1.2.1.92: 3,6-anhydro-alpha-L-galactose dehydrogenase
This is an abbreviated version!
For detailed information about 3,6-anhydro-alpha-L-galactose dehydrogenase, go to the full flat file.
Reaction
Synonyms
3,6-anhydro-L-galactose dehydrogenase, AHG dehydrogenase, AHGD, anhydrogalactose dehydrogenase, SCO3486, VejAHGD, VvAHGD
ECTree
1.2.1.92 3,6-anhydro-alpha-L-galactose dehydrogenaseAdvanced search results
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results (Engineering
Engineering on EC 1.2.1.92 - 3,6-anhydro-alpha-L-galactose dehydrogenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
E248A
E383A
the mutant shows severely reduced activity compared to the wild type enzyme
G206A
the mutant shows severely reduced activity compared to the wild type enzyme
K173A
the mutant shows severely reduced activity compared to the wild type enzyme
L249A
S176A
S227A
S233A
E383A
Vibrio variabilis JCM 19239
-
the mutant shows severely reduced activity compared to the wild type enzyme
-
K173A
Vibrio variabilis JCM 19239
-
the mutant shows severely reduced activity compared to the wild type enzyme
-
L249A
Vibrio variabilis JCM 19239
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to wild-type enzyme
-
S176A
S227A
S233A
Vibrio variabilis JCM 19239
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to wild-type enzyme
-
L249A
site-directed mutagenesis, the mutant shows slightly reduced activity compared to wild-type enzyme
L249A
the mutant shows slightly reduced activity (about 90%) compared to the wild type enzyme
S176A
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
S176A
the mutation dramatically reduces the kcat values of the enzyme against both NADP+ and 3,6-anhydro-alpha-L-galactopyranose and its affinity to NADP+, but has little impact on its affinity to 3,6-anhydro-alpha-L-galactopyranose
S227A
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
S227A
the mutation dramatically reduces the kcat values of the enzyme against both NADP+ and 3,6-anhydro-alpha-L-galactopyranose and its affinity to NADP+, but has little impact on its affinity to 3,6-anhydro-alpha-L-galactopyranose
S233A
site-directed mutagenesis, the mutant shows slightly reduced activity compared to wild-type enzyme
S233A
the mutant shows increased activity (about 110%) compared to the wild type enzyme
S176A
Vibrio variabilis JCM 19239
-
the mutation dramatically reduces the kcat values of the enzyme against both NADP+ and 3,6-anhydro-alpha-L-galactopyranose and its affinity to NADP+, but has little impact on its affinity to 3,6-anhydro-alpha-L-galactopyranose
-
S176A
Vibrio variabilis JCM 19239
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
-
S227A
Vibrio variabilis JCM 19239
-
the mutation dramatically reduces the kcat values of the enzyme against both NADP+ and 3,6-anhydro-alpha-L-galactopyranose and its affinity to NADP+, but has little impact on its affinity to 3,6-anhydro-alpha-L-galactopyranose
-
S227A
Vibrio variabilis JCM 19239
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
-
