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Literature summary for 3.2.1.54 extracted from

  • Park, K.H.; Kim, T.J.; Cheong, T.K.; Kim, J.W.; Oh, B.H.; Svensson, B.
    Structure, specificity and function of cyclomaltodextrinase, a multispecific enzyme of the alpha-amylase family (2000), Biochim. Biophys. Acta, 1478, 165-185.
    View publication on PubMed
Search for more literature for 3.2.1.54

Cloned(Commentary)

Cloned (Comment) Organism
-
 Bacillus sp. (in: Bacteria)
-
 Thermoanaerobacter ethanolicus
DNA sequence determination and analysis Klebsiella oxytoca
DNA sequence determination and analysis, expression in Escherichia coli Thermotoga maritima

Protein Variants

Protein Variants Comment Organism
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)
additional information single mutants of the catalytic residues Asp325, Glu354, and Asp421 are catalytically inactive Thermoanaerobacter ethanolicus
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)

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
 Klebsiella oxytoca 5737
-
periplasm
-
 Xanthomonas campestris
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
55000
-
 x * 55000 Xanthomonas campestris
55000
-
 x * 55000 Thermotoga maritima
62000
-
 x * 62000 Weizmannia coagulans
62000
-
 1 * 62000 Flavobacterium sp.
65000
-
 8 * 65000, strain I-5, in solution Bacillus sp. (in: Bacteria)
66000
-
 x * 66000 Escherichia coli
66000
-
 1 * 66000 Thermoanaerobacter ethanolicus
67000
-
 2 * 67000 Geobacillus stearothermophilus
67000
-
 2 * 67000, alkalophilic strain Bacillus sp. (in: Bacteria)
69000
-
 x * 69000 Klebsiella oxytoca
72000
-
 2 * 91200-95000, strain ATCC7055, 2 * 72000, strain E-244 Lysinibacillus sphaericus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli physiological role of the enzyme ?
-
 ?
additional information Geobacillus stearothermophilus physiological role of the enzyme ?
-
 ?
additional information Lysinibacillus sphaericus physiological role of the enzyme ?
-
 ?
additional information Weizmannia coagulans physiological role of the enzyme ?
-
 ?
additional information Bacillus sp. (in: Bacteria) physiological role of the enzyme ?
-
 ?
additional information Paenibacillus macerans physiological role of the enzyme ?
-
 ?
additional information Xanthomonas campestris physiological role of the enzyme ?
-
 ?
additional information Flavobacterium sp. physiological role of the enzyme ?
-
 ?
additional information Thermotoga maritima physiological role of the enzyme ?
-
 ?
additional information Thermoanaerobacter ethanolicus physiological role of the enzyme ?
-
 ?
additional information Bacteroides ovatus physiological role of the enzyme ?
-
 ?
additional information Alicyclobacillus acidocaldarius physiological role of the enzyme ?
-
 ?
additional information Klebsiella oxytoca physiological role of the enzyme, starch utilization pathway ?
-
 ?
additional information Klebsiella oxytoca M5a1 physiological role of the enzyme, starch utilization pathway ?
-
 ?
additional information Thermoanaerobacter ethanolicus 39E physiological role of the enzyme ?
-
 ?
additional information Geobacillus stearothermophilus K-12481 physiological role of the enzyme ?
-
 ?
additional information Xanthomonas campestris K-11151 physiological role of the enzyme ?
-
 ?
additional information Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 physiological role of the enzyme ?
-
 ?

Organism

Organism UniProt Comment Textmining
Alicyclobacillus acidocaldarius
-
-
-
Bacillus sp. (in: Bacteria)
-
 strain I-5 and the alkalophilic enzyme-containing strain
-
Bacteroides ovatus
-
-
-
Escherichia coli
-
-
-
Flavobacterium sp.
-
-
-
Geobacillus stearothermophilus
-
 starin K-12481
-
Geobacillus stearothermophilus K-12481
-
 starin K-12481
-
Klebsiella oxytoca
-
 enzyme CymH
-
Klebsiella oxytoca M5a1
-
 enzyme CymH
-
Lysinibacillus sphaericus
-
 strains E-244 and ATC7055
-
Paenibacillus macerans
-
-
-
Thermoanaerobacter ethanolicus
-
-
-
Thermoanaerobacter ethanolicus 39E
-
-
-
Thermotoga maritima
-
-
-
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
-
-
Weizmannia coagulans
-
-
-
Xanthomonas campestris
-
 bifunctional enzyme with combined activities of alpha-amylase and CD-/pullulan-degrading enzyme
-
Xanthomonas campestris K-11151
-
 bifunctional enzyme with combined activities of alpha-amylase and CD-/pullulan-degrading enzyme
-

Reaction

Reaction Comment Organism Reaction ID
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
a
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
a
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
a
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
a
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
a
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
a
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)
a
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
a
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.
a
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
a
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
a
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
a
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
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acarbose + H2O substrate is a pseudotetrasaccharide and potent inhibitor of glucosidases Bacillus sp. (in: Bacteria) ?
-
 ?
acarbose + H2O substrate is a pseudotetrasaccharide and potent inhibitor of glucosidases Thermotoga maritima ?
-
 ?
acarbose + H2O substrate is a pseudotetrasaccharide and potent inhibitor of glucosidases Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 ?
-
 ?
alpha-cyclomaltodextrin + H2O
-
 Paenibacillus macerans alpha-D-glucose + maltose
-
 ?
alpha-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Escherichia coli alpha-D-glucose + maltose
-
 ?
alpha-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Geobacillus stearothermophilus alpha-D-glucose + maltose
-
 ?
alpha-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Lysinibacillus sphaericus alpha-D-glucose + maltose
-
 ?
alpha-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Weizmannia coagulans alpha-D-glucose + maltose
-
 ?
alpha-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Bacillus sp. (in: Bacteria) alpha-D-glucose + maltose
-
 ?
alpha-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Xanthomonas campestris alpha-D-glucose + maltose
-
 ?
alpha-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Flavobacterium sp. alpha-D-glucose + maltose
-
 ?
alpha-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Thermotoga maritima alpha-D-glucose + maltose
-
 ?
alpha-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Thermoanaerobacter ethanolicus alpha-D-glucose + maltose
-
 ?
alpha-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Alicyclobacillus acidocaldarius alpha-D-glucose + maltose
-
 ?
alpha-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Thermoanaerobacter ethanolicus 39E alpha-D-glucose + maltose
-
 ?
alpha-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Geobacillus stearothermophilus K-12481 alpha-D-glucose + maltose
-
 ?
alpha-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Xanthomonas campestris K-11151 alpha-D-glucose + maltose
-
 ?
alpha-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 alpha-D-glucose + maltose
-
 ?
amylose + H2O
-
 Xanthomonas campestris alpha-D-glucose + maltose
-
 ?
amylose + H2O
-
 Xanthomonas campestris K-11151 alpha-D-glucose + maltose
-
 ?
beta-cyclomaltodextrin + H2O
-
 Paenibacillus macerans alpha-D-glucose + maltose
-
 ?
beta-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Escherichia coli alpha-D-glucose + maltose
-
 ?
beta-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Geobacillus stearothermophilus alpha-D-glucose + maltose
-
 ?
beta-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Lysinibacillus sphaericus alpha-D-glucose + maltose
-
 ?
beta-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Weizmannia coagulans alpha-D-glucose + maltose
-
 ?
beta-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Bacillus sp. (in: Bacteria) alpha-D-glucose + maltose
-
 ?
beta-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Xanthomonas campestris alpha-D-glucose + maltose
-
 ?
beta-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Flavobacterium sp. alpha-D-glucose + maltose
-
 ?
beta-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Thermotoga maritima alpha-D-glucose + maltose
-
 ?
beta-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Thermoanaerobacter ethanolicus alpha-D-glucose + maltose
-
 ?
beta-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Alicyclobacillus acidocaldarius alpha-D-glucose + maltose
-
 ?
beta-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Thermoanaerobacter ethanolicus 39E alpha-D-glucose + maltose
-
 ?
beta-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Geobacillus stearothermophilus K-12481 alpha-D-glucose + maltose
-
 ?
beta-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Xanthomonas campestris K-11151 alpha-D-glucose + maltose
-
 ?
beta-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 alpha-D-glucose + maltose
-
 ?
cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Bacteroides ovatus alpha-D-glucose + maltose
-
 ?
cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Klebsiella oxytoca maltooligosaccharide
-
 ?
cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Klebsiella oxytoca M5a1 maltooligosaccharide
-
 ?
gamma-cyclomaltodextrin + H2O
-
 Paenibacillus macerans alpha-D-glucose + maltose
-
 ?
gamma-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Escherichia coli alpha-D-glucose + maltose
-
 ?
gamma-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Geobacillus stearothermophilus alpha-D-glucose + maltose
-
 ?
gamma-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Lysinibacillus sphaericus alpha-D-glucose + maltose
-
 ?
gamma-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Weizmannia coagulans alpha-D-glucose + maltose
-
 ?
gamma-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Bacillus sp. (in: Bacteria) alpha-D-glucose + maltose
-
 ?
gamma-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Xanthomonas campestris alpha-D-glucose + maltose
-
 ?
gamma-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Flavobacterium sp. alpha-D-glucose + maltose
-
 ?
gamma-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Thermotoga maritima alpha-D-glucose + maltose
-
 ?
gamma-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Thermoanaerobacter ethanolicus alpha-D-glucose + maltose
-
 ?
gamma-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Alicyclobacillus acidocaldarius alpha-D-glucose + maltose
-
 ?
gamma-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Thermoanaerobacter ethanolicus 39E alpha-D-glucose + maltose
-
 ?
gamma-cyclomaltodextrin + H2O composed of 6 to 8 D-glucopyranosyl residues Geobacillus stearothermophilus K-12481 alpha-D-glucose + maltose
-
 ?
linear maltodextrins + H2O
-
 Escherichia coli alpha-D-glucose + maltose
-
 ?
linear maltodextrins + H2O
-
 Geobacillus stearothermophilus alpha-D-glucose + maltose
-
 ?
linear maltodextrins + H2O
-
 Weizmannia coagulans alpha-D-glucose + maltose
-
 ?
linear maltodextrins + H2O
-
 Bacillus sp. (in: Bacteria) alpha-D-glucose + maltose
-
 ?
linear maltodextrins + H2O
-
 Thermotoga maritima alpha-D-glucose + maltose
-
 ?
linear maltodextrins + H2O
-
 Thermoanaerobacter ethanolicus alpha-D-glucose + maltose
-
 ?
linear maltoheptaose + H2O
-
 Flavobacterium sp. alpha-D-glucose + maltose
-
 ?
linear maltohexaose + H2O
-
 Flavobacterium sp. alpha-D-glucose + maltose
-
 ?
linear maltooctaose + H2O
-
 Flavobacterium sp. alpha-D-glucose + maltose
-
 ?
additional information physiological role of the enzyme Escherichia coli ?
-
 ?
additional information physiological role of the enzyme Geobacillus stearothermophilus ?
-
 ?
additional information physiological role of the enzyme Lysinibacillus sphaericus ?
-
 ?
additional information physiological role of the enzyme Weizmannia coagulans ?
-
 ?
additional information physiological role of the enzyme Bacillus sp. (in: Bacteria) ?
-
 ?
additional information physiological role of the enzyme Paenibacillus macerans ?
-
 ?
additional information physiological role of the enzyme Xanthomonas campestris ?
-
 ?
additional information physiological role of the enzyme Flavobacterium sp. ?
-
 ?
additional information physiological role of the enzyme Thermotoga maritima ?
-
 ?
additional information physiological role of the enzyme Thermoanaerobacter ethanolicus ?
-
 ?
additional information physiological role of the enzyme Bacteroides ovatus ?
-
 ?
additional information physiological role of the enzyme Alicyclobacillus acidocaldarius ?
-
 ?
additional information physiological role of the enzyme, starch utilization pathway Klebsiella oxytoca ?
-
 ?
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 ?
-
 ?
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 ?
-
 ?
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 ?
-
 ?
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 ?
-
 ?
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 ?
-
 ?
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 ?
-
 ?
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 ?
-
 ?
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) ?
-
 ?
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. ?
-
 ?
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 ?
-
 ?
additional information part of the cyclomaltodextrin binding site is located between the third and fourth conserved regions Klebsiella oxytoca ?
-
 ?
additional information physiological role of the enzyme, starch utilization pathway Klebsiella oxytoca M5a1 ?
-
 ?
additional information part of the cyclomaltodextrin binding site is located between the third and fourth conserved regions Klebsiella oxytoca M5a1 ?
-
 ?
additional information physiological role of the enzyme Thermoanaerobacter ethanolicus 39E ?
-
 ?
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 ?
-
 ?
additional information physiological role of the enzyme Geobacillus stearothermophilus K-12481 ?
-
 ?
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 ?
-
 ?
additional information physiological role of the enzyme Xanthomonas campestris K-11151 ?
-
 ?
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 ?
-
 ?
additional information physiological role of the enzyme Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 ?
-
 ?
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 ?
-
 ?
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 ?
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 ?
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 ?
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 ?
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 ?
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 ?
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 ?
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 ?
starch + H2O no formation of cyclodextrins as products Lysinibacillus sphaericus alpha-D-glucose + maltose
-
 ?
starch + H2O no formation of cyclodextrins as products Weizmannia coagulans alpha-D-glucose + maltose
-
 ?
starch + H2O no formation of cyclodextrins as products Paenibacillus macerans alpha-D-glucose + maltose
-
 ?
starch + H2O no formation of cyclodextrins as products Thermoanaerobacter ethanolicus alpha-D-glucose + maltose
-
 ?
starch + H2O no formation of cyclodextrins as products Alicyclobacillus acidocaldarius alpha-D-glucose + maltose
-
 ?
starch + H2O soluble starch, no formation of cyclodextrins as products Geobacillus stearothermophilus alpha-D-glucose + maltose
-
 ?
starch + H2O soluble starch, no formation of cyclodextrins as products Bacillus sp. (in: Bacteria) alpha-D-glucose + maltose
-
 ?
starch + H2O soluble starch, no formation of cyclodextrins as products Xanthomonas campestris alpha-D-glucose + maltose
-
 ?
starch + H2O soluble starch, no formation of cyclodextrins as products Flavobacterium sp. alpha-D-glucose + maltose
-
 ?
starch + H2O soluble starch, no formation of cyclodextrins as products Thermotoga maritima alpha-D-glucose + maltose
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 67000 Geobacillus stearothermophilus
dimer 2 * 67000, alkalophilic strain Bacillus sp. (in: Bacteria)
dimer 2 * 91200-95000, strain ATCC7055, 2 * 72000, strain E-244 Lysinibacillus sphaericus
monomer 1 * 66000 Thermoanaerobacter ethanolicus
monomer 1 * 62000 Flavobacterium sp.
More multidomain (alphabeta)8 barrel structure Geobacillus stearothermophilus
More multidomain (alphabeta)8 barrel structure Thermoanaerobacter ethanolicus
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
More multidomain (alphabeta)8 barrel structure, scheme of dimeric enzyme in transglycosylation mode, transglycosylation is best performed in the dimeric state Flavobacterium sp.
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)
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
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
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
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
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
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
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
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
octamer 8 * 65000, strain I-5, in solution Bacillus sp. (in: Bacteria)
oligomer
-
 Paenibacillus macerans
oligomer
-
 Bacteroides ovatus
oligomer
-
 Alicyclobacillus acidocaldarius
oligomer x * 55000 Xanthomonas campestris
oligomer x * 55000 Thermotoga maritima
oligomer x * 66000 Escherichia coli
oligomer x * 62000 Weizmannia coagulans
oligomer x * 69000 Klebsiella oxytoca

Synonyms

Synonyms Comment Organism
alpha-amylase
-
 Xanthomonas campestris
CD-/pullulan-hydrolyzing enzyme
-
 Escherichia coli
CD-/pullulan-hydrolyzing enzyme
-
 Geobacillus stearothermophilus
CD-/pullulan-hydrolyzing enzyme
-
 Lysinibacillus sphaericus
CD-/pullulan-hydrolyzing enzyme
-
 Weizmannia coagulans
CD-/pullulan-hydrolyzing enzyme
-
 Bacillus sp. (in: Bacteria)
CD-/pullulan-hydrolyzing enzyme
-
 Paenibacillus macerans
CD-/pullulan-hydrolyzing enzyme
-
 Xanthomonas campestris
CD-/pullulan-hydrolyzing enzyme
-
 Flavobacterium sp.
CD-/pullulan-hydrolyzing enzyme
-
 Thermotoga maritima
CD-/pullulan-hydrolyzing enzyme
-
 Klebsiella oxytoca
CD-/pullulan-hydrolyzing enzyme
-
 Thermoanaerobacter ethanolicus
CD-/pullulan-hydrolyzing enzyme
-
 Bacteroides ovatus
CD-/pullulan-hydrolyzing enzyme
-
 Alicyclobacillus acidocaldarius
CDase
-
 Escherichia coli
CDase
-
 Geobacillus stearothermophilus
CDase
-
 Lysinibacillus sphaericus
CDase
-
 Weizmannia coagulans
CDase
-
 Bacillus sp. (in: Bacteria)
CDase
-
 Paenibacillus macerans
CDase
-
 Xanthomonas campestris
CDase
-
 Flavobacterium sp.
CDase
-
 Thermotoga maritima
CDase
-
 Klebsiella oxytoca
CDase
-
 Thermoanaerobacter ethanolicus
CDase
-
 Bacteroides ovatus
CDase
-
 Alicyclobacillus acidocaldarius
cyclodextrinase
-
 Paenibacillus macerans
cycloheptaglucanase
-
 Paenibacillus macerans
cyclohexaglucanase
-
 Paenibacillus macerans
CymH
-
 Klebsiella oxytoca
More the enzyme belongs to the alpha-amylase family of enzymes Escherichia coli
More the enzyme belongs to the alpha-amylase family of enzymes Geobacillus stearothermophilus
More the enzyme belongs to the alpha-amylase family of enzymes Lysinibacillus sphaericus
More the enzyme belongs to the alpha-amylase family of enzymes Weizmannia coagulans
More the enzyme belongs to the alpha-amylase family of enzymes Bacillus sp. (in: Bacteria)
More the enzyme belongs to the alpha-amylase family of enzymes Paenibacillus macerans
More the enzyme belongs to the alpha-amylase family of enzymes Xanthomonas campestris
More the enzyme belongs to the alpha-amylase family of enzymes Flavobacterium sp.
More the enzyme belongs to the alpha-amylase family of enzymes Thermotoga maritima
More the enzyme belongs to the alpha-amylase family of enzymes Klebsiella oxytoca
More the enzyme belongs to the alpha-amylase family of enzymes Thermoanaerobacter ethanolicus
More the enzyme belongs to the alpha-amylase family of enzymes Bacteroides ovatus
More the enzyme belongs to the alpha-amylase family of enzymes Alicyclobacillus acidocaldarius

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
 strain ATCC7055 Lysinibacillus sphaericus
42
-
-
 Bacteroides ovatus
45
-
 strain E-244 Lysinibacillus sphaericus
45
-
 strain I-5 Bacillus sp. (in: Bacteria)
50
-
-
 Weizmannia coagulans
50
-
 alkalophilic strain Bacillus sp. (in: Bacteria)
55
-
-
 Xanthomonas campestris
60
-
-
 Geobacillus stearothermophilus
65
-
-
 Thermoanaerobacter ethanolicus
85
-
 recombinant enzyme, substrates cyclomaltodextrins, starch, and acarbose Thermotoga maritima

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.5
-
-
 Xanthomonas campestris
5.9
-
-
 Thermoanaerobacter ethanolicus
6 7.5
-
 Flavobacterium sp.
6 6.5 strain ATCC7055 Lysinibacillus sphaericus
6
-
 alkalophilic strain Bacillus sp. (in: Bacteria)
6.2
-
-
 Weizmannia coagulans
6.5
-
-
 Geobacillus stearothermophilus
6.5
-
-
 Thermotoga maritima
6.5
-
 strain I-5 Bacillus sp. (in: Bacteria)
7
-
-
 Bacteroides ovatus
8
-
 strain E-244 Lysinibacillus sphaericus