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Literature summary for 3.2.1.135 extracted from

  • Kuriki, T.; Kaneko, H.; Yanase, M.; Takata, H.; Shimada, J.; Handa, S.; Takada, T.; Umeyama, H.; Okada, S.
    Controlling substrate preference and transglycosylation activity of neopullulanase by manipulating steric constraint and hydrophobicity in active center (1996), J. Biol. Chem., 271, 17321-17329.
    View publication on PubMed
Search for more literature for 3.2.1.135

Protein Variants

Protein Variants Comment Organism
I358V mutation decreases the preference for alpha(1-6)-branched oligosaccharides and pullulan as substrates Geobacillus stearothermophilus
I358W mutation reduces the acceptability of alpha(1-6)-branched oligo- and polysaccharides Geobacillus stearothermophilus
M375L mutation increases transglycosylation activity in comparison to wild-type enzyme Geobacillus stearothermophilus
S422V mutation increases transglycosylation activity in comparison to wild-type enzyme Geobacillus stearothermophilus
Y377D mutation decreases transglycosylation activity in comparison to wild-type enzyme Geobacillus stearothermophilus
Y377F mutation increases transglycosylation activity in comparison to wild-type enzyme Geobacillus stearothermophilus
Y377S mutation decreases transglycosylation activity in comparison to wild-type enzyme 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
-
 TRS40
-
Geobacillus stearothermophilus TRS40
-
 TRS40
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
16.6
-
 maltotriose as substrate, wild-type enzyme, comparison with mutant enzymes Geobacillus stearothermophilus
28.6
-
 pullulan as substrate, wild-type enzyme, comparison with mutant enzymes Geobacillus stearothermophilus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
maltotriose + H2O
-
 Geobacillus stearothermophilus maltose + D-glucose
-
 ?
maltotriose + H2O
-
 Geobacillus stearothermophilus TRS40 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 Geobacillus stearothermophilus ?
-
 ?
additional information enzyme hydrolyzes starch 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 enzyme hydrolyzes starch Geobacillus stearothermophilus TRS40 ?
-
 ?
pullulan + H2O
-
 Geobacillus stearothermophilus panose + ?
-
 ?
pullulan + H2O
-
 Geobacillus stearothermophilus TRS40 panose + ?
-
 ?