Literature summary 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

Protein Variants

EC Number	Protein Variants	Comment	Organism
2.4.1.19	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
2.4.1.19	P176G	the substrate affinity of the mutant is increased by 13% compared to the wild type	Bacillus sp. Y112
2.4.1.19	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
2.4.1.19	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
2.4.1.19	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

EC Number	Organism	UniProt	Comment	Textmining
2.4.1.19	Bacillus sp. Y112	-	-	-

Substrates and Products (Substrate)

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

Synonyms

EC Number	Synonyms	Comment	Organism
2.4.1.19	CGTase	-	Bacillus sp. Y112
2.4.1.19	cyclodextrin glucosyltransferase	-	Bacillus sp. Y112

Temperature Optimum [°C]

EC Number	Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
2.4.1.19	50	-	-	Bacillus sp. Y112

pH Optimum

EC Number	pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
2.4.1.19	10	-	-	Bacillus sp. Y112

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Release 2023.1 (January 2023)