Literature summary for 2.4.1.19 extracted from

Leemhuis, H.; Rozeboom, H.J.; Dijkstra, B.W.; Dijkhuizen, L.
Improved thermostability of Bacillus circulans cyclodextrin glycosyltransferase by the introduction of a salt bridge (2004), Proteins, 54, 128-134.

Search for more literature for 2.4.1.19

Protein Variants

Protein Variants	Comment	Organism
K192R	increase in half-life at 60°C from 9.7 min for the wild-type enzyme to 11.6 min for the mutant enzyme	Niallia circulans
N188D	increase in half-life at 60°C from 9.7 min for the wild-type enzyme to 35 min for the mutant enzyme	Niallia circulans
N188D/K192R	increase in half-life at 60°C from 9.7 min for the wild-type enzyme to 56 min for the mutant enzyme	Niallia circulans
T185S	increase in half-life at 60°C from 9.7 min for the wild-type enzyme to 14.8 min for the mutant enzyme	Niallia circulans
T186Y	decrease in half-life at 60°C from 9.7 min for the wild-type enzyme to 8 min for the mutant enzyme	Niallia circulans

Organism

Organism	UniProt	Comment	Textmining
Niallia circulans	-	-	-

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
60	-	half-life: 9.7 min for wild-type enzyme, 8 min for mutant enzyme T186Y, 35 min for mutant enzyme N188D, 11.6 min for mutant enzyme K192E and 56 min for mutant enzyme N188D/K192R	Niallia circulans

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Release 2023.1 (January 2023)