Literature summary for 3.2.1.73 extracted from

Mao, S.; Gao, P.; Lu, Z.; Lu, F.; Zhang, C.; Zhao, H.; Bie, X.
Engineering of a thermostable beta-1,3-1,4-glucanase from Bacillus altitudinis YC-9 to improve its catalytic efficiency (2016), J. Sci. Food Agric., 96, 109-115.

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Protein Variants

Protein Variants	Comment	Organism
K142N/Q203L/N214D	mutant isolated by error-prone PCR, 48.6 increase in catalytic activity compared to wild-type. The optimal pH of the mutated enzyme is 5.0, which is lower than the parent enzyme, but thermal stability is almost the same	Bacillus altitudinis

Organism

Organism	UniProt	Comment	Textmining
Bacillus altitudinis	K7XFI7	-	-
Bacillus altitudinis YC-9	K7XFI7	-	-

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
5	-	mutant K142N/Q203L/N214D	Bacillus altitudinis

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Release 2023.1 (January 2023)