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Literature summary extracted from

  • Li, L.; Dong, F.; Lin, L.; He, D.; Wei, W.; Wei, D.
    N-Terminal domain truncation and domain insertion-based engineering of a novel thermostable type I pullulanase from Geobacillus thermocatenulatus (2018), J. Agric. Food Chem., 66, 10788-10798 .
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.2.1.41 dithiothreitol 10 mM, 2.4fold activation Geobacillus thermocatenulatus
3.2.1.41 Triton X-100 0.1%, 1.2fold activation. 1%, 1.3fold activation Geobacillus thermocatenulatus

Application

EC Number Application Comment Organism
3.2.1.41 food industry the enzyme can be used directly for maize starch saccharification without adjusting the pH, which reduces cost and improves efficiency Geobacillus thermocatenulatus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.41 expression in Escherichia coli BL21 (DE3) Geobacillus thermocatenulatus

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.41 additional information different N-terminally domain truncated (730T) or spliced (730T-U1 and 730T-U2) mutants are constructed. Truncating the N-terminal 85 amino acids decreases the Km value and does not change its optimum pH. Wild-type enzyme can exhibit almost entirely soluble expression, but inclusion bodies are formed after truncating 85 amino acids from its N-terminus. This indicates that the N-terminal 85 amino acids of PulGT are responsible for ensuring secretory protein folding and maintaining its stability Geobacillus thermocatenulatus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.41 alpha-cyclodextrin 1%, 99% inhibition Geobacillus thermocatenulatus
3.2.1.41 CaCl2 1 mM, 1.8fold activation. 5 mM, 66% loss of activity. 10 mM, 97% loss of activity Geobacillus thermocatenulatus
3.2.1.41 CoCl2 1 mM, 97% inhibition Geobacillus thermocatenulatus
3.2.1.41 CuCl2 1 mM, complete inhibition Geobacillus thermocatenulatus
3.2.1.41 EDTA 5 mM, complete inhibition Geobacillus thermocatenulatus
3.2.1.41 Urea 2 M, complete inhibition Geobacillus thermocatenulatus
3.2.1.41 ZnSO4 1 mM, complete inhibition Geobacillus thermocatenulatus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.41 additional information
-
 pullulan pH 6.5, 70°C Geobacillus thermocatenulatus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.41 CaCl2 1 mM, 1.8fold activation. 5 mM, 66% loss of activity. 10 mM, 97% loss of activity Geobacillus thermocatenulatus
3.2.1.41 MgCl2 1 mM, 1.5fold activation. 5 mM, 1.8fold activation. 10 mM, 1.1fold activation Geobacillus thermocatenulatus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.41 80000
-
 SDS-PAGE Geobacillus thermocatenulatus
3.2.1.41 80370
-
 calculated from sequence Geobacillus thermocatenulatus

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.41 Geobacillus thermocatenulatus A0A1V0FWX7
-
-
3.2.1.41 Geobacillus thermocatenulatus DSMZ730 A0A1V0FWX7
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.41 192.56
-
 Km-value: 22.4 mg/ml, 70 °C, pH 6.5, recombinant wild-type enzyme Geobacillus thermocatenulatus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.41 amylopectin + H2O the enzyme specifically attacks alpha-1,6-linkages of branched oligosaccharides Geobacillus thermocatenulatus ?
-
 ?
3.2.1.41 amylopectin + H2O the enzyme specifically attacks alpha-1,6-linkages of branched oligosaccharides Geobacillus thermocatenulatus DSMZ730 ?
-
 ?
3.2.1.41 additional information the enzyme has no activity toward alpha-1,4-glycosidic linkages Geobacillus thermocatenulatus ?
-
 ?
3.2.1.41 additional information the enzyme has no activity toward alpha-1,4-glycosidic linkages Geobacillus thermocatenulatus DSMZ730 ?
-
 ?
3.2.1.41 pullulan + H2O
-
 Geobacillus thermocatenulatus maltotriose + ?
-
 ?
3.2.1.41 pullulan + H2O
-
 Geobacillus thermocatenulatus DSMZ730 maltotriose + ?
-
 ?
3.2.1.41 soluble starch + H2O the enzyme specifically attacks alpha-1,6-linkages of branched oligosaccharides Geobacillus thermocatenulatus ?
-
 ?
3.2.1.41 soluble starch + H2O the enzyme specifically attacks alpha-1,6-linkages of branched oligosaccharides Geobacillus thermocatenulatus DSMZ730 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.41 pulGT
-
 Geobacillus thermocatenulatus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.41 70
-
 wild-type enzyme Geobacillus thermocatenulatus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.41 50 80 50°C: about 60% of maximal activity, 80°C: about 30% of maximal activity, wild-type enzyme Geobacillus thermocatenulatus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.41 60
-
 3 h, about 45% loss of activity. 1 h, about 20% loss of activity, wild-type enzyme Geobacillus thermocatenulatus
3.2.1.41 70
-
 3 h, about 75% loss of activity. 1 h, about 20% loss of activity, wild-type enzyme Geobacillus thermocatenulatus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.41 6.5
-
 sodium phosphate buffer, wild-type enzyme Geobacillus thermocatenulatus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.41 5 9 pH 5.0: about 80% of maximal activity, pH 9.0: about 35% of maximal activity, wild-type enzyme Geobacillus thermocatenulatus

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.41 5
-
 4°C, 60 min, 75% residual activity, wild-type enzyme Geobacillus thermocatenulatus
3.2.1.41 6
-
 4°C, 60 min, 90% residual activity, wild-type enzyme Geobacillus thermocatenulatus
3.2.1.41 7
-
 4°C, 60 min, 85% residual activity, wild-type enzyme Geobacillus thermocatenulatus
3.2.1.41 8
-
 4°C, 60 min, 70% residual activity, wild-type enzyme Geobacillus thermocatenulatus
3.2.1.41 9
-
 4°C, 60 min, 55% residual activity, wild-type enzyme Geobacillus thermocatenulatus

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.2.1.41 Geobacillus thermocatenulatus calculated from sequence
-
 5.53