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Literature summary for 3.2.1.135 extracted from
- Pullulan degrading enzymes of bacterial origin (2004), Crit. Rev. Microbiol., 30, 107-121.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in bacteria | Geobacillus stearothermophilus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D328H | site-directed mutagenesis, inactive mutant | Geobacillus stearothermophilus |
| D328N | site-directed mutagenesis, inactive mutant | Geobacillus stearothermophilus |
| D424H | site-directed mutagenesis, inactive mutant | Geobacillus stearothermophilus |
| D424N | site-directed mutagenesis, inactive mutant | Geobacillus stearothermophilus |
| E357H | site-directed mutagenesis, inactive mutant | Geobacillus stearothermophilus |
| E357Q | site-directed mutagenesis, inactive mutant | Geobacillus stearothermophilus |
| I358V | site-directed mutagenesis, the mutant shows increased activity hydrolyzing alpha-1,6-glucosidic bonds, producing maltotriose, compared to the wild-type enzyme | Thermoactinomyces vulgaris |
| I358W | site-directed mutagenesis, the mutant shows decreased activity hydrolyzing alpha-1,6-glucosidic bonds, producing maltotriose, compared to the wild-type enzyme | Thermoactinomyces vulgaris |
| additional information | mutation of residues A357, Q359, and Y360X also leads to increased activity hydrolyzing alpha-1,6-glucosidic bonds, producing maltotriose | Thermoactinomyces vulgaris |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | - |
Paenibacillus polymyxa | - |
- |
| extracellular | - |
Bacteroides thetaiotaomicron | - |
- |
| extracellular | isozyme TVAI | Thermoactinomyces vulgaris | - |
- |
| intracellular | - |
Geobacillus stearothermophilus | 5622 | - |
| intracellular | - |
Alicyclobacillus acidocaldarius | 5622 | - |
| intracellular | isozyme TVAII | Thermoactinomyces vulgaris | 5622 | - |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 58000 | - |
- |
Paenibacillus polymyxa |
| 65000 | - |
enzyme from strain 95-1 | Bacteroides thetaiotaomicron |
| 65000 | - |
isozyme TVAI | Thermoactinomyces vulgaris |
| 66000 | - |
- |
Alicyclobacillus acidocaldarius |
| 69000 | - |
about | Geobacillus stearothermophilus |
| 70000 | - |
enzyme encoded by gene susA | Bacteroides thetaiotaomicron |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| pullulan + H2O | Geobacillus stearothermophilus | - |
6-alpha-D-glucosylmaltose + ? | i.e. panose | ? |  |
| pullulan + H2O | Paenibacillus polymyxa | - |
6-alpha-D-glucosylmaltose + ? | i.e. panose | ? | |
| pullulan + H2O | Thermoactinomyces vulgaris | - |
6-alpha-D-glucosylmaltose + ? | i.e. panose | ? | |
| pullulan + H2O | Bacteroides thetaiotaomicron | - |
6-alpha-D-glucosylmaltose + ? | i.e. panose | ? | |
| pullulan + H2O | Alicyclobacillus acidocaldarius | - |
6-alpha-D-glucosylmaltose + ? | i.e. panose | ? | |
| pullulan + H2O | Thermoactinomyces vulgaris R-47 | - |
6-alpha-D-glucosylmaltose + ? | i.e. panose | ? | |
| pullulan + H2O | Bacteroides thetaiotaomicron 95-1 | - |
6-alpha-D-glucosylmaltose + ? | i.e. panose | ? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Alicyclobacillus acidocaldarius | - |
strain ATCC 27009, gene Cda | - |
| Bacteroides thetaiotaomicron | - |
gene susA | - |
| Bacteroides thetaiotaomicron 95-1 | - |
gene susA | - |
| Geobacillus stearothermophilus | - |
strains TRS40, gene nplT | - |
| Paenibacillus polymyxa | - |
- |
- |
| Thermoactinomyces vulgaris | - |
genes TVAI and TVAII | - |
| Thermoactinomyces vulgaris R-47 | - |
genes TVAI and TVAII | - |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| pullulan + H2O = panose | acidic residues determine the substrate specificity, residues A357, Q359, and Y360, located in region II, are involved in action pattern formation | Thermoactinomyces vulgaris | |
| pullulan + H2O = panose | residues E357, D424, and D328 are involved in the catalytic reaction at the active site, residues H423, E332, and N331 are involved in substrate recognition | Geobacillus stearothermophilus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the enzyme also shows alpha-amylase activity hydrolysing alpha-1,6-glucosidic bonds, enzyme substrate specificity is determined by two Asp and one Glu residues | Thermoactinomyces vulgaris | ? | - |
? | |
| additional information | the enzyme also shows alpha-amylase activity hydrolysing alpha-1,6-glucosidic bonds, enzyme substrate specificity is determined by two Asp and one Glu residues | Thermoactinomyces vulgaris R-47 | ? | - |
? | |
| pullulan + H2O | - |
Geobacillus stearothermophilus | 6-alpha-D-glucosylmaltose + ? | i.e. panose | ? | |
| pullulan + H2O | - |
Paenibacillus polymyxa | 6-alpha-D-glucosylmaltose + ? | i.e. panose | ? | |
| pullulan + H2O | - |
Thermoactinomyces vulgaris | 6-alpha-D-glucosylmaltose + ? | i.e. panose | ? | |
| pullulan + H2O | - |
Bacteroides thetaiotaomicron | 6-alpha-D-glucosylmaltose + ? | i.e. panose | ? | |
| pullulan + H2O | - |
Alicyclobacillus acidocaldarius | 6-alpha-D-glucosylmaltose + ? | i.e. panose | ? | |
| pullulan + H2O | hydrolysis of alpha-1,4-glucosidic linkages | Thermoactinomyces vulgaris | 6-alpha-D-glucosylmaltose + ? | i.e. panose | ? | |
| pullulan + H2O | - |
Thermoactinomyces vulgaris R-47 | 6-alpha-D-glucosylmaltose + ? | i.e. panose | ? | |
| pullulan + H2O | hydrolysis of alpha-1,4-glucosidic linkages | Thermoactinomyces vulgaris R-47 | 6-alpha-D-glucosylmaltose + ? | i.e. panose | ? | |
| pullulan + H2O | - |
Bacteroides thetaiotaomicron 95-1 | 6-alpha-D-glucosylmaltose + ? | i.e. panose | ? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | analysis of conserved regions in the enzyme primary sequence, overview | Geobacillus stearothermophilus |
| More | analysis of conserved regions in the enzyme primary sequence, overview | Thermoactinomyces vulgaris |
| More | analysis of conserved regions in the enzyme primary structure, overview | Paenibacillus polymyxa |
| More | analysis of conserved regions in the enzyme primary structure, overview | Bacteroides thetaiotaomicron |
| More | analysis of conserved regions in the enzyme primary structure, overview | Alicyclobacillus acidocaldarius |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| More | bifunctional enzyme, cf. EC 3.2.1.1, alpha-amylase | Thermoactinomyces vulgaris |
| neopullulanase-alpha-amylase | - |
Thermoactinomyces vulgaris |
| pullulan 4-D-glucanohydrolase (6-alpha-D-glucosylmaltose) | - |
Geobacillus stearothermophilus |
| pullulan 4-D-glucanohydrolase (6-alpha-D-glucosylmaltose) | - |
Paenibacillus polymyxa |
| pullulan 4-D-glucanohydrolase (6-alpha-D-glucosylmaltose) | - |
Thermoactinomyces vulgaris |
| pullulan 4-D-glucanohydrolase (6-alpha-D-glucosylmaltose) | - |
Bacteroides thetaiotaomicron |
| pullulan 4-D-glucanohydrolase (6-alpha-D-glucosylmaltose) | - |
Alicyclobacillus acidocaldarius |
| pullulan hydrolase type I | - |
Geobacillus stearothermophilus |
| pullulan hydrolase type I | - |
Paenibacillus polymyxa |
| pullulan hydrolase type I | - |
Thermoactinomyces vulgaris |
| pullulan hydrolase type I | - |
Bacteroides thetaiotaomicron |
| pullulan hydrolase type I | - |
Alicyclobacillus acidocaldarius |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
optimal growth temperature is 30-70°C | Paenibacillus polymyxa |
| 40 | - |
- |
Thermoactinomyces vulgaris |
| 50 | - |
- |
Paenibacillus polymyxa |
| 55 | - |
- |
Alicyclobacillus acidocaldarius |
| 60 | 70 | - |
Geobacillus stearothermophilus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5 | - |
isozyme TVAI | Thermoactinomyces vulgaris |
| 5.5 | - |
- |
Alicyclobacillus acidocaldarius |
| 6 | - |
- |
Paenibacillus polymyxa |
| 6 | - |
isozyme TVAII | Thermoactinomyces vulgaris |
| 7.5 | - |
enzyme from strain 95-1 | Bacteroides thetaiotaomicron |
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Release 2023.1 (January 2023)
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