substrate binding and subsites -3 and +2 do not, substrate specificity, overview | Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.4.1.25 | ? | x * 59337, sequence calculation | Thermus thermophilus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.4.1.25 | AMase | - |
Thermus thermophilus |
2.4.1.25 | amylomaltase | - |
Thermus thermophilus |
2.4.1.25 | More | the enzyme belongs to the glycoside hydrolase family 77, GH77, which belongs to the alpha-amylase superfamily, Clan H, together with GH13 and GH70 | Thermus thermophilus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.4.1.25 | 70 | - |
assay at | Thermus thermophilus |
EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.4.1.25 | 50 | 90 | - |
Thermus thermophilus |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.4.1.25 | 80 | - |
stable up to at pH 5.5, half-life is 18 min | Thermus thermophilus |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.4.1.25 | 0.68 | - |
maltotriose | pH 5.5, 70°C, mutant D249S | Thermus thermophilus | |
2.4.1.25 | 0.97 | - |
maltotetraose | pH 5.5, 70°C, mutant D249S | Thermus thermophilus | |
2.4.1.25 | 1.99 | - |
maltoheptaose | pH 5.5, 70°C, mutant D249S | Thermus thermophilus | |
2.4.1.25 | 3.26 | - |
maltohexaose | pH 5.5, 70°C, mutant D249S | Thermus thermophilus | |
2.4.1.25 | 3.98 | - |
maltopentaose | pH 5.5, 70°C, mutant D249S | Thermus thermophilus | |
2.4.1.25 | 106 | - |
maltotetraose | pH 5.5, 70°C, mutant F366L | Thermus thermophilus | |
2.4.1.25 | 111 | - |
maltotriose | pH 5.5, 70°C, mutant F366L | Thermus thermophilus | |
2.4.1.25 | 159 | - |
maltoheptaose | pH 5.5, 70°C, mutant F366L | Thermus thermophilus | |
2.4.1.25 | 179 | - |
maltopentaose | pH 5.5, 70°C, mutant F366L | Thermus thermophilus | |
2.4.1.25 | 188 | - |
maltohexaose | pH 5.5, 70°C, mutant F366L | Thermus thermophilus | |
2.4.1.25 | 213 | - |
maltoheptaose | pH 5.5, 70°C, wild-type enzyme | Thermus thermophilus | |
2.4.1.25 | 304 | - |
maltohexaose | pH 5.5, 70°C, wild-type enzyme | Thermus thermophilus | |
2.4.1.25 | 317 | - |
maltotriose | pH 5.5, 70°C, wild-type enzyme | Thermus thermophilus | |
2.4.1.25 | 329 | - |
maltopentaose | pH 5.5, 70°C, wild-type enzyme | Thermus thermophilus | |
2.4.1.25 | 425 | - |
maltotetraose | pH 5.5, 70°C, wild-type enzyme | Thermus thermophilus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.4.1.25 | 5.5 | - |
assay at | Thermus thermophilus |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
2.4.1.25 | 4 | 7.5 | pH dependence of wild-type and mutant enzymes, D293N and E340Q are active below pH 6.5 and pH 5.5, respectively, but precipitate during the necessary prolonged incubation times, wild-type Tt AMase precipitates below pH 5.5 under similar extended incubation times as well, overview | Thermus thermophilus |
EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|---|
2.4.1.25 | 4 | 7.5 | pH stability of wild-type and mutant enzymes, overview | Thermus thermophilus |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.4.1.25 | 0.003 | - |
acarbose | pH 5.5, 70°C, competitive inhibition | Thermus thermophilus | |
2.4.1.25 | 0.004 | - |
acarbose | pH 5.5, 70°C, uncompetitive inhibition | Thermus thermophilus |