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Literature summary for 3.2.1.41 extracted from
- Characterization of amylolytic enzymes, having both alpha-1,4 and alpha-1,6 hydrolytic activity, from the thermophilic archaea Pyrococcus furiosus and Thermococcus litoralis (1993), Appl. Environ. Microbiol., 59, 2614-2621.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | 5 mM, the pullulan hydrolyzing activity is stimulated by about 25%, slight enhancing effect on hydrolysis of 4-nitrophenyl-alpha-D-maltotrioside | Pyrococcus furiosus |  |
| Ca2+ | 5 mM, the pullulan hydrolyzing activity is stimulated by about 25%, slight enhancing effect on hydrolysis of 4-nitrophenyl-alpha-D-maltotrioside | Thermococcus litoralis | |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | 5 mM, starch-hydrolyzing activity is inhibited by about 30%, hydrolytic activity against glycogen is slightly inhibited | Pyrococcus furiosus | |
| Ca2+ | 5 mM, starch-hydrolyzing activity is inhibited by about 14%, hydrolytic activity against glycogen is slightly inhibited | Thermococcus litoralis | |
| Mg2+ | reduces the thermoactivity of the enzymes below the level seen in the absence of added metal | Pyrococcus furiosus | |
| Mg2+ | reduces the thermoactivity of the enzymes below the level seen in the absence of added metal | Thermococcus litoralis | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Ca2+ causes a 10fold decrease in Km | Pyrococcus furiosus | |
| additional information | - |
additional information | Ca2+ causes a 10fold decrease in Km | Thermococcus litoralis | |
| 0.037 | - |
4-nitrophenyl alpha-D-maltotrioside | pH 5.6, 98°C, 5 mM Ca2+ | Thermococcus litoralis | |
| 0.067 | - |
4-nitrophenyl alpha-D-maltotrioside | pH 5.6, 98°C, no metal added | Thermococcus litoralis | |
| 0.077 | - |
4-nitrophenyl alpha-D-maltotrioside | pH 5.6, 98°C, 5 mM Ca2+ | Pyrococcus furiosus | |
| 0.664 | - |
4-nitrophenyl alpha-D-maltotrioside | pH 5.6, 98°C, no metal added | Pyrococcus furiosus | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | - |
Thermococcus litoralis | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | thermoactivity and thermostability of the enzyme is enhanced in the presence of 5 mM Ca2+, and under these conditions, enzyme activity can be measured at temperatures of up to 130 to 140°C | Pyrococcus furiosus | |
| Ca2+ | thermoactivity and thermostability of the enzyme is enhanced in the presence of 5 mM Ca2+, and under these conditions, enzyme activity can be measured at temperatures of up to 130 to 140°C | Thermococcus litoralis | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 110000 | - |
1 * 110000, SDS-PAGE | Pyrococcus furiosus |
| 119000 | - |
1 * 119000, SDS-PAGE | Thermococcus litoralis |
| 125000 | - |
gel filtration | Thermococcus litoralis |
| 135000 | - |
gel filtration | Pyrococcus furiosus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pyrococcus furiosus | - |
- |
- |
| Thermococcus litoralis | - |
- |
- |
| Thermococcus litoralis DSM 5473 | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | - |
Pyrococcus furiosus |
| glycoprotein | - |
Thermococcus litoralis |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Pyrococcus furiosus |
- |
Thermococcus litoralis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-nitrophenyl alpha-D-maltoheptaoside + H2O | hydrolyzed in an exo-fashion | Pyrococcus furiosus | 4-nitrophenol + alpha-D-maltoheptaose | - |
? | |
| 4-nitrophenyl alpha-D-maltoheptaoside + H2O | hydrolyzed in an exo-fashion | Thermococcus litoralis | 4-nitrophenol + alpha-D-maltoheptaose | - |
? | |
| 4-nitrophenyl alpha-D-maltoheptaoside + H2O | hydrolyzed in an exo-fashion | Thermococcus litoralis DSM 5473 | 4-nitrophenol + alpha-D-maltoheptaose | - |
? | |
| 4-nitrophenyl alpha-D-maltotrioside + H2O | hydrolyzed in an exo-fashion | Pyrococcus furiosus | 4-nitrophenol + alpha-D-maltotriose | - |
? | |
| 4-nitrophenyl alpha-D-maltotrioside + H2O | hydrolyzed in an exo-fashion | Thermococcus litoralis | 4-nitrophenol + alpha-D-maltotriose | - |
? | |
| glycogen + H2O | hydrolyzed slowly. Hydrolyzed in an endo fashion to form a series of oligosaccharides as small as glucose, with the majority of product in the DP4 to DP6 range | Pyrococcus furiosus | ? | - |
? | |
| glycogen + H2O | hydrolyzed slowly. Hydrolyzed in an endo fashion to form a series of oligosaccharides as small as glucose, with the majority of product in the DP4 to DP6 range | Thermococcus litoralis | ? | - |
? | |
| glycogen + H2O | hydrolyzed slowly. Hydrolyzed in an endo fashion to form a series of oligosaccharides as small as glucose, with the majority of product in the DP4 to DP6 range | Thermococcus litoralis DSM 5473 | ? | - |
? | |
| additional information | hydrolyzes the alpha-1,6 linkage in pullulan, alpha-1,4 linkages in amylose and soluble starch. No activity against maltohexaose or other smaller alpha-1,4-linked oligosaccharides | Pyrococcus furiosus | ? | - |
? | |
| additional information | hydrolyzes the alpha-1,6 linkage in pullulan, alpha-1,4 linkages in amylose and soluble starch. No activity against maltohexaose or other smaller alpha-1,4-linked oligosaccharides | Thermococcus litoralis | ? | - |
? | |
| additional information | hydrolyzes the alpha-1,6 linkage in pullulan, alpha-1,4 linkages in amylose and soluble starch. No activity against maltohexaose or other smaller alpha-1,4-linked oligosaccharides | Thermococcus litoralis DSM 5473 | ? | - |
? | |
| pullulan + H2O | higher specific activity against pullulan than against starch. Enzyme attacks only the alpha-1,6 linkages in pullulan | Pyrococcus furiosus | maltotriose + ? | - |
? | |
| pullulan + H2O | higher specific activity against pullulan than against starch. Enzyme attacks only the alpha-1,6 linkages in pullulan | Thermococcus litoralis | maltotriose + ? | - |
? | |
| pullulan + H2O | higher specific activity against pullulan than against starch. Enzyme attacks only the alpha-1,6 linkages in pullulan | Thermococcus litoralis DSM 5473 | maltotriose + ? | - |
? | |
| starch + H2O | higher specific activity against pullulan than against starch. Hydrolyzed in an endo fashion to form a series of oligosaccharides as small as glucose, with the majority of product in the DP4 to DP6 range | Pyrococcus furiosus | ? | - |
? | |
| starch + H2O | higher specific activity against pullulan than against starch. Hydrolyzed in an endo fashion to form a series of oligosaccharides as small as glucose, with the majority of product in the DP4 to DP6 range | Thermococcus litoralis | ? | - |
? | |
| starch + H2O | higher specific activity against pullulan than against starch. Hydrolyzed in an endo fashion to form a series of oligosaccharides as small as glucose, with the majority of product in the DP4 to DP6 range | Thermococcus litoralis DSM 5473 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | 1 * 110000, SDS-PAGE | Pyrococcus furiosus |
| monomer | 1 * 119000, SDS-PAGE | Thermococcus litoralis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| amylopullulanase | - |
Pyrococcus furiosus |
| amylopullulanase | - |
Thermococcus litoralis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 95 | - |
substrate: pullulan or starch, no metal added | Thermococcus litoralis |
| 95 | - |
substrate: pullulan, no metal added | Pyrococcus furiosus |
| 115 | - |
substrate: pullulan or starch, 5 mM Ca2+ | Thermococcus litoralis |
| 115 | - |
substrate: starch, no metal added | Pyrococcus furiosus |
| 125 | - |
substrate: pullulan or starch, 5 mM Ca2+ | Pyrococcus furiosus |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
the presence of Ca2+ has a significant positive effect on enzyme activity at temperatures above 120°C, extending the range at which activity can be measured up to 130 to 140°C | Pyrococcus furiosus |
| additional information | - |
the presence of Ca2+ has a significant positive effect on enzyme activity at temperatures above 120°C, extending the range at which activity can be measured up to 130 to 140°C | Thermococcus litoralis |
| 90 | 125 | 90°C: about 50% of maximal activity, 125°C: about 50% of maximal activity, substrate: starch, no metal added | Pyrococcus furiosus |
| 90 | 125 | 90°C: about 50% of maximal activity, 135°C: about 50% of maximal activity, substrate: pullulan, 5 mM Ca2+ | Thermococcus litoralis |
| 90 | 125 | 90°C: about 75% of maximal activity, 125°C: about 45% of maximal activity, substrate: pullulan, no metal added | Pyrococcus furiosus |
| 90 | 135 | 90°C: about 60% of maximal activity, 135°C: about 55% of maximal activity, substrate: pullulan, 5 mM Ca2+ | Pyrococcus furiosus |
| 90 | 115 | 90°C: about 60% of maximal activity, 125°C: about 70% of maximal activity, substrate: pullulan, no metal added | Thermococcus litoralis |
| 90 | 115 | 90°C: about 60% of maximal activity, 125°C: about 75% of maximal activity, substrate: starch, no metal added | Thermococcus litoralis |
| 95 | 125 | 100°C: about 65% of maximal activity, 135°C: about 80% of maximal activity, substrate: starch, 5 mM Ca2+ | Thermococcus litoralis |
| 100 | 135 | 100°C: about 40% of maximal activity, 135°C: about 60% of maximal activity, substrate: starch, 5 mM Ca2+ | Pyrococcus furiosus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
thermostability of the enzyme is enhanced in the presence of 5 mM Ca2+ | Pyrococcus furiosus |
| additional information | - |
thermostability of the enzyme is enhanced in the presence of 5 mM Ca2+ | Thermococcus litoralis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5.5 | - |
- |
Pyrococcus furiosus |
| 5.5 | - |
- |
Thermococcus litoralis |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 4.5 | 7.8 | 20% of maximal activity at pH 4.5 - pH 7.8 | Pyrococcus furiosus |
| 4.5 | 7.8 | 20% of maximal activity at pH 4.5 - pH 7.8 | Thermococcus litoralis |
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