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Literature summary for 3.2.1.135 extracted from

  • Takata, H.; Kuriki, T.; Okada, S.; Takesada, Y.; Iizuka, M.; Minamiura, N.; Imanaka, T.
    Action of neopullulanase. Neopullulanase catalyzes both hydrolysis and transglycosylation at alpha-(1-4)- and alpha-(1-6)-glucosidic linkages (1992), J. Biol. Chem., 267, 18447-18452.
    View publication on PubMed
Search for more literature for 3.2.1.135

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
pullulan + H2O Bacillus subtilis
-
 panose + ?
-
 ?
pullulan + H2O Bacillus subtilis NA-1
-
 panose + ?
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
 NA-1
-
Bacillus subtilis NA-1
-
 NA-1
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
maltotriose + H2O in presence of D-glucose Bacillus subtilis maltose + D-glucose
-
 ?
maltotriose + H2O in presence of D-glucose Bacillus subtilis NA-1 maltose + D-glucose
-
 ?
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 Bacillus subtilis ?
-
 ?
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 Bacillus subtilis NA-1 ?
-
 ?
pullulan + H2O
-
 Bacillus subtilis panose + ?
-
 ?
pullulan + H2O
-
 Bacillus subtilis NA-1 panose + ?
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
 assay at Bacillus subtilis