Literature summary for 3.2.1.94 extracted from

Nihira, T.; Mizuno, M.; Tonozuka, T.; Sakano, Y.; Mori, T.; Okahata, Y.
Kinetic studies of site-directed mutational isomalto-dextranase-catalyzed hydrolytic reactions on a 27 MHz quartz-crystal microbalance (2005), Biochemistry, 44, 9456-9461.

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Protein Variants

Protein Variants	Comment	Organism
D198N	0.003% of wild-type activity, largely increased Kd-value	Arthrobacter globiformis
D266N	0.011% of wild-type activity, without change in substrate binding ability	Arthrobacter globiformis
D313N	0.002% of wild-type activity, largely increased Kd-value	Arthrobacter globiformis

Organism

Organism	UniProt	Comment	Textmining
Arthrobacter globiformis	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme	Arthrobacter globiformis

Reaction

Reaction	Comment	Organism	Reaction ID
isomaltotriose + H2O = alpha-isomaltose + D-glucose	D266 acts as a general acid, D198 acts as both nucleophile in the catalytic process and +binding the substrate, D313 acts in substrate binding	Arthrobacter globiformis	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
dextran + H2O	-	Arthrobacter globiformis	alpha-isomaltose + O-alpha-D-Glcp-(1-3)-O-alpha-D-Glcp-(1-6)-D-Glc + O-alpha-D-Glcp-(1-4)-O-alpha-D-Glcp-(1-6)-D-Glc + O-alpha-D-Glcp-(1-2)-O-alpha-D-Glcp-(1-6)-D-Glc	-	?

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Release 2023.1 (January 2023)