EC Number | Cloned (Comment) | Organism |
---|---|---|
3.2.1.2 | expressed the gene in Escherichia coli | Thermococcus sp. |
3.2.1.B36 | expressed the gene in Escherichia coli | Thermococcus sp. |
3.2.1.133 | expressed the gene in Escherichia coli | Thermococcus sp. |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.2.1.2 | 4.25 | - |
maltotriose | pH 5.0, 85°C | Thermococcus sp. | |
3.2.1.2 | 16.2 | - |
maltopentaose | pH 5.0, 85°C | Thermococcus sp. | |
3.2.1.2 | 18.2 | - |
maltotetraose | pH 5.0, 85°C | Thermococcus sp. | |
3.2.1.B36 | 0.7 | - |
6-O-maltotetraosyl-beta-cyclodextrin | pH 6.0, 98°C | Thermococcus sp. | |
3.2.1.B36 | 4.25 | - |
maltotriose | pH 5.0, 85°C | Thermococcus sp. | |
3.2.1.B36 | 16.2 | - |
maltopentaose | pH 5.0, 85°C | Thermococcus sp. | |
3.2.1.B36 | 18.2 | - |
maltotetraose | pH 5.0, 85°C | Thermococcus sp. | |
3.2.1.133 | 4.25 | - |
maltotriose | pH 5.0, 85°C | Thermococcus sp. | |
3.2.1.133 | 16.2 | - |
maltopentaose | pH 5.0, 85°C | Thermococcus sp. | |
3.2.1.133 | 18.2 | - |
maltotetraose | pH 5.0, 85°C | Thermococcus sp. |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
3.2.1.2 | intracellular | - |
Thermococcus sp. | 5622 | - |
3.2.1.B36 | intracellular | - |
Thermococcus sp. | 5622 | - |
3.2.1.133 | intracellular | - |
Thermococcus sp. | 5622 | - |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.2.1.2 | 67120 | - |
- |
Thermococcus sp. |
3.2.1.2 | 70000 | - |
1 * 70000, SDS-PAGE | Thermococcus sp. |
3.2.1.B36 | 67120 | - |
- |
Thermococcus sp. |
3.2.1.B36 | 70000 | - |
1 * 70000, SDS-PAGE | Thermococcus sp. |
3.2.1.133 | 67120 | - |
- |
Thermococcus sp. |
3.2.1.133 | 70000 | - |
1 * 70000, SDS-PAGE | Thermococcus sp. |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.2 | Thermococcus sp. | I3ZTN9 | - |
- |
3.2.1.2 | Thermococcus sp. CL1 | I3ZTN9 | - |
- |
3.2.1.B36 | Thermococcus sp. | I3ZTN9 | - |
- |
3.2.1.B36 | Thermococcus sp. CL1 | I3ZTN9 | - |
- |
3.2.1.133 | Thermococcus sp. | I3ZTN9 | - |
- |
3.2.1.133 | Thermococcus sp. CL1 | I3ZTN9 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.2 | 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 + ? | - |
? | |
3.2.1.2 | 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 + ? | - |
? | |
3.2.1.2 | 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 + ? | - |
? | |
3.2.1.2 | 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 + ? | - |
? | |
3.2.1.2 | 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 | - |
? | |
3.2.1.2 | 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 | - |
? | |
3.2.1.2 | 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 | - |
? | |
3.2.1.2 | 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 | - |
? | |
3.2.1.2 | 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 | - |
? | |
3.2.1.2 | 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 | - |
? | |
3.2.1.2 | 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 + ? | - |
? | |
3.2.1.B36 | 6-O-maltosyl-beta-cyclodextrin + 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 + beta-cyclodextrin | - |
? | |
3.2.1.B36 | 6-O-maltotetraosyl-beta-cyclodextrin + H2O | - |
Thermococcus sp. | 2 maltose + beta-cyclodextrin | - |
? | |
3.2.1.B36 | amylopectin + H2O | the enzyme only released maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan | Thermococcus sp. | maltose + ? | - |
? | |
3.2.1.B36 | glycogen + H2O | the enzyme only released maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan | Thermococcus sp. | maltose + ? | - |
? | |
3.2.1.B36 | 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 | - |
? | |
3.2.1.B36 | 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 | - |
? | |
3.2.1.B36 | 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 | - |
? | |
3.2.1.B36 | soluble starch + H2O | the enzyme only released maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan | Thermococcus sp. | maltose + ? | - |
? | |
3.2.1.133 | 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 + ? | - |
? | |
3.2.1.133 | 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 + ? | - |
? | |
3.2.1.133 | 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 | - |
? | |
3.2.1.133 | 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 | - |
? | |
3.2.1.133 | 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 | - |
? | |
3.2.1.133 | 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 + ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.2.1.2 | monomer | 1 * 70000, SDS-PAGE | Thermococcus sp. |
3.2.1.B36 | monomer | 1 * 70000, SDS-PAGE | Thermococcus sp. |
3.2.1.133 | monomer | 1 * 70000, SDS-PAGE | Thermococcus sp. |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.2.1.2 | TCMA | - |
Thermococcus sp. |
3.2.1.B36 | TCMA | - |
Thermococcus sp. |
3.2.1.133 | TCMA | - |
Thermococcus sp. |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.2 | 85 | - |
alpha-1,4-glycosidic linkage hydrolysis | Thermococcus sp. |
3.2.1.2 | 98 | - |
alpha-1,6-glycosidic linkage hydrolysis | Thermococcus sp. |
3.2.1.B36 | 85 | - |
alpha-1,4-glycosidic linkage hydrolysis | Thermococcus sp. |
3.2.1.B36 | 98 | - |
alpha-1,6-glycosidic linkage hydrolysis | Thermococcus sp. |
3.2.1.133 | 85 | - |
alpha-1,4-glycosidic linkage hydrolysis | Thermococcus sp. |
3.2.1.133 | 98 | - |
alpha-1,6-glycosidic linkage hydrolysis | Thermococcus sp. |
EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.2 | 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. |
3.2.1.2 | 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. |
3.2.1.B36 | 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. |
3.2.1.B36 | 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. |
3.2.1.133 | 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. |
3.2.1.133 | 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. |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.2 | 67 | - |
melting temperature at pH 4.0 | Thermococcus sp. |
3.2.1.2 | 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. |
3.2.1.2 | 91 | - |
melting temperature at pH 5.0 | Thermococcus sp. |
3.2.1.2 | 105 | - |
melting temperature at pH 6.0 | Thermococcus sp. |
3.2.1.B36 | 67 | - |
melting temperature at pH 4.0 | Thermococcus sp. |
3.2.1.B36 | 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. |
3.2.1.B36 | 91 | - |
melting temperature at pH 5.0 | Thermococcus sp. |
3.2.1.B36 | 105 | - |
melting temperature at pH 6.0 | Thermococcus sp. |
3.2.1.133 | 67 | - |
melting temperature at pH 4.0 | Thermococcus sp. |
3.2.1.133 | 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. |
3.2.1.133 | 91 | - |
melting temperature at pH 5.0 | Thermococcus sp. |
3.2.1.133 | 105 | - |
melting temperature at pH 6.0 | Thermococcus sp. |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.2.1.2 | 3.85 | - |
maltopentaose | pH 5.0, 85°C | Thermococcus sp. | |
3.2.1.2 | 3.95 | - |
maltotetraose | pH 5.0, 85°C | Thermococcus sp. | |
3.2.1.2 | 11.45 | - |
maltotriose | pH 5.0, 85°C | Thermococcus sp. | |
3.2.1.B36 | 3.85 | - |
maltopentaose | pH 5.0, 85°C | Thermococcus sp. | |
3.2.1.B36 | 3.95 | - |
maltotetraose | pH 5.0, 85°C | Thermococcus sp. | |
3.2.1.B36 | 11.45 | - |
maltotriose | pH 5.0, 85°C | Thermococcus sp. | |
3.2.1.B36 | 30.1 | - |
6-O-maltotetraosyl-beta-cyclodextrin | pH 6.0, 98°C | Thermococcus sp. | |
3.2.1.133 | 3.85 | - |
maltopentaose | pH 5.0, 85°C | Thermococcus sp. | |
3.2.1.133 | 3.95 | - |
maltotetraose | pH 5.0, 85°C | Thermococcus sp. | |
3.2.1.133 | 11.45 | - |
maltotriose | pH 5.0, 85°C | Thermococcus sp. |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.2.1.2 | 5 | - |
alpha-1,4-glycosidic linkage hydrolysis | Thermococcus sp. |
3.2.1.2 | 6 | - |
alpha-1,6-glycosidic linkage hydrolysis | Thermococcus sp. |
3.2.1.B36 | 5 | - |
alpha-1,4-glycosidic linkage hydrolysis | Thermococcus sp. |
3.2.1.B36 | 6 | - |
alpha-1,6-glycosidic linkage hydrolysis | Thermococcus sp. |
3.2.1.133 | 5 | - |
alpha-1,4-glycosidic linkage hydrolysis | Thermococcus sp. |
3.2.1.133 | 6 | - |
alpha-1,6-glycosidic linkage hydrolysis | Thermococcus sp. |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
3.2.1.2 | 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. |
3.2.1.2 | 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. |
3.2.1.B36 | 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. |
3.2.1.B36 | 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. |
3.2.1.133 | 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. |
3.2.1.133 | 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. |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.2.1.2 | 0.22 | - |
maltotetraose | pH 5.0, 85°C | Thermococcus sp. | |
3.2.1.2 | 0.24 | - |
maltopentaose | pH 5.0, 85°C | Thermococcus sp. | |
3.2.1.2 | 2.7 | - |
maltotriose | pH 5.0, 85°C | Thermococcus sp. | |
3.2.1.B36 | 0.22 | - |
maltotetraose | pH 5.0, 85°C | Thermococcus sp. | |
3.2.1.B36 | 0.24 | - |
maltopentaose | pH 5.0, 85°C | Thermococcus sp. | |
3.2.1.B36 | 2.7 | - |
maltotriose | pH 5.0, 85°C | Thermococcus sp. | |
3.2.1.B36 | 42.8 | - |
6-O-maltotetraosyl-beta-cyclodextrin | pH 6.0, 98°C | Thermococcus sp. | |
3.2.1.133 | 0.22 | - |
maltotetraose | pH 5.0, 85°C | Thermococcus sp. | |
3.2.1.133 | 0.24 | - |
maltopentaose | pH 5.0, 85°C | Thermococcus sp. | |
3.2.1.133 | 2.7 | - |
maltotriose | pH 5.0, 85°C | Thermococcus sp. |