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Literature summary for 2.4.1.19 extracted from

  • Li, X.; Sun, J.; Wang, W.; Guo, J.; Song, K.; Hao, J.
    Site-saturation mutagenesis of proline 176 in cyclodextrin glucosyltransferase from Bacillus sp. Y112 effects product specificity and enzymatic properties (2020), Process Biochem., 94, 180-189 .
No PubMed abstract available
Search for more literature for 2.4.1.19

Protein Variants

Protein Variants Comment Organism
P176G compared to the wild type, the mutant shows 10.4% improvement in conversion from starch to cyclodextrins, whose beta-cyclodextrin yield increases by 6% and alpha-cyclodextrin yield decreases by 8% Bacillus sp. Y112
P176G the substrate affinity of the mutant is increased by 13% compared to the wild type Bacillus sp. Y112
P176I the mutant is increased by 9.4 % on cyclodextrin production, indicating replacement of hydrophobic amino acids significantly improve in cyclization activity Bacillus sp. Y112
P176K the substrate affinity of the mutant is increased by 14% and the catalytic efficiency is increased by 14% compared to the wild type Bacillus sp. Y112
P176L the mutant is increased by 7.9 % on cyclodextrin production, indicating replacement of hydrophobic amino acids significantly improve in cyclization activity Bacillus sp. Y112

Organism

Organism UniProt Comment Textmining
Bacillus sp. Y112
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
starch + glycosyl acceptor
-
 Bacillus sp. Y112 alpha-cyclodextrin + beta-cyclodextrin
-
 ?

Synonyms

Synonyms Comment Organism
CGTase
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 Bacillus sp. Y112
cyclodextrin glucosyltransferase
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 Bacillus sp. Y112

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
 Bacillus sp. Y112

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
10
-
-
 Bacillus sp. Y112