Protein Variants | Comment | Organism |
---|---|---|
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 |
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 |
D294S | site-directed mutagenesis, the mutant shows highly reduced kcat and reduced activity with malto-oligomers compared to the wild-type enzyme | Thermus thermophilus |
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 |
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 |
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 |
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 |
F366L | site-directed mutagenesis, the mutant shows reduced kcat compared and reduced activity with malto-oligomers compared to the wild-type enzyme | Thermus thermophilus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
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 |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics of wild-type and mutant enzymes at pH 6.5 and 70°C, overview | Thermus thermophilus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
59337 | - |
x * 59337, sequence calculation | Thermus thermophilus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Thermus thermophilus | Thermus thermophilus AMase is among the most efficient 4-alpha-glucanotransferases in the alpha-amylase superfamily | ? | - |
? | |
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 | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermus thermophilus | O87172 | - |
- |
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | O87172 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
maltoheptaose + maltoheptaose | - |
Thermus thermophilus | ? | - |
? | |
maltoheptaose + maltoheptaose | - |
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | ? | - |
? | |
maltohexaose + maltohexaose | - |
Thermus thermophilus | ? | - |
? | |
maltohexaose + maltohexaose | - |
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | ? | - |
? | |
maltopentaose + maltopentaose | - |
Thermus thermophilus | ? | - |
? | |
maltopentaose + maltopentaose | - |
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | ? | - |
? | |
maltotetraose + maltotetraose | - |
Thermus thermophilus | ? | - |
? | |
maltotriose + maltotriose | - |
Thermus thermophilus | glucose + maltooligosaccharides | - |
? | |
additional information | Thermus thermophilus AMase is among the most efficient 4-alpha-glucanotransferases in the alpha-amylase superfamily | Thermus thermophilus | ? | - |
? | |
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 | ? | - |
? | |
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 | ? | - |
? | |
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 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 59337, sequence calculation | Thermus thermophilus |
Synonyms | Comment | Organism |
---|---|---|
AMase | - |
Thermus thermophilus |
amylomaltase | - |
Thermus thermophilus |
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 |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
70 | - |
assay at | Thermus thermophilus |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
50 | 90 | - |
Thermus thermophilus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
80 | - |
stable up to at pH 5.5, half-life is 18 min | Thermus thermophilus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.68 | - |
maltotriose | pH 5.5, 70°C, mutant D249S | Thermus thermophilus | |
0.97 | - |
maltotetraose | pH 5.5, 70°C, mutant D249S | Thermus thermophilus | |
1.99 | - |
maltoheptaose | pH 5.5, 70°C, mutant D249S | Thermus thermophilus | |
3.26 | - |
maltohexaose | pH 5.5, 70°C, mutant D249S | Thermus thermophilus | |
3.98 | - |
maltopentaose | pH 5.5, 70°C, mutant D249S | Thermus thermophilus | |
106 | - |
maltotetraose | pH 5.5, 70°C, mutant F366L | Thermus thermophilus | |
111 | - |
maltotriose | pH 5.5, 70°C, mutant F366L | Thermus thermophilus | |
159 | - |
maltoheptaose | pH 5.5, 70°C, mutant F366L | Thermus thermophilus | |
179 | - |
maltopentaose | pH 5.5, 70°C, mutant F366L | Thermus thermophilus | |
188 | - |
maltohexaose | pH 5.5, 70°C, mutant F366L | Thermus thermophilus | |
213 | - |
maltoheptaose | pH 5.5, 70°C, wild-type enzyme | Thermus thermophilus | |
304 | - |
maltohexaose | pH 5.5, 70°C, wild-type enzyme | Thermus thermophilus | |
317 | - |
maltotriose | pH 5.5, 70°C, wild-type enzyme | Thermus thermophilus | |
329 | - |
maltopentaose | pH 5.5, 70°C, wild-type enzyme | Thermus thermophilus | |
425 | - |
maltotetraose | pH 5.5, 70°C, wild-type enzyme | Thermus thermophilus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5.5 | - |
assay at | Thermus thermophilus |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
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 |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
4 | 7.5 | pH stability of wild-type and mutant enzymes, overview | Thermus thermophilus |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.003 | - |
acarbose | pH 5.5, 70°C, competitive inhibition | Thermus thermophilus | |
0.004 | - |
acarbose | pH 5.5, 70°C, uncompetitive inhibition | Thermus thermophilus |