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D-fucose + NAD+
D-fucono-1,4-lactone + NADH + H+
-
-
-
-
r
D-fucose + NADP+
?
-
100% activity
-
-
?
D-fucose + NADP+
D-fucono-1,4-lactone + NADPH + H+
-
-
-
-
r
D-galactose + NAD+
D-galactono-1,4-lactone + NADH + H+
-
-
-
-
r
D-galactose + NAD+ + H2O
D-galactonate + NADH + H+
D-galactose + NADP+
D-galactono-1,4-lactone + NADPH + H+
D-galactose + NADP+ + H2O
D-galactonate + NADPH + H+
D-talose + NAD+
?
low activity
-
-
?
D-talose + NAD+
D-talono-1,4-lactone + NADH + H+
-
-
-
-
r
D-talose + NADP+
D-talono-1,4-lactone + NADPH + H+
-
-
-
-
r
L-arabinose + NAD(P)+
L-arabinono-1,4-lactone + NAD(P)H + H+
the enzyme initiates L-arabinose degradation
-
-
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH + H+
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
L-arabinose + NADP+ + H2O
L-arabinonate + NADPH + H+
additional information
?
-
D-galactose + NAD+
?
the enzyme shows high catalytic efficiency for both L-arabinose and D-galactose. The enzyme prefers NADP+ over NAD+
-
-
?
D-galactose + NAD+
?
the enzyme shows high catalytic efficiency for both L-arabinose and D-galactose. The enzyme prefers NADP+ over NAD+
-
-
?
D-galactose + NAD+ + H2O
D-galactonate + NADH + H+
the catalytic efficiency for NAD+ is 230 times lower as for NADP+ indicating NADP+ to be the physiological electron acceptor
-
-
?
D-galactose + NAD+ + H2O
D-galactonate + NADH + H+
the catalytic efficiency for NAD+ is 230 times lower as for NADP+ indicating NADP+ to be the physiological electron acceptor
-
-
?
D-galactose + NADP+
?
the enzyme shows high catalytic efficiency for both L-arabinose and D-galactose. The enzyme prefers NADP+ over NAD+
-
-
?
D-galactose + NADP+
?
the enzyme shows high catalytic efficiency for both L-arabinose and D-galactose. The enzyme prefers NADP+ over NAD+
-
-
?
D-galactose + NADP+
?
-
69% activity compared to D-fucose
-
-
?
D-galactose + NADP+
D-galactono-1,4-lactone + NADPH + H+
the enzyme has an essential function during growth on D-galactose
-
-
?
D-galactose + NADP+
D-galactono-1,4-lactone + NADPH + H+
the enzyme has an essential function during growth on D-galactose
-
-
?
D-galactose + NADP+
D-galactono-1,4-lactone + NADPH + H+
-
-
-
-
r
D-galactose + NADP+ + H2O
D-galactonate + NADPH + H+
the catalytic efficiency for NAD+ is 230 times lower as for NADP+ indicating NADP+ to be the physiological electron acceptor
-
-
?
D-galactose + NADP+ + H2O
D-galactonate + NADPH + H+
the catalytic efficiency for NAD+ is 230 times lower as for NADP+ indicating NADP+ to be the physiological electron acceptor
-
-
?
D-talose + NADP+
?
low activity
-
-
?
D-talose + NADP+
?
-
12% activity compared to D-fucose
-
-
?
D-xylose + NAD+
?
low activity
-
-
?
D-xylose + NAD+
?
low activity
-
-
?
D-xylose + NADP+
?
low activity
-
-
?
D-xylose + NADP+
?
low activity
-
-
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH + H+
-
-
-
-
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH + H+
-
-
-
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH + H+
-
-
-
-
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH + H+
the enzyme shows high catalytic efficiency for both L-arabinose and D-galactose. The enzyme prefers NADP+ over NAD+
-
-
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH + H+
preference of NADP+ over NAD+ is significantly subjected by a pair of Ser37 and Arg38
-
-
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH + H+
-
-
-
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH + H+
preference of NADP+ over NAD+ is significantly subjected by a pair of Ser37 and Arg38
-
-
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH + H+
-
-
-
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH + H+
the enzyme catalyzes the oxidation of L-arabinose with both NADP+ and NAD+ as electron acceptor, with a slight preference for NADP+. The enzyme is highly specific for L-arabinose as substrate. D-Ribose, D-glucose, D-talose, D-galactose, D-arabinose, D-xylose, D-mannose, L-mannose and D-fructose are not used at significant rates, measured with both NADP+ and NAD+, respectively, as electron acceptors
-
-
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH + H+
the enzyme catalyzes the oxidation of L-arabinose with both NADP+ and NAD+ as electron acceptor, with a slight preference for NADP+. The enzyme is highly specific for L-arabinose as substrate. D-Ribose, D-glucose, D-talose, D-galactose, D-arabinose, D-xylose, D-mannose, L-mannose and D-fructose are not used at significant rates, measured with both NADP+ and NAD+, respectively, as electron acceptors
-
-
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH + H+
-
the enzyme catalyzes the oxidation of L-arabinose with both NADP+ and NAD+ as electron acceptor, with a slight preference for NADP+. The enzyme is highly specific for L-arabinose as substrate. D-Ribose, D-glucose, D-talose, D-galactose, D-arabinose, D-xylose, D-mannose, L-mannose and D-fructose are not used at significant rates, measured with both NADP+ and NAD+, respectively, as electron acceptors
-
-
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH + H+
-
-
-
-
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
-
-
-
-
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
-
-
-
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
-
-
-
-
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
first step of L-arabinose metabolism. The enzyme is involved in the metabolism of L-arabinose but not D-galactose
-
-
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
the enzyme shows high catalytic efficiency for both L-arabinose and D-galactose. The enzyme prefers NADP+ over NAD+
-
-
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
preference of NADP+ over NAD+ is significantly subjected by a pair of Ser37 and Arg38
-
-
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
-
-
-
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
preference of NADP+ over NAD+ is significantly subjected by a pair of Ser37 and Arg38
-
-
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
-
-
-
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
the enzyme catalyzes the oxidation of L-arabinose with both NADP+ and NAD+ as electron acceptor, with a slight preference for NADP+. The enzyme is highly specific for L-arabinose as substrate. D-Ribose, D-glucose, D-talose, D-galactose, D-arabinose, D-xylose, D-mannose, L-mannose and D-fructose are not used at significant rates, measured with both NADP+ and NAD+, respectively, as electron acceptors
-
-
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
the enzyme catalyzes the oxidation of L-arabinose with both NADP+ and NAD+ as electron acceptor, with a slight preference for NADP+. The enzyme is highly specific for L-arabinose as substrate. D-Ribose, D-glucose, D-talose, D-galactose, D-arabinose, D-xylose, D-mannose, L-mannose and D-fructose are not used at significant rates, measured with both NADP+ and NAD+, respectively, as electron acceptors
-
-
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
-
the enzyme catalyzes the oxidation of L-arabinose with both NADP+ and NAD+ as electron acceptor, with a slight preference for NADP+. The enzyme is highly specific for L-arabinose as substrate. D-Ribose, D-glucose, D-talose, D-galactose, D-arabinose, D-xylose, D-mannose, L-mannose and D-fructose are not used at significant rates, measured with both NADP+ and NAD+, respectively, as electron acceptors
-
-
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
-
-
-
-
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
-
21% activity compared to D-fucose
-
-
?
L-arabinose + NADP+ + H2O
L-arabinonate + NADPH + H+
-
-
-
?
L-arabinose + NADP+ + H2O
L-arabinonate + NADPH + H+
-
-
-
?
additional information
?
-
no activity with D-arabinose, D-glucose, D-ribose, L-xylose, L-mannose, L-lyxose, and D-fructose (less than 1% of the activity with L-arabinose)
-
-
?
additional information
?
-
no activity with D-arabinose, D-glucose, D-ribose, L-xylose, L-mannose, L-lyxose, and D-fructose (less than 1% of the activity with L-arabinose)
-
-
?
additional information
?
-
low activity was observed with D-xylose (5%), D-glucose, D-fructose and D-mannose are not oxidized at significant rates
-
-
-
additional information
?
-
low activity was observed with D-xylose (5%), D-glucose, D-fructose and D-mannose are not oxidized at significant rates
-
-
-
additional information
?
-
-
some minor activity (about 1%) is measured with D-xylose and L-lyxose, while no activity is detected with D-glucose or L-rhamnose
-
-
?
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1.3
D-fucose
-
with NADP+ as cosubstrate, in 100 mM Tris-HCl, pH 9.0, 23°C
2.72
D-fucose
-
with NAD+ as cosubstrate, in 100 mM Tris-HCl, pH 9.0, 23°C
0.109
D-galactose
pH 9.0, 30°C, cofactor: NADP+, enzyme purified from Azospirillum brasilense
0.48
D-galactose
-
with NAD+ as cosubstrate, in 100 mM Tris-HCl, pH 9.0, 23°C
0.5
D-galactose
-
with NADP+ as cosubstrate, in 100 mM Tris-HCl, pH 9.0, 23°C
1.49
D-galactose
pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense
2 - 3
D-galactose
pH 8.0, temperature not specified in the publication
3.95
D-talose
pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense
5.87
D-talose
pH 9.0, 30°C, cofactor: NADP+, enzyme purified from Azospirillum brasilense
23.39
D-talose
-
with NAD+ as cosubstrate, in 100 mM Tris-HCl, pH 9.0, 23°C
57.3
D-talose
-
with NADP+ as cosubstrate, in 100 mM Tris-HCl, pH 9.0, 23°C
2 - 10
D-xylose
pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense
72
D-xylose
pH 9.0, 30°C, cofactor: NADP+, enzyme purified from Azospirillum brasilense
0.075
L-arabinose
-
pH 9,0, 25°C, cofactor: NADP+
0.14
L-arabinose
-
pH 9.0, 25°C, cofactor: NAD+
0.168
L-arabinose
30°C, pH 9.0, wild-type enzyme
0.168
L-arabinose
pH 9.0, 30°C, wild-type enzyme
0.255
L-arabinose
pH 9.0, 30°C, cofactor: NADP+, enzyme purified from Azospirillum brasilense
0.26
L-arabinose
pH 9.0, 30°C, cofactor: NADP+, recombinant wild-type enzyme
0.33
L-arabinose
-
with NADP+ as cosubstrate, in 100 mM Tris-HCl, pH 9.0, 23°C
0.588
L-arabinose
30°C, pH 9.0, mutant enzyme W152Y
0.588
L-arabinose
pH 9.0, 30°C, mutant enzyme W152Y
0.785
L-arabinose
pH 9.0, 30°C, cofactor: NAD+, recombinant wild-type enzyme
0.93
L-arabinose
-
with NAD+ as cosubstrate, in 100 mM Tris-HCl, pH 9.0, 23°C
1.02
L-arabinose
30°C, pH 9.0, mutant enzyme W152H
1.02
L-arabinose
pH 9.0, 30°C, mutant enzyme W152H
1.41
L-arabinose
pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense
8.47
L-arabinose
30°C, pH 9.0, mutant enzyme W152F
8.47
L-arabinose
pH 9.0, 30°C, mutant enzyme W152F
15.8
L-arabinose
30°C, pH 9.0, mutant enzyme N173A
15.8
L-arabinose
pH 9.0, 30°C, mutant enzyme N173A
16
L-arabinose
30°C, pH 9.0, mutant enzyme N173S
16
L-arabinose
pH 9.0, 30°C, mutant enzyme N173S
21.7
L-arabinose
30°C, pH 9.0, mutant enzyme W231A
21.7
L-arabinose
pH 9.0, 30°C, mutant enzyme W231A
22.1
L-arabinose
30°C, pH 9.0, mutant enzyme N173V
22.1
L-arabinose
pH 9.0, 30°C, mutant enzyme N173V
22.7
L-arabinose
30°C, pH 9.0, mutant enzyme N173G
22.7
L-arabinose
pH 9.0, 30°C, mutant enzyme N173G
28.9
L-arabinose
pH 9.0, 30°C, cofactor: NADP+, mutant enzyme N172A
29
L-arabinose
30°C, pH 9.0, mutant enzyme N173Q
29
L-arabinose
pH 9.0, 30°C, mutant enzyme N173Q
35
L-arabinose
pH 8.0, temperature not specified in the publication
42.5
L-arabinose
pH 9.0, 30°C, cofactor: NAD+, mutant enzyme N172A
59.6
L-arabinose
30°C, pH 9.0, mutant enzyme W152A
59.6
L-arabinose
pH 9.0, 30°C, mutant enzyme W152A
748
L-arabinose
30°C, pH 9.0, mutant enzyme H119N
748
L-arabinose
pH 9.0, 30°C, mutant enzyme H119N
0.539
NAD+
30°C, pH 9.0, mutant enzyme S37D
0.539
NAD+
pH 9.0, 30°C, mutant enzyme S37D
0.77
NAD+
-
L-arabinose as cosubstrate, in 100 mM Tris-HCl, pH 9.0, 23°C
0.879
NAD+
30°C, pH 9.0, mutant enzyme S37D/R38A
0.879
NAD+
pH 9.0, 30°C, mutant enzyme S37D/R38A
1.16
NAD+
30°C, pH 9.0, mutant enzyme R38A
1.16
NAD+
pH 9.0, 30°C, mutant enzyme R38A
3.5
NAD+
30°C, pH 9.0, wild-type enzyme
3.5
NAD+
pH 9.0, 30°C, wild-type enzyme enzyme
0.0028
NADP+
pH 9.0, 30°C
0.05
NADP+
-
L-arabinose as cosubstrate, in 100 mM Tris-HCl, pH 9.0, 23°C
0.082
NADP+
30°C, pH 9.0, wild-type enzyme
0.082
NADP+
pH 9.0, 30°C, wild-type enzyme
0.137
NADP+
30°C, pH 9.0, mutant enzyme R38A
0.137
NADP+
pH 9.0, 30°C, mutant enzyme R38A
0.18
NADP+
30°C, pH 9.0, mutant enzyme S37D/R38A
0.18
NADP+
pH 9.0, 30°C, mutant enzyme S37D/R38A
0.32
NADP+
pH 8.0, temperature not specified in the publication
0.602
NADP+
30°C, pH 9.0, mutant enzyme S37D
0.602
NADP+
pH 9.0, 30°C, mutant enzyme S37D
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
110.1
D-fucose
-
with NADP+ as cosubstrate, in 100 mM Tris-HCl, pH 9.0, 23°C
120.4
D-fucose
-
with NAD+ as cosubstrate, in 100 mM Tris-HCl, pH 9.0, 23°C
19.8
D-galactose
pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense
26
D-galactose
pH 9.0, 30°C, cofactor: NADP+, enzyme purified from Azospirillum brasilense
38.12
D-galactose
-
with NAD+ as cosubstrate, in 100 mM Tris-HCl, pH 9.0, 23°C
69.9
D-galactose
-
with NADP+ as cosubstrate, in 100 mM Tris-HCl, pH 9.0, 23°C
1.04
D-talose
pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense
9.7
D-talose
pH 9.0, 30°C, cofactor: NADP+, enzyme purified from Azospirillum brasilense
74.58
D-talose
-
with NAD+ as cosubstrate, in 100 mM Tris-HCl, pH 9.0, 23°C
99.52
D-talose
-
with NADP+ as cosubstrate, in 100 mM Tris-HCl, pH 9.0, 23°C
4
D-xylose
pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense
12
D-xylose
pH 9.0, 30°C, cofactor: NADP+, enzyme purified from Azospirillum brasilense
0.1
L-arabinose
pH 9.0, 30°C, cofactor: NAD+, mutant enzyme N172A
0.3
L-arabinose
pH 9.0, 30°C, cofactor: NADP+, mutant enzyme N172A
0.417
L-arabinose
pH 9.0, 30°C, mutant enzyme N173S
0.42
L-arabinose
30°C, pH 9.0, mutant enzyme N173S
0.47
L-arabinose
30°C, pH 9.0, mutant enzyme N173A
0.47
L-arabinose
pH 9.0, 30°C, mutant enzyme N173A
0.54
L-arabinose
30°C, pH 9.0, mutant enzyme N173Q
0.54
L-arabinose
pH 9.0, 30°C, mutant enzyme N173Q
1.175
L-arabinose
pH 9.0, 30°C, mutant enzyme N173G
1.18
L-arabinose
30°C, pH 9.0, mutant enzyme N173G
2.17
L-arabinose
pH 9.0, 30°C, mutant enzyme N173V
2.2
L-arabinose
30°C, pH 9.0, mutant enzyme N173V
6.1
L-arabinose
pH 9.0, 30°C, cofactor: NAD+, recombinant wild-type enzyme
6.4
L-arabinose
30°C, pH 9.0, mutant enzyme W152Y
6.43
L-arabinose
pH 9.0, 30°C, mutant enzyme W152Y
16.5
L-arabinose
pH 9.0, 30°C, cofactor: NADP+, recombinant wild-type enzyme
17
L-arabinose
30°C, pH 9.0, mutant enzyme H119N
17
L-arabinose
pH 9.0, 30°C, mutant enzyme H119N
19
L-arabinose
pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense
20.85
L-arabinose
-
with NADP+ as cosubstrate, in 100 mM Tris-HCl, pH 9.0, 23°C
30.5
L-arabinose
pH 9.0, 30°C, wild-type enzyme
30.5
L-arabinose
30°C, pH 9.0, wild-type enzyme
33.3
L-arabinose
pH 9.0, 30°C, cofactor: NADP+, enzyme purified from Azospirillum brasilense
54.3
L-arabinose
30°C, pH 9.0, mutant enzyme W152F
54.3
L-arabinose
pH 9.0, 30°C, mutant enzyme W152F
65.55
L-arabinose
-
with NAD+ as cosubstrate, in 100 mM Tris-HCl, pH 9.0, 23°C
68
L-arabinose
30°C, pH 9.0, mutant enzyme W152H
68
L-arabinose
pH 9.0, 30°C, mutant enzyme W152H
102.8
L-arabinose
30°C, pH 9.0, mutant enzyme W152A
102.8
L-arabinose
pH 9.0, 30°C, mutant enzyme W152A
119.8
L-arabinose
30°C, pH 9.0, mutant enzyme W231A
119.8
L-arabinose
pH 9.0, 30°C, mutant enzyme W231A
48.7
NAD+
30°C, pH 9.0, wild-type enzyme
48.7
NAD+
pH 9.0, 30°C, wild-type enzyme enzyme
67.33
NAD+
30°C, pH 9.0, mutant enzyme S37D/R38A
67.33
NAD+
pH 9.0, 30°C, mutant enzyme S37D/R38A
72.2
NAD+
30°C, pH 9.0, mutant enzyme S37D
72.2
NAD+
pH 9.0, 30°C, mutant enzyme S37D
83
NAD+
30°C, pH 9.0, mutant enzyme R38A
83
NAD+
pH 9.0, 30°C, mutant enzyme R38A
85.73
NAD+
-
L-arabinose as cosubstrate, in 100 mM Tris-HCl, pH 9.0, 23°C
0.98
NADP+
30°C, pH 9.0, mutant enzyme S37D/R38A
0.98
NADP+
pH 9.0, 30°C, mutant enzyme S37D/R38A
35.45
NADP+
-
L-arabinose as cosubstrate, in 100 mM Tris-HCl, pH 9.0, 23°C
66.5
NADP+
30°C, pH 9.0, mutant enzyme S37D
66.5
NADP+
pH 9.0, 30°C, mutant enzyme S37D
66.7
NADP+
pH 9.0, 30°C, wild-type enzyme
66.7
NADP+
30°C, pH 9.0, wild-type enzyme
175
NADP+
30°C, pH 9.0, mutant enzyme R38A
175
NADP+
pH 9.0, 30°C, mutant enzyme R38A
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
44.3
D-fucose
-
with NAD+ as cosubstrate, in 100 mM Tris-HCl, pH 9.0, 23°C
85.3
D-fucose
-
with NADP+ as cosubstrate, in 100 mM Tris-HCl, pH 9.0, 23°C
9.1
D-galactose
pH 8.0, temperature not specified in the publication
13.3
D-galactose
pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense
80.2
D-galactose
-
with NAD+ as cosubstrate, in 100 mM Tris-HCl, pH 9.0, 23°C
140
D-galactose
-
with NADP+ as cosubstrate, in 100 mM Tris-HCl, pH 9.0, 23°C
240
D-galactose
pH 9.0, 30°C, cofactor: NADP+, enzyme purified from Azospirillum brasilense
0.26
D-talose
pH 9.0, 30°C, cofactor: NADP+, enzyme purified from Azospirillum brasilense
1.6
D-talose
pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense
1.8
D-talose
-
with NADP+ as cosubstrate, in 100 mM Tris-HCl, pH 9.0, 23°C
3.3
D-talose
-
with NAD+ as cosubstrate, in 100 mM Tris-HCl, pH 9.0, 23°C
0.019
D-xylose
pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense
0.17
D-xylose
pH 9.0, 30°C, cofactor: NADP*, enzyme purified from Azospirillum brasilense
0.01
L-arabinose
pH 9.0, 30°C, cofactor: NADP+, mutant enzyme N172A
0.019
L-arabinose
30°C, pH 9.0, mutant enzyme N173Q
0.019
L-arabinose
pH 9.0, 30°C, mutant enzyme N173Q
0.023
L-arabinose
30°C, pH 9.0, mutant enzyme H119N
0.023
L-arabinose
pH 9.0, 30°C, mutant enzyme H119N
0.026
L-arabinose
30°C, pH 9.0, mutant enzyme N173S
0.026
L-arabinose
pH 9.0, 30°C, mutant enzyme N173S
0.03
L-arabinose
pH 9.0, 30°C, cofactor: NAD+, mutant enzyme N172A
0.03
L-arabinose
30°C, pH 9.0, mutant enzyme N173A
0.03
L-arabinose
pH 9.0, 30°C, mutant enzyme N173A
0.0535
L-arabinose
pH 9.0, 30°C, mutant enzyme N173G
0.054
L-arabinose
30°C, pH 9.0, mutant enzyme N173G
0.098
L-arabinose
30°C, pH 9.0, mutant enzyme N173V
0.098
L-arabinose
pH 9.0, 30°C, mutant enzyme N173V
1.7
L-arabinose
30°C, pH 9.0, mutant enzyme W152A
1.7
L-arabinose
pH 9.0, 30°C, mutant enzyme W152A
5.5
L-arabinose
30°C, pH 9.0, mutant enzyme W231A
5.52
L-arabinose
pH 9.0, 30°C, mutant enzyme W231A
6.45
L-arabinose
30°C, pH 9.0, mutant enzyme W152F
6.45
L-arabinose
pH 9.0, 30°C, mutant enzyme W152F
7
L-arabinose
pH 8.0, temperature not specified in the publication
7.78
L-arabinose
pH 9.0, 30°C, cofactor: NAD+, recombinant wild-type enzyme
13.4
L-arabinose
pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense
63.5
L-arabinose
pH 9.0, 30°C, cofactor: NADP+, recombinant wild-type enzyme
63.5
L-arabinose
-
with NADP+ as cosubstrate, in 100 mM Tris-HCl, pH 9.0, 23°C
66.5
L-arabinose
30°C, pH 9.0, mutant enzyme W152H
66.5
L-arabinose
pH 9.0, 30°C, mutant enzyme W152H
70.7
L-arabinose
-
with NAD+ as cosubstrate, in 100 mM Tris-HCl, pH 9.0, 23°C
109.8
L-arabinose
30°C, pH 9.0, mutant enzyme W152Y
109.8
L-arabinose
pH 9.0, 30°C, mutant enzyme W152Y
131
L-arabinose
pH 9.0, 30°C, cofactor: NADP+, enzyme purified from Azospirillum brasilense
183
L-arabinose
30°C, pH 9.0, wild-type enzyme
183.3
L-arabinose
pH 9.0, 30°C, wild-type enzyme
13.9
NAD+
30°C, pH 9.0, wild-type enzyme
13.9
NAD+
pH 9.0, 30°C, wild-type enzyme enzyme
71.6
NAD+
30°C, pH 9.0, mutant enzyme R38A
71.8
NAD+
pH 9.0, 30°C, mutant enzyme R38A
76.6
NAD+
30°C, pH 9.0, mutant enzyme S37D/R38A
77.5
NAD+
pH 9.0, 30°C, mutant enzyme S37D/R38A
111.8
NAD+
-
L-arabinose as cosubstrate, in 100 mM Tris-HCl, pH 9.0, 23°C
133.8
NAD+
pH 9.0, 30°C, mutant enzyme S37D
140
NAD+
30°C, pH 9.0, mutant enzyme S37D
5.3
NADP+
30°C, pH 9.0, mutant enzyme S37D/R38A
5.47
NADP+
pH 9.0, 30°C, mutant enzyme S37D/R38A
110.5
NADP+
30°C, pH 9.0, mutant enzyme S37D
110.5
NADP+
pH 9.0, 30°C, mutant enzyme S37D
741.7
NADP+
-
L-arabinose as cosubstrate, in 100 mM Tris-HCl, pH 9.0, 23°C
810
NADP+
pH 9.0, 30°C, wild-type enzyme
813.4
NADP+
30°C, pH 9.0, wild-type enzyme
1275
NADP+
pH 9.0, 30°C, mutant enzyme R38A
1277
NADP+
30°C, pH 9.0, mutant enzyme R38A
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0.042
pH 9.0, 30°C, L-arabinose + NAD+, mutant enzyme N172A
0.148
pH 9.0, 30°C, L-arabinose + NADP+, mutant enzyme N172A
1.7
pH 9.0, 30°C, D-talose + NAD+, enzyme purified from Azospirillum brasilense
12.8
pH 9.0, 30°C, D-talose + NADP+, enzyme purified from Azospirillum brasilense
14.8
pH 9.0, 30°C, D-xylose + NADP+, enzyme purified from Azospirillum brasilense
14.9
pH 9.0, 30°C, L-arabinose + NAD+, recombinant wild-type enzyme
2.6
-
pH 9.0, 25°C, L-arabinose + NADP+
23.8
pH 9.0, 30°C, D-galactose + NAD+, enzyme purified from Azospirillum brasilense
25
pH 9.0, 30°C, L-arabinose + NAD+, enzyme purified from Azospirillum brasilense
32
pH 9.0, 30°C, L-arabinose + NADP+, recombinant wild-type enzyme
323
substrate: D-galactose, pH 8.0, temperature not specified in the publication
35.6
pH 9.0, 30°C, D-galactose + NADP+, enzyme purified from Azospirillum brasilense
376
substrate: L-arabinose, pH 8.0, temperature not specified in the publication
4.1
-
pH 9.0, 25°C, L-arabinose + NAD+
44.9
pH 9.0, 30°C, L-arabinose + NADP+, enzyme purified from Azospirillum brasilense
5.3
pH 9.0, 30°C, D-xylose + NAD+, enzyme purified from Azospirillum brasilense
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D168A
mutant shows no activity under standard assay conditions
H119N/N173H
mutant enzyme is completely inactive
H119N/N173Y
mutant enzyme is completely inactive
N172A
kinetic analysis shows that the N172A mutant decreases by 4 orders of magnitude in kcat/Km values, compared with the wild-type enzyme
N173D
mutant enzyme is completely inactive
N173H
mutant enzyme is completely inactive
N173Y
mutant enzyme is completely inactive
S37D
7.3fold increase in Km-value for NADP+ and 6.5fold decrease in KM-value for NAD+
S37D/R38A
mutant enzyme shows a complete reversal of coenzyme specificity. The kcat/Km value for NADP+ decreases further by 20fold from that of the S37D mutant, and the ratio of NADP+ to NAD+ is about 0.07
W152F
-
kcat/KM for L-arabinose is 28.4fold lower than the wild-type value
-
D168A
-
mutant shows no activity under standard assay conditions
-
N172A
-
kinetic analysis shows that the N172A mutant decreases by 4 orders of magnitude in kcat/Km values, compared with the wild-type enzyme
-
H119N
kcat/KM for L-arabinose is 8088fold lower than the wild-type value
H119N
mutant emzyme is significantly active, Km value is markedly higher (4450fold) than that of wild-type
N173A
kcat/KM for L-arabinose is 6111fold lower than the wild-type value
N173A
strong decrease kcat/Km
N173G
kcat/KM for L-arabinose is 3427fold lower than the wild-type value
N173G
strong decrease kcat/Km
N173Q
kcat/KM for L-arabinose is 9735fold lower than the wild-type value
N173Q
strong decrease kcat/Km
N173S
kcat/KM for L-arabinose is 7051fold lower than the wild-type value
N173S
strong decrease kcat/Km
N173V
kcat/KM for L-arabinose is 1874fold lower than the wild-type value
N173V
strong decrease kcat/Km
W152A
kcat/KM for L-arabinose is 106fold lower than the wild-type value
W152A
the kcat/Km value by 2 orders of magnitude from wild-type enzyme
W152F
kcat/KM for L-arabinose is 28.4fold lower than the wild-type value
W152F
mutant shows an 14fold higher Km value than the W152Y mutant
W152H
kcat/KM for L-arabinose is 2.8fold lower than the wild-type value
W152H
kcat/Km value is similar to that of wild-type
W152Y
kcat/KM for L-arabinose is 1.7fold lower than the wild-type value
W152Y
kcat/Km value is similar to that of wild-type
W152Y
mutant shows an 14fold higher Km value than the W152Y mutant
W231A
kcat/KM for L-arabinose is 33.2fold lower than the wild-type value
W231A
the kcat/Km value by 2 orders of magnitude from wild-type enzyme
N173A
-
kcat/KM for L-arabinose is 6111fold lower than the wild-type value
-
N173A
-
strong decrease kcat/Km
-
W231A
-
kcat/KM for L-arabinose is 33.2fold lower than the wild-type value
-
W231A
-
the kcat/Km value by 2 orders of magnitude from wild-type enzyme
-
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Novick, N.J.; Tyler, M.E.
Partial purification and properties of an L-arabinose dehydrogenase from Azospirillium brasilense
Can. J. Microbiol.
29
242-246
1983
Azospirillum brasilense
-
brenda
Watanabe, S.; Kodaki, T.; Kodak, T.; Makino, K.
Cloning, expression, and characterization of bacterial L-arabinose 1-dehydrogenase involved in an alternative pathway of L-arabinose metabolism
J. Biol. Chem.
281
2612-2623
2006
Azospirillum brasilense (Q53TZ2), Azospirillum brasilense DSM 1690 (Q53TZ2)
brenda
Johnsen, U.; Sutter, J.M.; Zai, H.; Schnheit, P.
L-Arabinose degradation pathway in the haloarchaeon Haloferax volcanii involves a novel type of L-arabinose dehydrogenase
Extremophiles
17
897-909
2013
Haloferax volcanii (D4GP33), Haloferax volcanii, Haloferax volcanii DSM 3757 (D4GP33)
brenda
Aro-Kaerkkaeinen, N.; Toivari, M.; Maaheimo, H.; Ylilauri, M.; Pentikaeinen, O.T.; Andberg, M.; Oja, M.; Penttilae, M.; Wiebe, M.G.; Ruohonen, L.; Koivula, A.
L-arabinose/D-galactose 1-dehydrogenase of Rhizobium leguminosarum bv. trifolii characterised and applied for bioconversion of L-arabinose to L-arabonate with Saccharomyces cerevisiae
Appl. Microbiol. Biotechnol.
98
9653-9665
2014
Rhizobium leguminosarum bv. trifolii
brenda
Taestensen, J.B.; Johnsen, U.; Reinhardt, A.; Ortjohann, M.; Schoenheit, P.
D-galactose catabolism in archaea operation of the DeLey-Doudoroff pathway in Haloferax volcanii
FEMS Microbiol. Lett.
367
fnaa029
2020
Haloferax volcanii (D4GR07), Haloferax volcanii ATCC 29605 (D4GR07)
brenda
Yoshiwara, K.; Watanabe, S.; Watanabe, Y.
Crystal structure of bacterial L-arabinose 1-dehydrogenase in complex with L-arabinose and NADP
Biochem. Biophys. Res. Commun.
530
203-208
2020
Azospirillum brasilense (Q53TZ2), Azospirillum brasilense ATCC 29145 (Q53TZ2)
brenda
Watanabe, Y.; Iga, C.; Watanabe, Y.; Watanabe, S.
Structural insights into the catalytic and substrate recognition mechanisms of bacterial L-arabinose 1-dehydrogenase
FEBS Lett.
593
1257-1266
2019
Azospirillum brasilense (Q53TZ2), Azospirillum brasilense, Azospirillum brasilense ATCC29145 (Q53TZ2)
brenda