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Literature summary extracted from

  • Tao, X.; Su, L.; Wang, L.; Chen, X.; Wu, J.
    Improved production of cyclodextrin glycosyltransferase from Bacillus stearothermophilus NO2 in Escherichia coli via directed evolution (2020), Appl. Microbiol. Biotechnol., 104, 173-185 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.19 mutant enzymes I631T, I641T and K647E are expressed in Escherichia coli BL21(DE3) cells Geobacillus stearothermophilus

Protein Variants

EC Number Protein Variants Comment Organism
2.4.1.19 I631T the specific activities of the mutant is slightly higher than that of the wild type enzyme. The mutation has negligible effects on either the temperature and pH optima of the enzyme or its temperature and pH stability Geobacillus stearothermophilus
2.4.1.19 I641T the specific activities of the mutant is slightly higher than that of the wild type enzyme. The mutation has negligible effects on either the temperature and pH optima of the enzyme or its temperature and pH stability Geobacillus stearothermophilus
2.4.1.19 K647E the specific activities of the mutant is slightly higher than that of the wild type enzyme. The mutation has negligible effects on either the temperature and pH optima of the enzyme or its temperature and pH stability Geobacillus stearothermophilus

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.19 Geobacillus stearothermophilus P31797
-
-
2.4.1.19 Geobacillus stearothermophilus NO2 P31797
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.19 DEAE-Sepharose column chromatography Geobacillus stearothermophilus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.4.1.19 450
-
 wild type enzyme, at pH 6.0 and 50°C Geobacillus stearothermophilus
2.4.1.19 456
-
 mutant enzyme I641T, at pH 6.0 and 50°C Geobacillus stearothermophilus
2.4.1.19 463
-
 mutant enzyme I631T, at pH 6.0 and 50°C Geobacillus stearothermophilus
2.4.1.19 487
-
 mutant enzyme K647E, at pH 6.0 and 50°C Geobacillus stearothermophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.19 4-nitrophenyl alpha-D-maltoheptaoside-4-6-O-ethylidene + maltose
-
 Geobacillus stearothermophilus ?
-
 ?
2.4.1.19 4-nitrophenyl alpha-D-maltoheptaoside-4-6-O-ethylidene + maltose
-
 Geobacillus stearothermophilus NO2 ?
-
 ?
2.4.1.19 L-ascorbic acid + maltodextrin
-
 Geobacillus stearothermophilus L-ascorbic acid-2-O-alpha-D-glucoside + ?
-
 ?
2.4.1.19 L-ascorbic acid + maltodextrin
-
 Geobacillus stearothermophilus NO2 L-ascorbic acid-2-O-alpha-D-glucoside + ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.4.1.19 ? x * 66000, SDS-PAGE Geobacillus stearothermophilus

Synonyms

EC Number Synonyms Comment Organism
2.4.1.19 CGT
-
 Geobacillus stearothermophilus
2.4.1.19 CGTase
-
 Geobacillus stearothermophilus
2.4.1.19 cyclodextrin glucosyltransferase
-
 Geobacillus stearothermophilus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.19 70
-
-
 Geobacillus stearothermophilus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.4.1.19 30
-
 the enzyme remains stable (more than 90% activity) for 120 min at 30°C Geobacillus stearothermophilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.1.19 6
-
-
 Geobacillus stearothermophilus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.4.1.19 5 7 more than 70% activity between pH 5.0 and 7.0 Geobacillus stearothermophilus

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
2.4.1.19 5 8 the enzyme remains stable for 120 min at pH 5.0-8.0 Geobacillus stearothermophilus