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Literature summary for 3.2.1.135 extracted from

  • Hondoh, H.; Kuriki, T.; Matsuura, Y.
    Three-dimensional structure and substrate binding of Bacillus stearothermophilus neopullulanase (2003), J. Mol. Biol., 326, 177-188.
    View publication on PubMed
Search for more literature for 3.2.1.135

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structures of enzyme an dits complexes with panose, maltoteraose and isopanose are detemined Geobacillus stearothermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
pullulan + H2O Geobacillus stearothermophilus
-
 panose + ?
-
 ?
pullulan + H2O Geobacillus stearothermophilus TRS40
-
 panose + ?
-
 ?

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus P38940 TRS40
-
Geobacillus stearothermophilus TRS40 P38940 TRS40
-

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 the dual specificity of the enzyme toward alpha-1,4-, and alpha-1,6-glucosidic linkages based on structural analyses of the complexes with the enzyme and substrates is demonstrated 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 Geobacillus stearothermophilus TRS40 ?
-
 ?
additional information the dual specificity of the enzyme toward alpha-1,4-, and alpha-1,6-glucosidic linkages based on structural analyses of the complexes with the enzyme and substrates is demonstrated Geobacillus stearothermophilus TRS40 ?
-
 ?
pullulan + H2O
-
 Geobacillus stearothermophilus panose + ?
-
 ?
pullulan + H2O
-
 Geobacillus stearothermophilus TRS40 panose + ?
-
 ?

Subunits

Subunits Comment Organism
dimer the active enzyme forms a dimer in the crystalline states and in solution Geobacillus stearothermophilus