Cloned (Comment) | Organism |
---|---|
expressed the gene in Escherichia coli | Thermococcus sp. |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
4.25 | - |
maltotriose | pH 5.0, 85°C | Thermococcus sp. | |
16.2 | - |
maltopentaose | pH 5.0, 85°C | Thermococcus sp. | |
18.2 | - |
maltotetraose | pH 5.0, 85°C | Thermococcus sp. |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
intracellular | - |
Thermococcus sp. | 5622 | - |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
67120 | - |
- |
Thermococcus sp. |
70000 | - |
1 * 70000, SDS-PAGE | Thermococcus sp. |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermococcus sp. | I3ZTN9 | - |
- |
Thermococcus sp. CL1 | I3ZTN9 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
amylopectin + H2O | the enzyme only releases maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan | Thermococcus sp. | maltose + ? | - |
? | |
amylopectin + H2O | the enzyme only releases maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan | Thermococcus sp. CL1 | maltose + ? | - |
? | |
glycogen + H2O | the enzyme only releases maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan | Thermococcus sp. | maltose + ? | - |
? | |
glycogen + H2O | the enzyme only releases maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan | Thermococcus sp. CL1 | maltose + ? | - |
? | |
maltopentaose + H2O | the enzyme displays dual hydrolysis activity toward alpha-1,4- and alpha-1,6-glycosidic linkages, the catalytic efficiency of 6-O-maltosyl-beta-cyclodextrin is 16fold higher than that of maltotriose. Compared to the kcat/Km value toward maltotriose, the values for longer substrates such as maltotetraose and maltopentaose are negligible | Thermococcus sp. | 2 maltose + D-glucose | - |
? | |
maltopentaose + H2O | the enzyme displays dual hydrolysis activity toward alpha-1,4- and alpha-1,6-glycosidic linkages, the catalytic efficiency of 6-O-maltosyl-beta-cyclodextrin is 16fold higher than that of maltotriose. Compared to the kcat/Km value toward maltotriose, the values for longer substrates such as maltotetraose and maltopentaose are negligible | Thermococcus sp. CL1 | 2 maltose + D-glucose | - |
? | |
maltotetraose + H2O | the enzyme displays dual hydrolysis activity toward alpha-1,4- and alpha-1,6-glycosidic linkages, the catalytic efficiency of 6-O-maltosyl-beta-cyclodextrin is 16fold higher than that of maltotriose. Compared to the kcat/Km value toward maltotriose, the values for longer substrates such as maltotetraose and maltopentaose are negligible | Thermococcus sp. | 2 maltose | - |
? | |
maltotetraose + H2O | the enzyme displays dual hydrolysis activity toward alpha-1,4- and alpha-1,6-glycosidic linkages, the catalytic efficiency of 6-O-maltosyl-beta-cyclodextrin is 16fold higher than that of maltotriose. Compared to the kcat/Km value toward maltotriose, the values for longer substrates such as maltotetraose and maltopentaose are negligible | Thermococcus sp. CL1 | 2 maltose | - |
? | |
maltotriose + H2O | the enzyme displays dual hydrolysis activity toward alpha-1,4- and alpha-1,6-glycosidic linkages, the catalytic efficiency of 6-O-maltosyl-beta-cyclodextrin is 16fold higher than that of maltotriose. Compared to the kcat/Km value toward maltotriose, the values for longer substrates such as maltotetraose and maltopentaose are negligible | Thermococcus sp. | maltose + D-glucose | - |
? | |
maltotriose + H2O | the enzyme displays dual hydrolysis activity toward alpha-1,4- and alpha-1,6-glycosidic linkages, the catalytic efficiency of 6-O-maltosyl-beta-cyclodextrin is 16fold higher than that of maltotriose. Compared to the kcat/Km value toward maltotriose, the values for longer substrates such as maltotetraose and maltopentaose are negligible | Thermococcus sp. CL1 | maltose + D-glucose | - |
? | |
soluble starch + H2O | the enzyme only releases maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan | Thermococcus sp. | maltose + ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
monomer | 1 * 70000, SDS-PAGE | Thermococcus sp. |
Synonyms | Comment | Organism |
---|---|---|
TCMA | - |
Thermococcus sp. |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
85 | - |
alpha-1,4-glycosidic linkage hydrolysis | Thermococcus sp. |
98 | - |
alpha-1,6-glycosidic linkage hydrolysis | Thermococcus sp. |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
60 | 95 | 60°C; about 50% of maximal activity, 60°C: about 60% of maximal activity, alpha-1,4-glycosidic linkage hydrolysis of maltotriose | Thermococcus sp. |
80 | 98 | activity at 80°C is about 50% compared to the activity at 98°C, alpha-1,6-glycosidic linkage hydrolysis of 6-O-maltotetraosyl-beta-cyclodextrin | Thermococcus sp. |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
67 | - |
melting temperature at pH 4.0 | Thermococcus sp. |
85 | - |
the half-life is 69 min, 225 min, and 255 min at pH 5.0, pH 6.0, and pH 7.0 | Thermococcus sp. |
91 | - |
melting temperature at pH 5.0 | Thermococcus sp. |
105 | - |
melting temperature at pH 6.0 | Thermococcus sp. |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
3.85 | - |
maltopentaose | pH 5.0, 85°C | Thermococcus sp. | |
3.95 | - |
maltotetraose | pH 5.0, 85°C | Thermococcus sp. | |
11.45 | - |
maltotriose | pH 5.0, 85°C | Thermococcus sp. |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5 | - |
alpha-1,4-glycosidic linkage hydrolysis | Thermococcus sp. |
6 | - |
alpha-1,6-glycosidic linkage hydrolysis | Thermococcus sp. |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
4 | 6 | pH 4.0: about 85% of maximal activity, pH 6.0: about 60% of maximal activity, alpha-1,4-glycosidic linkage hydrolysis of maltotriose | Thermococcus sp. |
4 | 8 | pH 4.0: about 50% of maximal activity, pH 8.0: about 70% of maximal activity, alpha-1,6-glycosidic linkage hydrolysis of 6-O-maltotetraosyl-beta-cyclodextrin | Thermococcus sp. |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.22 | - |
maltotetraose | pH 5.0, 85°C | Thermococcus sp. | |
0.24 | - |
maltopentaose | pH 5.0, 85°C | Thermococcus sp. | |
2.7 | - |
maltotriose | pH 5.0, 85°C | Thermococcus sp. |