Cloned (Comment) | Organism |
---|---|
expression in bacteria | Geobacillus stearothermophilus |
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 | 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 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 | 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 | 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 | 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 | 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 | 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 | 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 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 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 |