EC Number | Cloned (Comment) | Organism |
---|---|---|
3.2.1.54 | - |
Bacillus sp. (in: Bacteria) |
3.2.1.54 | - |
Thermoanaerobacter ethanolicus |
3.2.1.54 | DNA sequence determination and analysis | Klebsiella oxytoca |
3.2.1.54 | DNA sequence determination and analysis, expression in Escherichia coli | Thermotoga maritima |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.2.1.54 | I388E | mutant from strain I-5, decreased hydrophobicity, between the third and the fourth conserved region resulting in decreased cyclomaltodextrin degrading activity | Bacillus sp. (in: Bacteria) |
3.2.1.54 | additional information | single mutants of the catalytic residues Asp325, Glu354, and Asp421 are catalytically inactive | Thermoanaerobacter ethanolicus |
3.2.1.54 | V380T | mutant from strain I-5, decreased hydrophobicity, between the third and the fourth conserved region resulting in decreased cyclomaltodextrin degrading activity | Bacillus sp. (in: Bacteria) |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
3.2.1.54 | cytoplasm | - |
Klebsiella oxytoca | 5737 | - |
3.2.1.54 | periplasm | - |
Xanthomonas campestris | - |
- |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.2.1.54 | 55000 | - |
x * 55000 | Xanthomonas campestris |
3.2.1.54 | 55000 | - |
x * 55000 | Thermotoga maritima |
3.2.1.54 | 62000 | - |
x * 62000 | Weizmannia coagulans |
3.2.1.54 | 62000 | - |
1 * 62000 | Flavobacterium sp. |
3.2.1.54 | 65000 | - |
8 * 65000, strain I-5, in solution | Bacillus sp. (in: Bacteria) |
3.2.1.54 | 66000 | - |
x * 66000 | Escherichia coli |
3.2.1.54 | 66000 | - |
1 * 66000 | Thermoanaerobacter ethanolicus |
3.2.1.54 | 67000 | - |
2 * 67000 | Geobacillus stearothermophilus |
3.2.1.54 | 67000 | - |
2 * 67000, alkalophilic strain | Bacillus sp. (in: Bacteria) |
3.2.1.54 | 69000 | - |
x * 69000 | Klebsiella oxytoca |
3.2.1.54 | 72000 | - |
2 * 91200-95000, strain ATCC7055, 2 * 72000, strain E-244 | Lysinibacillus sphaericus |
3.2.1.135 | 62000 | - |
- |
Geobacillus stearothermophilus |
3.2.1.135 | 66000 | - |
- |
Klebsiella pneumoniae |
3.2.1.135 | 68000 | - |
- |
Bacillus sp. KSM-1876 |
3.2.1.135 | 70000 | - |
- |
Bacteroides thetaiotaomicron |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.54 | additional information | Escherichia coli | physiological role of the enzyme | ? | - |
? | |
3.2.1.54 | additional information | Geobacillus stearothermophilus | physiological role of the enzyme | ? | - |
? | |
3.2.1.54 | additional information | Lysinibacillus sphaericus | physiological role of the enzyme | ? | - |
? | |
3.2.1.54 | additional information | Weizmannia coagulans | physiological role of the enzyme | ? | - |
? | |
3.2.1.54 | additional information | Bacillus sp. (in: Bacteria) | physiological role of the enzyme | ? | - |
? | |
3.2.1.54 | additional information | Paenibacillus macerans | physiological role of the enzyme | ? | - |
? | |
3.2.1.54 | additional information | Xanthomonas campestris | physiological role of the enzyme | ? | - |
? | |
3.2.1.54 | additional information | Flavobacterium sp. | physiological role of the enzyme | ? | - |
? | |
3.2.1.54 | additional information | Thermotoga maritima | physiological role of the enzyme | ? | - |
? | |
3.2.1.54 | additional information | Thermoanaerobacter ethanolicus | physiological role of the enzyme | ? | - |
? | |
3.2.1.54 | additional information | Bacteroides ovatus | physiological role of the enzyme | ? | - |
? | |
3.2.1.54 | additional information | Alicyclobacillus acidocaldarius | physiological role of the enzyme | ? | - |
? | |
3.2.1.54 | additional information | Klebsiella oxytoca | physiological role of the enzyme, starch utilization pathway | ? | - |
? | |
3.2.1.54 | additional information | Klebsiella oxytoca M5a1 | physiological role of the enzyme, starch utilization pathway | ? | - |
? | |
3.2.1.54 | additional information | Thermoanaerobacter ethanolicus 39E | physiological role of the enzyme | ? | - |
? | |
3.2.1.54 | additional information | Geobacillus stearothermophilus K-12481 | physiological role of the enzyme | ? | - |
? | |
3.2.1.54 | additional information | Xanthomonas campestris K-11151 | physiological role of the enzyme | ? | - |
? | |
3.2.1.54 | additional information | Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 | physiological role of the enzyme | ? | - |
? | |
3.2.1.135 | pullulan + H2O | Geobacillus stearothermophilus | - |
panose + ? | - |
? | |
3.2.1.135 | pullulan + H2O | Klebsiella pneumoniae | - |
panose + ? | - |
? | |
3.2.1.135 | pullulan + H2O | Paenibacillus polymyxa | - |
panose + ? | - |
? | |
3.2.1.135 | pullulan + H2O | Bacteroides thetaiotaomicron | - |
panose + ? | - |
? | |
3.2.1.135 | pullulan + H2O | Bacillus sp. KSM-1876 | - |
panose + ? | - |
? | |
3.2.1.135 | pullulan + H2O | Bacteroides thetaiotaomicron 95-1 | - |
panose + ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.54 | Alicyclobacillus acidocaldarius | - |
- |
- |
3.2.1.54 | Bacillus sp. (in: Bacteria) | - |
strain I-5 and the alkalophilic enzyme-containing strain | - |
3.2.1.54 | Bacteroides ovatus | - |
- |
- |
3.2.1.54 | Escherichia coli | - |
- |
- |
3.2.1.54 | Flavobacterium sp. | - |
- |
- |
3.2.1.54 | Geobacillus stearothermophilus | - |
starin K-12481 | - |
3.2.1.54 | Geobacillus stearothermophilus K-12481 | - |
starin K-12481 | - |
3.2.1.54 | Klebsiella oxytoca | - |
enzyme CymH | - |
3.2.1.54 | Klebsiella oxytoca M5a1 | - |
enzyme CymH | - |
3.2.1.54 | Lysinibacillus sphaericus | - |
strains E-244 and ATC7055 | - |
3.2.1.54 | Paenibacillus macerans | - |
- |
- |
3.2.1.54 | Thermoanaerobacter ethanolicus | - |
- |
- |
3.2.1.54 | Thermoanaerobacter ethanolicus 39E | - |
- |
- |
3.2.1.54 | Thermotoga maritima | - |
- |
- |
3.2.1.54 | Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 | - |
- |
- |
3.2.1.54 | Weizmannia coagulans | - |
- |
- |
3.2.1.54 | Xanthomonas campestris | - |
bifunctional enzyme with combined activities of alpha-amylase and CD-/pullulan-degrading enzyme | - |
3.2.1.54 | Xanthomonas campestris K-11151 | - |
bifunctional enzyme with combined activities of alpha-amylase and CD-/pullulan-degrading enzyme | - |
3.2.1.135 | Bacillus sp. KSM-1876 | - |
- |
- |
3.2.1.135 | Bacteroides thetaiotaomicron | - |
95-1 | - |
3.2.1.135 | Bacteroides thetaiotaomicron 95-1 | - |
95-1 | - |
3.2.1.135 | Geobacillus stearothermophilus | - |
- |
- |
3.2.1.135 | Klebsiella pneumoniae | - |
- |
- |
3.2.1.135 | Paenibacillus polymyxa | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
3.2.1.54 | cyclomaltodextrin + H2O = linear maltodextrin | also hydrolyses linear maltodextrin, model of coupled hydrolysis and transglycosylation catalyzed by cyclodextrin-degrading enzymes, catalytic mechanism of double-displacement reaction, active site cleft structure, conserved Glu332 plays an important role in the binding of oligosaccharide acceptors | Paenibacillus macerans | |
3.2.1.54 | cyclomaltodextrin + H2O = linear maltodextrin | model of coupled hydrolysis and transglycosylation catalyzed by cyclodextrin-degrading enzymes, catalytic mechanism of double-displacement reaction, active site cleft structure, catalytically important residues are Asp325, Glu354, and Asp421, conserved Glu332 plays an important role in the binding of oligosaccharide acceptors | Thermoanaerobacter ethanolicus | |
3.2.1.54 | cyclomaltodextrin + H2O = linear maltodextrin | model of coupled hydrolysis and transglycosylation catalyzed by cyclodextrin-degrading enzymes, catalytic mechanism of double-displacement reaction, active site cleft structure, conserved Glu332 plays an important role in the binding of oligosaccharide acceptors | Escherichia coli | |
3.2.1.54 | cyclomaltodextrin + H2O = linear maltodextrin | model of coupled hydrolysis and transglycosylation catalyzed by cyclodextrin-degrading enzymes, catalytic mechanism of double-displacement reaction, active site cleft structure, conserved Glu332 plays an important role in the binding of oligosaccharide acceptors | Geobacillus stearothermophilus | |
3.2.1.54 | cyclomaltodextrin + H2O = linear maltodextrin | model of coupled hydrolysis and transglycosylation catalyzed by cyclodextrin-degrading enzymes, catalytic mechanism of double-displacement reaction, active site cleft structure, conserved Glu332 plays an important role in the binding of oligosaccharide acceptors | Lysinibacillus sphaericus | |
3.2.1.54 | cyclomaltodextrin + H2O = linear maltodextrin | model of coupled hydrolysis and transglycosylation catalyzed by cyclodextrin-degrading enzymes, catalytic mechanism of double-displacement reaction, active site cleft structure, conserved Glu332 plays an important role in the binding of oligosaccharide acceptors | Weizmannia coagulans | |
3.2.1.54 | cyclomaltodextrin + H2O = linear maltodextrin | model of coupled hydrolysis and transglycosylation catalyzed by cyclodextrin-degrading enzymes, catalytic mechanism of double-displacement reaction, active site cleft structure, conserved Glu332 plays an important role in the binding of oligosaccharide acceptors | Bacillus sp. (in: Bacteria) | |
3.2.1.54 | cyclomaltodextrin + H2O = linear maltodextrin | model of coupled hydrolysis and transglycosylation catalyzed by cyclodextrin-degrading enzymes, catalytic mechanism of double-displacement reaction, active site cleft structure, conserved Glu332 plays an important role in the binding of oligosaccharide acceptors | Xanthomonas campestris | |
3.2.1.54 | cyclomaltodextrin + H2O = linear maltodextrin | model of coupled hydrolysis and transglycosylation catalyzed by cyclodextrin-degrading enzymes, catalytic mechanism of double-displacement reaction, active site cleft structure, conserved Glu332 plays an important role in the binding of oligosaccharide acceptors | Flavobacterium sp. | |
3.2.1.54 | cyclomaltodextrin + H2O = linear maltodextrin | model of coupled hydrolysis and transglycosylation catalyzed by cyclodextrin-degrading enzymes, catalytic mechanism of double-displacement reaction, active site cleft structure, conserved Glu332 plays an important role in the binding of oligosaccharide acceptors | Thermotoga maritima | |
3.2.1.54 | cyclomaltodextrin + H2O = linear maltodextrin | model of coupled hydrolysis and transglycosylation catalyzed by cyclodextrin-degrading enzymes, catalytic mechanism of double-displacement reaction, active site cleft structure, conserved Glu332 plays an important role in the binding of oligosaccharide acceptors | Klebsiella oxytoca | |
3.2.1.54 | cyclomaltodextrin + H2O = linear maltodextrin | model of coupled hydrolysis and transglycosylation catalyzed by cyclodextrin-degrading enzymes, catalytic mechanism of double-displacement reaction, active site cleft structure, conserved Glu332 plays an important role in the binding of oligosaccharide acceptors | Bacteroides ovatus | |
3.2.1.54 | cyclomaltodextrin + H2O = linear maltodextrin | model of coupled hydrolysis and transglycosylation catalyzed by cyclodextrin-degrading enzymes, catalytic mechanism of double-displacement reaction, active site cleft structure, conserved Glu332 plays an important role in the binding of oligosaccharide acceptors | Alicyclobacillus acidocaldarius |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.54 | acarbose + H2O | substrate is a pseudotetrasaccharide and potent inhibitor of glucosidases | Bacillus sp. (in: Bacteria) | ? | - |
? | |
3.2.1.54 | acarbose + H2O | substrate is a pseudotetrasaccharide and potent inhibitor of glucosidases | Thermotoga maritima | ? | - |
? | |
3.2.1.54 | acarbose + H2O | substrate is a pseudotetrasaccharide and potent inhibitor of glucosidases | Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 | ? | - |
? | |
3.2.1.54 | alpha-cyclomaltodextrin + H2O | - |
Paenibacillus macerans | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | alpha-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Escherichia coli | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | alpha-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Geobacillus stearothermophilus | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | alpha-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Lysinibacillus sphaericus | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | alpha-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Weizmannia coagulans | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | alpha-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Bacillus sp. (in: Bacteria) | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | alpha-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Xanthomonas campestris | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | alpha-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Flavobacterium sp. | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | alpha-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Thermotoga maritima | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | alpha-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Thermoanaerobacter ethanolicus | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | alpha-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Alicyclobacillus acidocaldarius | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | alpha-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Thermoanaerobacter ethanolicus 39E | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | alpha-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Geobacillus stearothermophilus K-12481 | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | alpha-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Xanthomonas campestris K-11151 | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | alpha-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | amylose + H2O | - |
Xanthomonas campestris | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | amylose + H2O | - |
Xanthomonas campestris K-11151 | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | beta-cyclomaltodextrin + H2O | - |
Paenibacillus macerans | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | beta-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Escherichia coli | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | beta-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Geobacillus stearothermophilus | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | beta-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Lysinibacillus sphaericus | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | beta-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Weizmannia coagulans | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | beta-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Bacillus sp. (in: Bacteria) | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | beta-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Xanthomonas campestris | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | beta-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Flavobacterium sp. | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | beta-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Thermotoga maritima | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | beta-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Thermoanaerobacter ethanolicus | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | beta-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Alicyclobacillus acidocaldarius | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | beta-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Thermoanaerobacter ethanolicus 39E | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | beta-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Geobacillus stearothermophilus K-12481 | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | beta-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Xanthomonas campestris K-11151 | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | beta-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Bacteroides ovatus | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Klebsiella oxytoca | maltooligosaccharide | - |
? | |
3.2.1.54 | cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Klebsiella oxytoca M5a1 | maltooligosaccharide | - |
? | |
3.2.1.54 | gamma-cyclomaltodextrin + H2O | - |
Paenibacillus macerans | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | gamma-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Escherichia coli | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | gamma-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Geobacillus stearothermophilus | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | gamma-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Lysinibacillus sphaericus | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | gamma-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Weizmannia coagulans | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | gamma-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Bacillus sp. (in: Bacteria) | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | gamma-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Xanthomonas campestris | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | gamma-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Flavobacterium sp. | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | gamma-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Thermotoga maritima | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | gamma-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Thermoanaerobacter ethanolicus | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | gamma-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Alicyclobacillus acidocaldarius | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | gamma-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Thermoanaerobacter ethanolicus 39E | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | gamma-cyclomaltodextrin + H2O | composed of 6 to 8 D-glucopyranosyl residues | Geobacillus stearothermophilus K-12481 | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | linear maltodextrins + H2O | - |
Escherichia coli | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | linear maltodextrins + H2O | - |
Geobacillus stearothermophilus | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | linear maltodextrins + H2O | - |
Weizmannia coagulans | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | linear maltodextrins + H2O | - |
Bacillus sp. (in: Bacteria) | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | linear maltodextrins + H2O | - |
Thermotoga maritima | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | linear maltodextrins + H2O | - |
Thermoanaerobacter ethanolicus | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | linear maltoheptaose + H2O | - |
Flavobacterium sp. | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | linear maltohexaose + H2O | - |
Flavobacterium sp. | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | linear maltooctaose + H2O | - |
Flavobacterium sp. | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | additional information | physiological role of the enzyme | Escherichia coli | ? | - |
? | |
3.2.1.54 | additional information | physiological role of the enzyme | Geobacillus stearothermophilus | ? | - |
? | |
3.2.1.54 | additional information | physiological role of the enzyme | Lysinibacillus sphaericus | ? | - |
? | |
3.2.1.54 | additional information | physiological role of the enzyme | Weizmannia coagulans | ? | - |
? | |
3.2.1.54 | additional information | physiological role of the enzyme | Bacillus sp. (in: Bacteria) | ? | - |
? | |
3.2.1.54 | additional information | physiological role of the enzyme | Paenibacillus macerans | ? | - |
? | |
3.2.1.54 | additional information | physiological role of the enzyme | Xanthomonas campestris | ? | - |
? | |
3.2.1.54 | additional information | physiological role of the enzyme | Flavobacterium sp. | ? | - |
? | |
3.2.1.54 | additional information | physiological role of the enzyme | Thermotoga maritima | ? | - |
? | |
3.2.1.54 | additional information | physiological role of the enzyme | Thermoanaerobacter ethanolicus | ? | - |
? | |
3.2.1.54 | additional information | physiological role of the enzyme | Bacteroides ovatus | ? | - |
? | |
3.2.1.54 | additional information | physiological role of the enzyme | Alicyclobacillus acidocaldarius | ? | - |
? | |
3.2.1.54 | additional information | physiological role of the enzyme, starch utilization pathway | Klebsiella oxytoca | ? | - |
? | |
3.2.1.54 | additional information | broad specificity, cleavage of alpha-1,4- and alpha-1,6-glycosidic bonds, the cyclomaltodextrins are the preferred substrates, substrate ring size effects the activity | Weizmannia coagulans | ? | - |
? | |
3.2.1.54 | additional information | broad specificity, cleavage of alpha-1,4- and alpha-1,6-glycosidic bonds, the cyclomaltodextrins are the preferred substrates, substrate ring size effects the activity, the enzyme also shows transglucosylation activity transferring cleavage products to the sugar moiety of various acceptor molecules resulting in a series of branched oligosaccharides | Paenibacillus macerans | ? | - |
? | |
3.2.1.54 | additional information | broad specificity, cleavage of alpha-1,4- and alpha-1,6-glycosidic bonds, the cyclomaltodextrins are the preferred substrates, substrate ring size effects the activity, the enzyme also shows transglucosylation activity transferring cleavage products to the sugar moiety of various acceptor molecules resulting in a series of branched oligosaccharides, part of the cyclomaltodextrin binding site is located between the third and fourth conserved regions | Alicyclobacillus acidocaldarius | ? | - |
? | |
3.2.1.54 | additional information | broad specificity, cleavage of alpha-1,4-glycosidic bonds, linear maltodextrins are the preferred substrates before cyclomaltodextrins, soluble starch, and pullulan, substrate ring size effects the activity | Geobacillus stearothermophilus | ? | - |
? | |
3.2.1.54 | additional information | broad specificity, cleavage of alpha-1,4-glycosidic bonds, the cyclomaltodextrins are the preferred substrates, substrate ring size effects the activity | Xanthomonas campestris | ? | - |
? | |
3.2.1.54 | additional information | broad specificity, cleavage of alpha-1,4-glycosidic bonds, the cyclomaltodextrins are the preferred substrates, substrate ring size effects the activity, substrate specificity is different between different the strains, overview, part of the cyclomaltodextrin binding site is located between the third and fourth conserved regions | Lysinibacillus sphaericus | ? | - |
? | |
3.2.1.54 | additional information | broad specificity, cleavage of alpha-1,4-glycosidic bonds, the linear maltodextrins are the preferred substrates, substrate ring size effects the activity | Thermotoga maritima | ? | - |
? | |
3.2.1.54 | additional information | broad specificity, cleavage of mainly alpha-1,4- and also alpha-1,6-glycosidic bonds in strain I-5, the cyclomaltodextrins are the preferred substrates, substrate ring size effects the activity, the enzyme also shows very high transglucosylation activity transferring cleavage products to the sugar moiety of various acceptor molecules resulting in a series of branched oligosaccharides with alpha-1,3-, alpha1,4-, and alpha1,6-glycosidic bonds in strain I-5, substrate specificities and cleavage activities are different between different Bacillus strains, overview, part of the cyclomaltodextrin binding site is located between the third and fourth conserved regions | Bacillus sp. (in: Bacteria) | ? | - |
? | |
3.2.1.54 | additional information | broad substrate specificity, cleavage of alpha-1,4- and alpha-1,6-glycosidic bonds, the cyclomaltodextrins and linear maltodextrins are the preferred substrates, substrate ring size effects the activity, the enzyme also shows very high transglucosylation activity transferring cleavage products to the sugar moiety of various acceptor molecules resulting in a series of branched oligosaccharides in alpha-1,4- and alpha1,6-glycosidic bonds | Flavobacterium sp. | ? | - |
? | |
3.2.1.54 | additional information | broad substrate specificity, cleavage of alpha-1,4-glycosidic bonds, the cyclomaltodextrins are the preferred substrates, substrate ring size effects the activity, part of the cyclomaltodextrin binding site is located between the third and fourth conserved regions | Thermoanaerobacter ethanolicus | ? | - |
? | |
3.2.1.54 | additional information | part of the cyclomaltodextrin binding site is located between the third and fourth conserved regions | Klebsiella oxytoca | ? | - |
? | |
3.2.1.54 | additional information | physiological role of the enzyme, starch utilization pathway | Klebsiella oxytoca M5a1 | ? | - |
? | |
3.2.1.54 | additional information | part of the cyclomaltodextrin binding site is located between the third and fourth conserved regions | Klebsiella oxytoca M5a1 | ? | - |
? | |
3.2.1.54 | additional information | physiological role of the enzyme | Thermoanaerobacter ethanolicus 39E | ? | - |
? | |
3.2.1.54 | additional information | broad substrate specificity, cleavage of alpha-1,4-glycosidic bonds, the cyclomaltodextrins are the preferred substrates, substrate ring size effects the activity, part of the cyclomaltodextrin binding site is located between the third and fourth conserved regions | Thermoanaerobacter ethanolicus 39E | ? | - |
? | |
3.2.1.54 | additional information | physiological role of the enzyme | Geobacillus stearothermophilus K-12481 | ? | - |
? | |
3.2.1.54 | additional information | broad specificity, cleavage of alpha-1,4-glycosidic bonds, linear maltodextrins are the preferred substrates before cyclomaltodextrins, soluble starch, and pullulan, substrate ring size effects the activity | Geobacillus stearothermophilus K-12481 | ? | - |
? | |
3.2.1.54 | additional information | physiological role of the enzyme | Xanthomonas campestris K-11151 | ? | - |
? | |
3.2.1.54 | additional information | broad specificity, cleavage of alpha-1,4-glycosidic bonds, the cyclomaltodextrins are the preferred substrates, substrate ring size effects the activity | Xanthomonas campestris K-11151 | ? | - |
? | |
3.2.1.54 | additional information | physiological role of the enzyme | Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 | ? | - |
? | |
3.2.1.54 | additional information | broad specificity, cleavage of alpha-1,4-glycosidic bonds, the linear maltodextrins are the preferred substrates, substrate ring size effects the activity | Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 | ? | - |
? | |
3.2.1.54 | pullulan + H2O | substrate is a linear polysaccharide composed of maltotriose units linked by alpha-1,6-bonds, low activity | Flavobacterium sp. | branched pullulan tetrasaccharide | main products | ? | |
3.2.1.54 | pullulan + H2O | substrate is a linear polysaccharide composed of maltotriose units linked by alpha-1,6-bonds, low activity | Geobacillus stearothermophilus | panose + maltose | main products | ? | |
3.2.1.54 | pullulan + H2O | substrate is a linear polysaccharide composed of maltotriose units linked by alpha-1,6-bonds, low activity | Lysinibacillus sphaericus | panose + maltose | main products | ? | |
3.2.1.54 | pullulan + H2O | substrate is a linear polysaccharide composed of maltotriose units linked by alpha-1,6-bonds, low activity | Bacillus sp. (in: Bacteria) | panose + maltose | main products | ? | |
3.2.1.54 | pullulan + H2O | substrate is a linear polysaccharide composed of maltotriose units linked by alpha-1,6-bonds, low activity | Paenibacillus macerans | panose + maltose | main products | ? | |
3.2.1.54 | pullulan + H2O | substrate is a linear polysaccharide composed of maltotriose units linked by alpha-1,6-bonds, low activity | Xanthomonas campestris | panose + maltose | main products | ? | |
3.2.1.54 | pullulan + H2O | substrate is a linear polysaccharide composed of maltotriose units linked by alpha-1,6-bonds, low activity | Thermoanaerobacter ethanolicus | panose + maltose | main products | ? | |
3.2.1.54 | pullulan + H2O | substrate is a linear polysaccharide composed of maltotriose units linked by alpha-1,6-bonds, low activity | Alicyclobacillus acidocaldarius | panose + maltose | main products | ? | |
3.2.1.54 | starch + H2O | no formation of cyclodextrins as products | Lysinibacillus sphaericus | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | starch + H2O | no formation of cyclodextrins as products | Weizmannia coagulans | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | starch + H2O | no formation of cyclodextrins as products | Paenibacillus macerans | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | starch + H2O | no formation of cyclodextrins as products | Thermoanaerobacter ethanolicus | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | starch + H2O | no formation of cyclodextrins as products | Alicyclobacillus acidocaldarius | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | starch + H2O | soluble starch, no formation of cyclodextrins as products | Geobacillus stearothermophilus | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | starch + H2O | soluble starch, no formation of cyclodextrins as products | Bacillus sp. (in: Bacteria) | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | starch + H2O | soluble starch, no formation of cyclodextrins as products | Xanthomonas campestris | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | starch + H2O | soluble starch, no formation of cyclodextrins as products | Flavobacterium sp. | alpha-D-glucose + maltose | - |
? | |
3.2.1.54 | starch + H2O | soluble starch, no formation of cyclodextrins as products | Thermotoga maritima | alpha-D-glucose + maltose | - |
? | |
3.2.1.135 | additional information | 4 reactions are catalyzed by the enzyme: 1. hydrolysis of alpha-1,4-glucosidic linkage, 2. hydrolysis of alpha-1,6-glucosidic linkage, 3. transglycosylation to form alpha-1,4-glucosidic linkage, 4. transglycosylation to form alpha-1,6-glucosidic linkage | Geobacillus stearothermophilus | ? | - |
? | |
3.2.1.135 | additional information | 4 reactions are catalyzed by the enzyme: 1. hydrolysis of alpha-1,4-glucosidic linkage, 2. hydrolysis of alpha-1,6-glucosidic linkage, 3. transglycosylation to form alpha-1,4-glucosidic linkage, 4. transglycosylation to form alpha-1,6-glucosidic linkage | Paenibacillus polymyxa | ? | - |
? | |
3.2.1.135 | additional information | 4 reactions are catalyzed by the enzyme: 1. hydrolysis of alpha-1,4-glucosidic linkage, 2. hydrolysis of alpha-1,6-glucosidic linkage, 3. transglycosylation to form alpha-1,4-glucosidic linkage, 4. transglycosylation to form alpha-1,6-glucosidic linkage | Bacteroides thetaiotaomicron | ? | - |
? | |
3.2.1.135 | additional information | enzyme hydrolyzes starch | Geobacillus stearothermophilus | ? | - |
? | |
3.2.1.135 | additional information | enzyme hydrolyzes starch | Paenibacillus polymyxa | ? | - |
? | |
3.2.1.135 | additional information | enzyme hydrolyzes starch | Bacteroides thetaiotaomicron | ? | - |
? | |
3.2.1.135 | additional information | 4 reactions are catalyzed by the enzyme: 1. hydrolysis of alpha-1,4-glucosidic linkage, 2. hydrolysis of alpha-1,6-glucosidic linkage, 3. transglycosylation to form alpha-1,4-glucosidic linkage, 4. transglycosylation to form alpha-1,6-glucosidic linkage | Bacteroides thetaiotaomicron 95-1 | ? | - |
? | |
3.2.1.135 | additional information | enzyme hydrolyzes starch | Bacteroides thetaiotaomicron 95-1 | ? | - |
? | |
3.2.1.135 | pullulan + H2O | - |
Geobacillus stearothermophilus | panose + ? | - |
? | |
3.2.1.135 | pullulan + H2O | - |
Klebsiella pneumoniae | panose + ? | - |
? | |
3.2.1.135 | pullulan + H2O | - |
Paenibacillus polymyxa | panose + ? | - |
? | |
3.2.1.135 | pullulan + H2O | - |
Bacteroides thetaiotaomicron | panose + ? | - |
? | |
3.2.1.135 | pullulan + H2O | - |
Bacillus sp. KSM-1876 | panose + ? | - |
? | |
3.2.1.135 | pullulan + H2O | - |
Bacteroides thetaiotaomicron 95-1 | panose + ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.2.1.54 | dimer | 2 * 67000 | Geobacillus stearothermophilus |
3.2.1.54 | dimer | 2 * 67000, alkalophilic strain | Bacillus sp. (in: Bacteria) |
3.2.1.54 | dimer | 2 * 91200-95000, strain ATCC7055, 2 * 72000, strain E-244 | Lysinibacillus sphaericus |
3.2.1.54 | monomer | 1 * 66000 | Thermoanaerobacter ethanolicus |
3.2.1.54 | monomer | 1 * 62000 | Flavobacterium sp. |
3.2.1.54 | More | multidomain (alphabeta)8 barrel structure | Geobacillus stearothermophilus |
3.2.1.54 | More | multidomain (alphabeta)8 barrel structure | Thermoanaerobacter ethanolicus |
3.2.1.54 | More | multidomain (alphabeta)8 barrel structure, no N-terminal domain, the oligomeric state of the enzyme in vitro depends on the protein concentration and the type of added salt | Thermotoga maritima |
3.2.1.54 | More | multidomain (alphabeta)8 barrel structure, scheme of dimeric enzyme in transglycosylation mode, transglycosylation is best performed in the dimeric state | Flavobacterium sp. |
3.2.1.54 | More | multidomain (alphabeta)8 barrel structure, scheme of dimeric enzyme in transglycosylation mode, transglycosylation is best performed in the dimeric state, the oligomeric state of the enzyme in vitro depends on the protein concentration and the type of added salt | Bacillus sp. (in: Bacteria) |
3.2.1.54 | More | multidomain (alphabeta)8 barrel structure, scheme of dimeric enzyme in transglycosylation mode, transglycosylation is best performed in the dimeric state, the oligomeric state of the enzyme in vitro depends on the protein concentration and the type of added salt | Paenibacillus macerans |
3.2.1.54 | More | multidomain (alphabeta)8 barrel structure, scheme of dimeric enzyme in transglycosylation mode, transglycosylation is best performed in the dimeric statethe oligomeric state of the enzyme in vitro depends on the protein concentration and the type of added salt | Alicyclobacillus acidocaldarius |
3.2.1.54 | More | multidomain (alphabeta)8 barrel structure, the oligomeric state of the enzyme in vitro depends on the protein concentration and the type of added salt | Escherichia coli |
3.2.1.54 | More | multidomain (alphabeta)8 barrel structure, the oligomeric state of the enzyme in vitro depends on the protein concentration and the type of added salt | Lysinibacillus sphaericus |
3.2.1.54 | More | multidomain (alphabeta)8 barrel structure, the oligomeric state of the enzyme in vitro depends on the protein concentration and the type of added salt | Weizmannia coagulans |
3.2.1.54 | More | multidomain (alphabeta)8 barrel structure, the oligomeric state of the enzyme in vitro depends on the protein concentration and the type of added salt | Xanthomonas campestris |
3.2.1.54 | More | multidomain (alphabeta)8 barrel structure, the oligomeric state of the enzyme in vitro depends on the protein concentration and the type of added salt | Klebsiella oxytoca |
3.2.1.54 | More | multidomain (alphabeta)8 barrel structure, the oligomeric state of the enzyme in vitro depends on the protein concentration and the type of added salt | Bacteroides ovatus |
3.2.1.54 | octamer | 8 * 65000, strain I-5, in solution | Bacillus sp. (in: Bacteria) |
3.2.1.54 | oligomer | - |
Paenibacillus macerans |
3.2.1.54 | oligomer | - |
Bacteroides ovatus |
3.2.1.54 | oligomer | - |
Alicyclobacillus acidocaldarius |
3.2.1.54 | oligomer | x * 55000 | Xanthomonas campestris |
3.2.1.54 | oligomer | x * 55000 | Thermotoga maritima |
3.2.1.54 | oligomer | x * 66000 | Escherichia coli |
3.2.1.54 | oligomer | x * 62000 | Weizmannia coagulans |
3.2.1.54 | oligomer | x * 69000 | Klebsiella oxytoca |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.2.1.54 | alpha-amylase | - |
Xanthomonas campestris |
3.2.1.54 | CD-/pullulan-hydrolyzing enzyme | - |
Escherichia coli |
3.2.1.54 | CD-/pullulan-hydrolyzing enzyme | - |
Geobacillus stearothermophilus |
3.2.1.54 | CD-/pullulan-hydrolyzing enzyme | - |
Lysinibacillus sphaericus |
3.2.1.54 | CD-/pullulan-hydrolyzing enzyme | - |
Weizmannia coagulans |
3.2.1.54 | CD-/pullulan-hydrolyzing enzyme | - |
Bacillus sp. (in: Bacteria) |
3.2.1.54 | CD-/pullulan-hydrolyzing enzyme | - |
Paenibacillus macerans |
3.2.1.54 | CD-/pullulan-hydrolyzing enzyme | - |
Xanthomonas campestris |
3.2.1.54 | CD-/pullulan-hydrolyzing enzyme | - |
Flavobacterium sp. |
3.2.1.54 | CD-/pullulan-hydrolyzing enzyme | - |
Thermotoga maritima |
3.2.1.54 | CD-/pullulan-hydrolyzing enzyme | - |
Klebsiella oxytoca |
3.2.1.54 | CD-/pullulan-hydrolyzing enzyme | - |
Thermoanaerobacter ethanolicus |
3.2.1.54 | CD-/pullulan-hydrolyzing enzyme | - |
Bacteroides ovatus |
3.2.1.54 | CD-/pullulan-hydrolyzing enzyme | - |
Alicyclobacillus acidocaldarius |
3.2.1.54 | CDase | - |
Escherichia coli |
3.2.1.54 | CDase | - |
Geobacillus stearothermophilus |
3.2.1.54 | CDase | - |
Lysinibacillus sphaericus |
3.2.1.54 | CDase | - |
Weizmannia coagulans |
3.2.1.54 | CDase | - |
Bacillus sp. (in: Bacteria) |
3.2.1.54 | CDase | - |
Paenibacillus macerans |
3.2.1.54 | CDase | - |
Xanthomonas campestris |
3.2.1.54 | CDase | - |
Flavobacterium sp. |
3.2.1.54 | CDase | - |
Thermotoga maritima |
3.2.1.54 | CDase | - |
Klebsiella oxytoca |
3.2.1.54 | CDase | - |
Thermoanaerobacter ethanolicus |
3.2.1.54 | CDase | - |
Bacteroides ovatus |
3.2.1.54 | CDase | - |
Alicyclobacillus acidocaldarius |
3.2.1.54 | cyclodextrinase | - |
Paenibacillus macerans |
3.2.1.54 | cycloheptaglucanase | - |
Paenibacillus macerans |
3.2.1.54 | cyclohexaglucanase | - |
Paenibacillus macerans |
3.2.1.54 | CymH | - |
Klebsiella oxytoca |
3.2.1.54 | More | the enzyme belongs to the alpha-amylase family of enzymes | Escherichia coli |
3.2.1.54 | More | the enzyme belongs to the alpha-amylase family of enzymes | Geobacillus stearothermophilus |
3.2.1.54 | More | the enzyme belongs to the alpha-amylase family of enzymes | Lysinibacillus sphaericus |
3.2.1.54 | More | the enzyme belongs to the alpha-amylase family of enzymes | Weizmannia coagulans |
3.2.1.54 | More | the enzyme belongs to the alpha-amylase family of enzymes | Bacillus sp. (in: Bacteria) |
3.2.1.54 | More | the enzyme belongs to the alpha-amylase family of enzymes | Paenibacillus macerans |
3.2.1.54 | More | the enzyme belongs to the alpha-amylase family of enzymes | Xanthomonas campestris |
3.2.1.54 | More | the enzyme belongs to the alpha-amylase family of enzymes | Flavobacterium sp. |
3.2.1.54 | More | the enzyme belongs to the alpha-amylase family of enzymes | Thermotoga maritima |
3.2.1.54 | More | the enzyme belongs to the alpha-amylase family of enzymes | Klebsiella oxytoca |
3.2.1.54 | More | the enzyme belongs to the alpha-amylase family of enzymes | Thermoanaerobacter ethanolicus |
3.2.1.54 | More | the enzyme belongs to the alpha-amylase family of enzymes | Bacteroides ovatus |
3.2.1.54 | More | the enzyme belongs to the alpha-amylase family of enzymes | Alicyclobacillus acidocaldarius |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.54 | 40 | - |
strain ATCC7055 | Lysinibacillus sphaericus |
3.2.1.54 | 42 | - |
- |
Bacteroides ovatus |
3.2.1.54 | 45 | - |
strain E-244 | Lysinibacillus sphaericus |
3.2.1.54 | 45 | - |
strain I-5 | Bacillus sp. (in: Bacteria) |
3.2.1.54 | 50 | - |
- |
Weizmannia coagulans |
3.2.1.54 | 50 | - |
alkalophilic strain | Bacillus sp. (in: Bacteria) |
3.2.1.54 | 55 | - |
- |
Xanthomonas campestris |
3.2.1.54 | 60 | - |
- |
Geobacillus stearothermophilus |
3.2.1.54 | 65 | - |
- |
Thermoanaerobacter ethanolicus |
3.2.1.54 | 85 | - |
recombinant enzyme, substrates cyclomaltodextrins, starch, and acarbose | Thermotoga maritima |
3.2.1.135 | 40 | - |
- |
Bacillus sp. KSM-1876 |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.2.1.54 | 4.5 | - |
- |
Xanthomonas campestris |
3.2.1.54 | 5.9 | - |
- |
Thermoanaerobacter ethanolicus |
3.2.1.54 | 6 | 7.5 | - |
Flavobacterium sp. |
3.2.1.54 | 6 | 6.5 | strain ATCC7055 | Lysinibacillus sphaericus |
3.2.1.54 | 6 | - |
alkalophilic strain | Bacillus sp. (in: Bacteria) |
3.2.1.54 | 6.2 | - |
- |
Weizmannia coagulans |
3.2.1.54 | 6.5 | - |
- |
Geobacillus stearothermophilus |
3.2.1.54 | 6.5 | - |
- |
Thermotoga maritima |
3.2.1.54 | 6.5 | - |
strain I-5 | Bacillus sp. (in: Bacteria) |
3.2.1.54 | 7 | - |
- |
Bacteroides ovatus |
3.2.1.54 | 8 | - |
strain E-244 | Lysinibacillus sphaericus |
3.2.1.135 | 7.5 | - |
- |
Bacillus sp. KSM-1876 |