Any feedback?
Literature summary extracted from
- Pullulan degrading enzymes of bacterial origin (2004), Crit. Rev. Microbiol., 30, 107-121.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.2.1.135 | expression in bacteria | Geobacillus stearothermophilus |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.2.1.135 | D328H | site-directed mutagenesis, inactive mutant | Geobacillus stearothermophilus |
| 3.2.1.135 | D328N | site-directed mutagenesis, inactive mutant | Geobacillus stearothermophilus |
| 3.2.1.135 | D424H | site-directed mutagenesis, inactive mutant | Geobacillus stearothermophilus |
| 3.2.1.135 | D424N | site-directed mutagenesis, inactive mutant | Geobacillus stearothermophilus |
| 3.2.1.135 | E357H | site-directed mutagenesis, inactive mutant | Geobacillus stearothermophilus |
| 3.2.1.135 | E357Q | site-directed mutagenesis, inactive mutant | Geobacillus stearothermophilus |
| 3.2.1.135 | 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 |
| 3.2.1.135 | 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 |
| 3.2.1.135 | 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
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.2.1.135 | extracellular | - |
Paenibacillus polymyxa | - |
- |
| 3.2.1.135 | extracellular | - |
Bacteroides thetaiotaomicron | - |
- |
| 3.2.1.135 | extracellular | isozyme TVAI | Thermoactinomyces vulgaris | - |
- |
| 3.2.1.135 | intracellular | - |
Geobacillus stearothermophilus | 5622 | - |
| 3.2.1.135 | intracellular | - |
Alicyclobacillus acidocaldarius | 5622 | - |
| 3.2.1.135 | intracellular | isozyme TVAII | Thermoactinomyces vulgaris | 5622 | - |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.135 | 58000 | - |
- |
Paenibacillus polymyxa |
| 3.2.1.135 | 65000 | - |
enzyme from strain 95-1 | Bacteroides thetaiotaomicron |
| 3.2.1.135 | 65000 | - |
isozyme TVAI | Thermoactinomyces vulgaris |
| 3.2.1.135 | 66000 | - |
- |
Alicyclobacillus acidocaldarius |
| 3.2.1.135 | 69000 | - |
about | Geobacillus stearothermophilus |
| 3.2.1.135 | 70000 | - |
enzyme encoded by gene susA | Bacteroides thetaiotaomicron |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.135 | pullulan + H2O | Geobacillus stearothermophilus | - |
6-alpha-D-glucosylmaltose + ? | i.e. panose | ? |  |
| 3.2.1.135 | pullulan + H2O | Paenibacillus polymyxa | - |
6-alpha-D-glucosylmaltose + ? | i.e. panose | ? | |
| 3.2.1.135 | pullulan + H2O | Thermoactinomyces vulgaris | - |
6-alpha-D-glucosylmaltose + ? | i.e. panose | ? | |
| 3.2.1.135 | pullulan + H2O | Bacteroides thetaiotaomicron | - |
6-alpha-D-glucosylmaltose + ? | i.e. panose | ? | |
| 3.2.1.135 | pullulan + H2O | Alicyclobacillus acidocaldarius | - |
6-alpha-D-glucosylmaltose + ? | i.e. panose | ? | |
| 3.2.1.135 | pullulan + H2O | Thermoactinomyces vulgaris R-47 | - |
6-alpha-D-glucosylmaltose + ? | i.e. panose | ? | |
| 3.2.1.135 | pullulan + H2O | Bacteroides thetaiotaomicron 95-1 | - |
6-alpha-D-glucosylmaltose + ? | i.e. panose | ? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.2.1.135 | Alicyclobacillus acidocaldarius | - |
strain ATCC 27009, gene Cda | - |
| 3.2.1.135 | Bacteroides thetaiotaomicron | - |
gene susA | - |
| 3.2.1.135 | Bacteroides thetaiotaomicron 95-1 | - |
gene susA | - |
| 3.2.1.135 | Geobacillus stearothermophilus | - |
strains TRS40, gene nplT | - |
| 3.2.1.135 | Paenibacillus polymyxa | - |
- |
- |
| 3.2.1.135 | Thermoactinomyces vulgaris | - |
genes TVAI and TVAII | - |
| 3.2.1.135 | Thermoactinomyces vulgaris R-47 | - |
genes TVAI and TVAII | - |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 3.2.1.135 | 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 | |
| 3.2.1.135 | 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)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.135 | 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 | ? | - |
? | |
| 3.2.1.135 | 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 | ? | - |
? | |
| 3.2.1.135 | pullulan + H2O | - |
Geobacillus stearothermophilus | 6-alpha-D-glucosylmaltose + ? | i.e. panose | ? | |
| 3.2.1.135 | pullulan + H2O | - |
Paenibacillus polymyxa | 6-alpha-D-glucosylmaltose + ? | i.e. panose | ? | |
| 3.2.1.135 | pullulan + H2O | - |
Thermoactinomyces vulgaris | 6-alpha-D-glucosylmaltose + ? | i.e. panose | ? | |
| 3.2.1.135 | pullulan + H2O | - |
Bacteroides thetaiotaomicron | 6-alpha-D-glucosylmaltose + ? | i.e. panose | ? | |
| 3.2.1.135 | pullulan + H2O | - |
Alicyclobacillus acidocaldarius | 6-alpha-D-glucosylmaltose + ? | i.e. panose | ? | |
| 3.2.1.135 | pullulan + H2O | hydrolysis of alpha-1,4-glucosidic linkages | Thermoactinomyces vulgaris | 6-alpha-D-glucosylmaltose + ? | i.e. panose | ? | |
| 3.2.1.135 | pullulan + H2O | - |
Thermoactinomyces vulgaris R-47 | 6-alpha-D-glucosylmaltose + ? | i.e. panose | ? | |
| 3.2.1.135 | pullulan + H2O | hydrolysis of alpha-1,4-glucosidic linkages | Thermoactinomyces vulgaris R-47 | 6-alpha-D-glucosylmaltose + ? | i.e. panose | ? | |
| 3.2.1.135 | pullulan + H2O | - |
Bacteroides thetaiotaomicron 95-1 | 6-alpha-D-glucosylmaltose + ? | i.e. panose | ? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.2.1.135 | More | analysis of conserved regions in the enzyme primary sequence, overview | Geobacillus stearothermophilus |
| 3.2.1.135 | More | analysis of conserved regions in the enzyme primary sequence, overview | Thermoactinomyces vulgaris |
| 3.2.1.135 | More | analysis of conserved regions in the enzyme primary structure, overview | Paenibacillus polymyxa |
| 3.2.1.135 | More | analysis of conserved regions in the enzyme primary structure, overview | Bacteroides thetaiotaomicron |
| 3.2.1.135 | More | analysis of conserved regions in the enzyme primary structure, overview | Alicyclobacillus acidocaldarius |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.2.1.135 | More | bifunctional enzyme, cf. EC 3.2.1.1, alpha-amylase | Thermoactinomyces vulgaris |
| 3.2.1.135 | neopullulanase-alpha-amylase | - |
Thermoactinomyces vulgaris |
| 3.2.1.135 | pullulan 4-D-glucanohydrolase (6-alpha-D-glucosylmaltose) | - |
Geobacillus stearothermophilus |
| 3.2.1.135 | pullulan 4-D-glucanohydrolase (6-alpha-D-glucosylmaltose) | - |
Paenibacillus polymyxa |
| 3.2.1.135 | pullulan 4-D-glucanohydrolase (6-alpha-D-glucosylmaltose) | - |
Thermoactinomyces vulgaris |
| 3.2.1.135 | pullulan 4-D-glucanohydrolase (6-alpha-D-glucosylmaltose) | - |
Bacteroides thetaiotaomicron |
| 3.2.1.135 | pullulan 4-D-glucanohydrolase (6-alpha-D-glucosylmaltose) | - |
Alicyclobacillus acidocaldarius |
| 3.2.1.135 | pullulan hydrolase type I | - |
Geobacillus stearothermophilus |
| 3.2.1.135 | pullulan hydrolase type I | - |
Paenibacillus polymyxa |
| 3.2.1.135 | pullulan hydrolase type I | - |
Thermoactinomyces vulgaris |
| 3.2.1.135 | pullulan hydrolase type I | - |
Bacteroides thetaiotaomicron |
| 3.2.1.135 | pullulan hydrolase type I | - |
Alicyclobacillus acidocaldarius |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.135 | additional information | - |
optimal growth temperature is 30-70°C | Paenibacillus polymyxa |
| 3.2.1.135 | 40 | - |
- |
Thermoactinomyces vulgaris |
| 3.2.1.135 | 50 | - |
- |
Paenibacillus polymyxa |
| 3.2.1.135 | 55 | - |
- |
Alicyclobacillus acidocaldarius |
| 3.2.1.135 | 60 | 70 | - |
Geobacillus stearothermophilus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.135 | 5 | - |
isozyme TVAI | Thermoactinomyces vulgaris |
| 3.2.1.135 | 5.5 | - |
- |
Alicyclobacillus acidocaldarius |
| 3.2.1.135 | 6 | - |
- |
Paenibacillus polymyxa |
| 3.2.1.135 | 6 | - |
isozyme TVAII | Thermoactinomyces vulgaris |
| 3.2.1.135 | 7.5 | - |
enzyme from strain 95-1 | Bacteroides thetaiotaomicron |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
