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Literature summary for 3.2.1.135 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 3.2.1.135

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
62000
-
-
 Geobacillus stearothermophilus
66000
-
-
 Klebsiella pneumoniae
68000
-
-
 Bacillus sp. KSM-1876
70000
-
-
 Bacteroides thetaiotaomicron

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
pullulan + H2O Geobacillus stearothermophilus
-
 panose + ?
-
 ?
pullulan + H2O Klebsiella pneumoniae
-
 panose + ?
-
 ?
pullulan + H2O Paenibacillus polymyxa
-
 panose + ?
-
 ?
pullulan + H2O Bacteroides thetaiotaomicron
-
 panose + ?
-
 ?
pullulan + H2O Bacillus sp. KSM-1876
-
 panose + ?
-
 ?
pullulan + H2O Bacteroides thetaiotaomicron 95-1
-
 panose + ?
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus sp. KSM-1876
-
-
-
Bacteroides thetaiotaomicron
-
 95-1
-
Bacteroides thetaiotaomicron 95-1
-
 95-1
-
Geobacillus stearothermophilus
-
-
-
Klebsiella pneumoniae
-
-
-
Paenibacillus polymyxa
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
 ?
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 ?
-
 ?
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 ?
-
 ?
additional information enzyme hydrolyzes starch Geobacillus stearothermophilus ?
-
 ?
additional information enzyme hydrolyzes starch Paenibacillus polymyxa ?
-
 ?
additional information enzyme hydrolyzes starch Bacteroides thetaiotaomicron ?
-
 ?
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 ?
-
 ?
additional information enzyme hydrolyzes starch Bacteroides thetaiotaomicron 95-1 ?
-
 ?
pullulan + H2O
-
 Geobacillus stearothermophilus panose + ?
-
 ?
pullulan + H2O
-
 Klebsiella pneumoniae panose + ?
-
 ?
pullulan + H2O
-
 Paenibacillus polymyxa panose + ?
-
 ?
pullulan + H2O
-
 Bacteroides thetaiotaomicron panose + ?
-
 ?
pullulan + H2O
-
 Bacillus sp. KSM-1876 panose + ?
-
 ?
pullulan + H2O
-
 Bacteroides thetaiotaomicron 95-1 panose + ?
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
-
 Bacillus sp. KSM-1876

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
 Bacillus sp. KSM-1876