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Literature summary extracted from

  • Ban, X.; Wu, J.; Kaustubh, B.; Lahiri, P.; Dhoble, A.S.; Gu, Z.; Li, C.; Cheng, L.; Hong, Y.; Tong, Y.; Li, Z.
    Additional salt bridges improve the thermostability of 1,4-alpha-glucan branching enzyme (2020), Food Chem., 316, 126348 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.18 expressed in Escherichia coli BL21(DE3) cells Parageobacillus thermoglucosidasius

Protein Variants

EC Number Protein Variants Comment Organism
2.4.1.18 I571D the mutant shows increased thermostability and activity nearly identical to that of the wild type enzyme Parageobacillus thermoglucosidasius
2.4.1.18 Q231K the mutant shows increased thermostability and activity nearly identical to that of the wild type enzyme Parageobacillus thermoglucosidasius
2.4.1.18 Q231R the mutant shows increased thermostability and activity nearly identical to that of the wild type enzyme Parageobacillus thermoglucosidasius
2.4.1.18 T339D the mutant shows increased thermostability and activity nearly identical to that of the wild type enzyme Parageobacillus thermoglucosidasius
2.4.1.18 T339E the mutant shows increased thermostability and activity nearly identical to that of the wild type enzyme Parageobacillus thermoglucosidasius

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.18 Parageobacillus thermoglucosidasius A0A068F9H3
-
-
2.4.1.18 Parageobacillus thermoglucosidasius STB02 A0A068F9H3
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.18 HisTrap column chromatography Parageobacillus thermoglucosidasius

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.4.1.18 0.281
-
 mutant enzyme I571D, pH and temperature not specified in the publication Parageobacillus thermoglucosidasius
2.4.1.18 0.282
-
 wild type enzyme, pH and temperature not specified in the publication Parageobacillus thermoglucosidasius
2.4.1.18 0.293
-
 mutant enzyme T339E, pH and temperature not specified in the publication Parageobacillus thermoglucosidasius
2.4.1.18 0.295
-
 mutant enzyme Q231R, pH and temperature not specified in the publication Parageobacillus thermoglucosidasius
2.4.1.18 0.296
-
 mutant enzyme T339D, pH and temperature not specified in the publication Parageobacillus thermoglucosidasius
2.4.1.18 0.298
-
 mutant enzyme Q231K, pH and temperature not specified in the publication Parageobacillus thermoglucosidasius

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.18 amylopectin
-
 Parageobacillus thermoglucosidasius amylopectin containing alpha-1,6-glucosidic linkages
-
 ?
2.4.1.18 amylopectin
-
 Parageobacillus thermoglucosidasius STB02 amylopectin containing alpha-1,6-glucosidic linkages
-
 ?
2.4.1.18 amylose
-
 Parageobacillus thermoglucosidasius amylose containing alpha-1,6-glucosidic linkages
-
 ?
2.4.1.18 amylose
-
 Parageobacillus thermoglucosidasius STB02 amylose containing alpha-1,6-glucosidic linkages
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.18 GBE
-
 Parageobacillus thermoglucosidasius

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.4.1.18 60
-
 the wild type enzyme shows a half-life of 42.1 min at 60°C and retains less than 20% activity after 2 h at 60°C. Mutant enzyme Q231R shows a half-life of 53.2 min at 60°C and retains about 31% activity after 2 h at 60°C. Mutant enzyme Q231K shows a half-life of 53.6 min at 60°C and retains about 33% activity after 2 h at 60°C. Mutant enzyme T339E shows a half-life of 49.1 min at 60°C and retains about 28% activity after 2 h at 60°C. Mutant enzyme T339D shows a half-life of 50.4 min at 60°C and retains about 23% activity after 2 h at 60°C. Mutant enzyme I571D shows a half-life of 64.2 min at 60°C and retains about 36% activity after 2 h at 60°C Parageobacillus thermoglucosidasius