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3.2.1.70: glucan 1,6-alpha-glucosidase

This is an abbreviated version!
For detailed information about glucan 1,6-alpha-glucosidase, go to the full flat file.

Word Map on EC 3.2.1.70

Reaction

isomaltoheptaose
+
H2O
=
isomaltohexaose
 +
D-glucose

Synonyms

1,6-alpha-D-glucan glucohydrolase, alpha-1,6-glucosidase, dextran glucosidase, DGase, exo-1,6-alpha-glucosidase, exodextranase, GH13_31 glucan 1,6-alpha-glucosidase, glucodextranase, glucose-forming exodextranase, LaGH13_31, MalL, oligo-alpha-1,6-glucosidase, SMDG, TreX

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.70 glucan 1,6-alpha-glucosidase

Engineering

Engineering on EC 3.2.1.70 - glucan 1,6-alpha-glucosidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E458Q
-
mutant enzyme shows 0.0005% of the wild-type activity
E656Q
-
mutant enzyme shows 0.0003% of the wild-type activity
E458Q
-
mutant enzyme shows 0.0005% of the wild-type activity
-
E656Q
-
mutant enzyme shows 0.0003% of the wild-type activity
-
D318A
-
shows an activity level identical to that of the wild-type
E94A
-
shows a relatively minor change in the alpha-1,6-glucosidase activity, but a sharply increased alpha-1,4-transferase activity compared with the wild-type
C129S/C532S
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme, the mutant predominantly catalyzes hydrolysis
D194A/C129S/C532S
site-directed mutagenesis
D194C/C129S/C532S
site-directed mutagenesis, the mutant shows highly reduced activity compared with the wild-type enzyme and mutant C129S/C532S, oxidation with KI activates the mutant by 330fold which is 0.27% activity of the activity of mutant C129S/C532S, the oxidized mutant Ox-D194C-2CS catalyzes both hydrolysis and transglucosylation
E236Q
catalysis is compromised in complex with isomaltotriose
W238A
mutant shows lower preference for kojibiose, nigerose, and sucrose and higher preference for maltooligosaccharides, trehalose, and p-nitrophenyl alpha-D-glucoside. Altough trehalose is not a substrate for the wild-type, the mutant enzyme hydrolyzes trehalose
W238N
mutant shows lower preference for kojibiose, nigerose, and sucrose and higher preference for maltooligosaccharides, trehalose, and p-nitrophenyl alpha-D-glucoside. Altough trehalose is not a substrate for the wild-type, the mutant enzyme hydrolyzes trehalose
W238P
mutant shows lower preference for kojibiose, nigerose, and sucrose and higher preference for maltooligosaccharides, trehalose, and p-nitrophenyl alpha-D-glucoside. Altough trehalose is not a substrate for the wild-type, the mutant enzyme hydrolyzes trehalose
C129S/C532S
-
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme, the mutant predominantly catalyzes hydrolysis
-
D194A/C129S/C532S
-
site-directed mutagenesis
-
D194C/C129S/C532S
-
site-directed mutagenesis, the mutant shows highly reduced activity compared with the wild-type enzyme and mutant C129S/C532S, oxidation with KI activates the mutant by 330fold which is 0.27% activity of the activity of mutant C129S/C532S, the oxidized mutant Ox-D194C-2CS catalyzes both hydrolysis and transglucosylation
-
F262A
the mutant enzyme has a stronger preference for transglucosylation than that of the wild type enzyme
F262W
the mutant enzyme has a weaker preference for transglucosylation than that of the wild type enzyme
F262A
-
the mutant enzyme has a stronger preference for transglucosylation than that of the wild type enzyme
-
F262W
-
the mutant enzyme has a weaker preference for transglucosylation than that of the wild type enzyme
-
additional information