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3,6-anhydro-alpha-L-galactopyranose + NAD(P)+ + H2O
3,6-anhydro-alpha-L-galactonate + NAD(P)H + H+
3,6-anhydro-alpha-L-galactopyranose + NAD+ + H2O
3,6-anhydro-L-galactonate + NADH + H+
3,6-anhydro-alpha-L-galactopyranose + NADP+ + H2O
3,6-anhydro-L-galactonate + NADPH + H+
D-fructose + NADP+ + H2O
?
D-galactose + NADP+ + H2O
?
D-glucose + NADP+ + H2O
?
D-glyceraldehyde + NADP+ + H2O
?
less than 20% activity compared to 3,6-anhydro-alpha-L-galactopyranose
-
-
?
D-lyxose + NADP+ + H2O
?
about 15% activity compared to 3,6-anhydro-alpha-L-galactopyranose
-
-
?
D-ribose + NADP+ + H2O
?
about 45% activity compared to 3,6-anhydro-alpha-L-galactopyranose
-
-
?
L-fucose + NADP+ + H2O
?
25% activity compared to 3,6-anhydro-alpha-L-galactopyranose
-
-
?
L-glyceraldehyde + NADP+ + H2O
?
less than 10% activity compared to 3,6-anhydro-alpha-L-galactopyranose
-
-
?
L-rhamnose + NADP+ + H2O
?
less than 1% activity compared to 3,6-anhydro-alpha-L-galactopyranose
-
-
?
additional information
?
-
3,6-anhydro-alpha-L-galactopyranose + NAD(P)+ + H2O
3,6-anhydro-alpha-L-galactonate + NAD(P)H + H+
the enzyme is involved in a degradation pathway for 3,6-anhydro-alpha-L-galactose, a major component of the polysaccharides produced by red macroalgae, such as agarose and porphyran
-
-
?
3,6-anhydro-alpha-L-galactopyranose + NAD(P)+ + H2O
3,6-anhydro-alpha-L-galactonate + NAD(P)H + H+
among the cofactors, NADP+, NAD+ and NADPH, the highest abundances of reaction products are observed when NADP+ is added to the crude enzyme reaction mixture
-
-
?
3,6-anhydro-alpha-L-galactopyranose + NAD+ + H2O
3,6-anhydro-L-galactonate + NADH + H+
-
-
-
?
3,6-anhydro-alpha-L-galactopyranose + NAD+ + H2O
3,6-anhydro-L-galactonate + NADH + H+
-
-
-
?
3,6-anhydro-alpha-L-galactopyranose + NADP+ + H2O
3,6-anhydro-L-galactonate + NADPH + H+
-
-
-
?
3,6-anhydro-alpha-L-galactopyranose + NADP+ + H2O
3,6-anhydro-L-galactonate + NADPH + H+
100% activity
-
-
?
3,6-anhydro-alpha-L-galactopyranose + NADP+ + H2O
3,6-anhydro-L-galactonate + NADPH + H+
-
-
-
?
3,6-anhydro-alpha-L-galactopyranose + NADP+ + H2O
3,6-anhydro-L-galactonate + NADPH + H+
100% activity
-
-
?
3,6-anhydro-alpha-L-galactopyranose + NADP+ + H2O
3,6-anhydro-L-galactonate + NADPH + H+
the enzyme is highly specific to 3,6-anhydro-alpha-L-galactopyranose
-
-
?
3,6-anhydro-alpha-L-galactopyranose + NADP+ + H2O
3,6-anhydro-L-galactonate + NADPH + H+
-
-
-
?
3,6-anhydro-alpha-L-galactopyranose + NADP+ + H2O
3,6-anhydro-L-galactonate + NADPH + H+
L-AHG is the preferred substrate, and NADP+ is the preferred cofactor
-
-
?
3,6-anhydro-alpha-L-galactopyranose + NADP+ + H2O
3,6-anhydro-L-galactonate + NADPH + H+
-
-
-
?
3,6-anhydro-alpha-L-galactopyranose + NADP+ + H2O
3,6-anhydro-L-galactonate + NADPH + H+
L-AHG is the preferred substrate, and NADP+ is the preferred cofactor
-
-
?
D-fructose + NADP+ + H2O
?
about 55% activity compared to 3,6-anhydro-alpha-L-galactopyranose
-
-
?
D-fructose + NADP+ + H2O
?
about 55% activity compared to 3,6-anhydro-alpha-L-galactopyranose
-
-
?
D-galactose + NADP+ + H2O
?
about 50% activity compared to 3,6-anhydro-alpha-L-galactopyranose
-
-
?
D-galactose + NADP+ + H2O
?
about 50% activity compared to 3,6-anhydro-alpha-L-galactopyranose
-
-
?
D-glucose + NADP+ + H2O
?
20% activity compared to 3,6-anhydro-alpha-L-galactopyranose
-
-
?
D-glucose + NADP+ + H2O
?
20% activity compared to 3,6-anhydro-alpha-L-galactopyranose
-
-
?
additional information
?
-
no activity with D-glucose, D-galactose, D-fructose, sucrose, maltose, arabinose, xylose, agarohexose, agarotetrose and neoagarobiose
-
-
-
additional information
?
-
-
enzyme VvAHGD shows high activity toward 3,6-anhydro-L-galactose (L-AHG). VvAHGD hardly oxidizes lactaldehyde, D-AHG, galactose, or glucose, no or poor activity. Substrate specificity and substrate binding mode in VvAHGD, overview. VvAHGD oxidizes L-AHG using both NADP+ and NAD+ as the cofactor
-
-
-
additional information
?
-
enzyme VvAHGD shows high activity toward 3,6-anhydro-L-galactose (L-AHG). VvAHGD hardly oxidizes lactaldehyde, D-AHG, galactose, or glucose, no or poor activity. Substrate specificity and substrate binding mode in VvAHGD, overview. VvAHGD oxidizes L-AHG using both NADP+ and NAD+ as the cofactor
-
-
-
additional information
?
-
-
the enzyme hardly oxidizes lactaldehyde, 3,6-anhydro-alpha-D-galactopyranose, D-galactose, or D-glucose
-
-
-
additional information
?
-
the enzyme hardly oxidizes lactaldehyde, 3,6-anhydro-alpha-D-galactopyranose, D-galactose, or D-glucose
-
-
-
additional information
?
-
-
the enzyme hardly oxidizes lactaldehyde, 3,6-anhydro-alpha-D-galactopyranose, D-galactose, or D-glucose
-
-
-
additional information
?
-
the enzyme hardly oxidizes lactaldehyde, 3,6-anhydro-alpha-D-galactopyranose, D-galactose, or D-glucose
-
-
-
additional information
?
-
-
enzyme VvAHGD shows high activity toward 3,6-anhydro-L-galactose (L-AHG). VvAHGD hardly oxidizes lactaldehyde, D-AHG, galactose, or glucose, no or poor activity. Substrate specificity and substrate binding mode in VvAHGD, overview. VvAHGD oxidizes L-AHG using both NADP+ and NAD+ as the cofactor
-
-
-
additional information
?
-
enzyme VvAHGD shows high activity toward 3,6-anhydro-L-galactose (L-AHG). VvAHGD hardly oxidizes lactaldehyde, D-AHG, galactose, or glucose, no or poor activity. Substrate specificity and substrate binding mode in VvAHGD, overview. VvAHGD oxidizes L-AHG using both NADP+ and NAD+ as the cofactor
-
-
-
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3,6-anhydro-alpha-L-galactopyranose + NAD(P)+ + H2O
3,6-anhydro-alpha-L-galactonate + NAD(P)H + H+
the enzyme is involved in a degradation pathway for 3,6-anhydro-alpha-L-galactose, a major component of the polysaccharides produced by red macroalgae, such as agarose and porphyran
-
-
?
3,6-anhydro-alpha-L-galactopyranose + NAD+ + H2O
3,6-anhydro-L-galactonate + NADH + H+
3,6-anhydro-alpha-L-galactopyranose + NADP+ + H2O
3,6-anhydro-L-galactonate + NADPH + H+
3,6-anhydro-alpha-L-galactopyranose + NAD+ + H2O
3,6-anhydro-L-galactonate + NADH + H+
-
-
-
?
3,6-anhydro-alpha-L-galactopyranose + NAD+ + H2O
3,6-anhydro-L-galactonate + NADH + H+
-
-
-
?
3,6-anhydro-alpha-L-galactopyranose + NADP+ + H2O
3,6-anhydro-L-galactonate + NADPH + H+
-
-
-
?
3,6-anhydro-alpha-L-galactopyranose + NADP+ + H2O
3,6-anhydro-L-galactonate + NADPH + H+
-
-
-
?
3,6-anhydro-alpha-L-galactopyranose + NADP+ + H2O
3,6-anhydro-L-galactonate + NADPH + H+
the enzyme is highly specific to 3,6-anhydro-alpha-L-galactopyranose
-
-
?
3,6-anhydro-alpha-L-galactopyranose + NADP+ + H2O
3,6-anhydro-L-galactonate + NADPH + H+
-
-
-
?
3,6-anhydro-alpha-L-galactopyranose + NADP+ + H2O
3,6-anhydro-L-galactonate + NADPH + H+
-
-
-
?
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0.19 - 1.45
3,6-anhydro-alpha-L-galactopyranose
0.19
3,6-anhydro-alpha-L-galactopyranose
at pH 8.0 and 20°C
1.11
3,6-anhydro-alpha-L-galactopyranose
mutant enzyme L249A, at pH 7.0 and 40°C
1.11
3,6-anhydro-alpha-L-galactopyranose
pH 7.0, 40°C, recombinant mutant L249A
1.2
3,6-anhydro-alpha-L-galactopyranose
wild type enzyme, at pH 7.0 and 40°C
1.2
3,6-anhydro-alpha-L-galactopyranose
pH 7.0, 40°C, recombinant wild-type enzyme
1.26
3,6-anhydro-alpha-L-galactopyranose
mutant enzyme S227A, at pH 7.0 and 40°C
1.26
3,6-anhydro-alpha-L-galactopyranose
pH 7.0, 40°C, recombinant mutant S227A
1.35
3,6-anhydro-alpha-L-galactopyranose
mutant enzyme S233A, at pH 7.0 and 40°C
1.35
3,6-anhydro-alpha-L-galactopyranose
pH 7.0, 40°C, recombinant mutant S233A
1.45
3,6-anhydro-alpha-L-galactopyranose
mutant enzyme S176A, at pH 7.0 and 40°C
1.45
3,6-anhydro-alpha-L-galactopyranose
pH 7.0, 40°C, recombinant mutant S176A
0.33
NADP+
wild type enzyme, at pH 7.0 and 40°C
0.33
NADP+
pH 7.0, 40°C, recombinant wild-type enzyme
0.38
NADP+
mutant enzyme S233A, at pH 7.0 and 40°C
0.38
NADP+
pH 7.0, 40°C, recombinant mutant S233A
0.41
NADP+
mutant enzyme L249A, at pH 7.0 and 40°C
0.41
NADP+
pH 7.0, 40°C, recombinant mutant L249A
0.58
NADP+
mutant enzyme S227A, at pH 7.0 and 40°C
0.58
NADP+
pH 7.0, 40°C, recombinant mutant S227A
1.11
NADP+
mutant enzyme S176A, at pH 7.0 and 40°C
1.11
NADP+
pH 7.0, 40°C, recombinant mutant S176A
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0.006 - 63.18
3,6-anhydro-alpha-L-galactopyranose
0.006
3,6-anhydro-alpha-L-galactopyranose
at pH 8.0 and 20°C
10.67
3,6-anhydro-alpha-L-galactopyranose
mutant enzyme S176A, at pH 7.0 and 40°C
10.67
3,6-anhydro-alpha-L-galactopyranose
pH 7.0, 40°C, recombinant mutant S176A
35.99
3,6-anhydro-alpha-L-galactopyranose
mutant enzyme S227A, at pH 7.0 and 40°C
35.99
3,6-anhydro-alpha-L-galactopyranose
pH 7.0, 40°C, recombinant mutant S227A
52.77
3,6-anhydro-alpha-L-galactopyranose
mutant enzyme L249A, at pH 7.0 and 40°C
52.77
3,6-anhydro-alpha-L-galactopyranose
pH 7.0, 40°C, recombinant mutant L249A
58.29
3,6-anhydro-alpha-L-galactopyranose
pH 7.0, 40°C, recombinant wild-type enzyme
58.29
3,6-anhydro-alpha-L-galactopyranose
wild type enzyme, at pH 7.0 and 40°C
63.18
3,6-anhydro-alpha-L-galactopyranose
mutant enzyme S233A, at pH 7.0 and 40°C
63.18
3,6-anhydro-alpha-L-galactopyranose
pH 7.0, 40°C, recombinant mutant S233A
19.15
NADP+
mutant enzyme S176A, at pH 7.0 and 40°C
19.15
NADP+
pH 7.0, 40°C, recombinant mutant S176A
44.55
NADP+
mutant enzyme S227A, at pH 7.0 and 40°C
44.55
NADP+
pH 7.0, 40°C, recombinant mutant S227A
63.34
NADP+
mutant enzyme L249A, at pH 7.0 and 40°C
63.34
NADP+
pH 7.0, 40°C, recombinant mutant L249A
69.09
NADP+
pH 7.0, 40°C, recombinant wild-type enzyme
69.09
NADP+
wild type enzyme, at pH 7.0 and 40°C
75.9
NADP+
mutant enzyme S233A, at pH 7.0 and 40°C
75.9
NADP+
pH 7.0, 40°C, recombinant mutant S233A
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0.032 - 48.58
3,6-anhydro-alpha-L-galactopyranose
0.032
3,6-anhydro-alpha-L-galactopyranose
at pH 8.0 and 20°C
7.36
3,6-anhydro-alpha-L-galactopyranose
mutant enzyme S176A, at pH 7.0 and 40°C
7.36
3,6-anhydro-alpha-L-galactopyranose
pH 7.0, 40°C, recombinant mutant S176A
28.56
3,6-anhydro-alpha-L-galactopyranose
mutant enzyme S227A, at pH 7.0 and 40°C
28.56
3,6-anhydro-alpha-L-galactopyranose
pH 7.0, 40°C, recombinant mutant S227A
46.8
3,6-anhydro-alpha-L-galactopyranose
mutant enzyme S233A, at pH 7.0 and 40°C
46.8
3,6-anhydro-alpha-L-galactopyranose
pH 7.0, 40°C, recombinant mutant S233A
47.54
3,6-anhydro-alpha-L-galactopyranose
mutant enzyme L249A, at pH 7.0 and 40°C
47.54
3,6-anhydro-alpha-L-galactopyranose
pH 7.0, 40°C, recombinant mutant L249A
48.575
3,6-anhydro-alpha-L-galactopyranose
pH 7.0, 40°C, recombinant wild-type enzyme
48.58
3,6-anhydro-alpha-L-galactopyranose
wild type enzyme, at pH 7.0 and 40°C
17.25
NADP+
mutant enzyme S176A, at pH 7.0 and 40°C
17.25
NADP+
pH 7.0, 40°C, recombinant mutant S176A
76.81
NADP+
mutant enzyme S227A, at pH 7.0 and 40°C
76.81
NADP+
pH 7.0, 40°C, recombinant mutant S227A
154.49
NADP+
mutant enzyme L249A, at pH 7.0 and 40°C
154.49
NADP+
pH 7.0, 40°C, recombinant mutant L249A
199.74
NADP+
mutant enzyme S233A, at pH 7.0 and 40°C
199.74
NADP+
pH 7.0, 40°C, recombinant mutant S233A
209.36
NADP+
wild type enzyme, at pH 7.0 and 40°C
209.36
NADP+
pH 7.0, 40°C, recombinant wild-type enzyme
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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
W149A
the mutant is almost inactive
E248A
-
site-directed mutagenesis, inactive mutant
-
E383A
-
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
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to wild-type enzyme
-
S233A
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to wild-type enzyme
-
E248A
inactive
E248A
site-directed mutagenesis, inactive mutant
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
-
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
-
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
-
S227A
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme
-
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Yun, E.; Lee, S.; Kim, H.; Pelton, J.; Kim, S.; Ko, H.; Choi, I.; Kim, K.
The novel catabolic pathway of 3,6-anhydro-L-galactose, the main component of red macroalgae, in a marine bacterium
Environ. Microbiol.
17
1677-1688
2015
Vibrio sp. (H2IFE7), Vibrio sp.
brenda
Pathiraja, D.; Kim, K.H.; Choi, I.G.
Rapid and robust enzymatic sensing and quantitation of 3,6-anhydro-L-galactose in a heterogeneous sugar mixture
Carbohydr. Res.
446-447
13-18
2017
Vibrio sp. EJY3 (H2IFE7)
brenda
Tsevelkhorloo, M.; Kim, S.H.; Kang, D.K.; Lee, C.R.; Hong, S.K.
NADP+-dependent dehydrogenase SCO3486 and cycloisomerase SCO3480 key enzymes for 3,6-anhydro-L-galactose catabolism in Streptomyces coelicolor A3(2)
J. Microbiol. Biotechnol.
31
756-763
2021
Streptomyces coelicolor (Q9RKF1), Streptomyces coelicolor, Streptomyces coelicolor A3(2) (Q9RKF1), Streptomyces coelicolor A3(2)
brenda
Wang, Y.; Li, P.Y.; Zhang, Y.; Cao, H.Y.; Wang, Y.J.; Li, C.Y.; Wang, P.; Su, H.N.; Chen, Y.; Chen, X.L.; Zhang, Y.Z.
3,6-Anhydro-L-galactose dehydrogenase VvAHGD is a member of a new aldehyde dehydrogenase family and catalyzes by a novel mechanism with conformational switch of two catalytic residues cysteine 282 and glutamate 248
J. Mol. Biol.
432
2186-2203
2020
Vibrio variabilis, Vibrio variabilis (A0A090SK43), Vibrio variabilis JCM 19239, Vibrio variabilis JCM 19239 (A0A090SK43)
brenda