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Information on EC 1.1.1.376 - L-arabinose 1-dehydrogenase [NAD(P)+]
for references in articles please use BRENDA:EC1.1.1.376
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.376 L-arabinose 1-dehydrogenase [NAD(P)+]
IUBMB Comments
The enzymes from the bacterium Azospirillum brasilense and the archaeon Haloferax volcanii are part of the L-arabinose degradation pathway and prefer NADP+ over NAD+. In vitro the enzyme from Azospirillum brasilense shows also high catalytic efficiency with D-galactose. The enzyme is specific for α-L-arabinopyranose [3,4].
The expected taxonomic range for this enzyme is: Bacteria, Archaea
showSynonyms
hvo_b0032, nad(p)-dependent l-arabinose 1-dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AraDH
HVO_A0330
HVO_B0032
L-arabinose 1-dehydrogenase
L-AraDH
NAD(P)-dependent L-arabinose 1-dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
alpha-L-arabinopyranose + NAD(P)+ = L-arabinono-1,4-lactone + NAD(P)H + H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
L-arabinose degradation III, L-arabinose degradation IV, L-arabinose degradation V
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SYSTEMATIC NAME
IUBMB Comments
alpha-L-arabinopyranose:NAD(P)+ 1-oxidoreductase
The enzymes from the bacterium Azospirillum brasilense and the archaeon Haloferax volcanii are part of the L-arabinose degradation pathway and prefer NADP+ over NAD+. In vitro the enzyme from Azospirillum brasilense shows also high catalytic efficiency with D-galactose. The enzyme is specific for alpha-L-arabinopyranose [3,4].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-fucose + NAD+
D-fucono-1,4-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-fucose + NADP+
?
-
Substrates: 100% activity
Products: -
Products: -
?
D-fucose + NADP+
D-fucono-1,4-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
D-galactose + NAD+
D-galactono-1,4-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-talose + NAD+
D-talono-1,4-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-talose + NADP+
D-talono-1,4-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
L-arabinose + NAD(P)+
L-arabinono-1,4-lactone + NAD(P)H + H+
Substrates: the enzyme initiates L-arabinose degradation
Products: -
Products: -
?
D-galactose + NAD+
?
Substrates: the enzyme shows high catalytic efficiency for both L-arabinose and D-galactose. The enzyme prefers NADP+ over NAD+
Products: -
Products: -
?
D-galactose + NAD+
?
Substrates: the enzyme shows high catalytic efficiency for both L-arabinose and D-galactose. The enzyme prefers NADP+ over NAD+
Products: -
Products: -
?
D-galactose + NAD+ + H2O
D-galactonate + NADH + H+
Substrates: the catalytic efficiency for NAD+ is 230 times lower as for NADP+ indicating NADP+ to be the physiological electron acceptor
Products: -
Products: -
?
D-galactose + NAD+ + H2O
D-galactonate + NADH + H+
Substrates: the catalytic efficiency for NAD+ is 230 times lower as for NADP+ indicating NADP+ to be the physiological electron acceptor
Products: -
Products: -
?
D-galactose + NADP+
?
Substrates: the enzyme shows high catalytic efficiency for both L-arabinose and D-galactose. The enzyme prefers NADP+ over NAD+
Products: -
Products: -
?
D-galactose + NADP+
?
Substrates: the enzyme shows high catalytic efficiency for both L-arabinose and D-galactose. The enzyme prefers NADP+ over NAD+
Products: -
Products: -
?
D-galactose + NADP+
?
-
Substrates: 69% activity compared to D-fucose
Products: -
Products: -
?
D-galactose + NADP+
D-galactono-1,4-lactone + NADPH + H+
Substrates: the enzyme has an essential function during growth on D-galactose
Products: -
Products: -
?
D-galactose + NADP+
D-galactono-1,4-lactone + NADPH + H+
Substrates: the enzyme has an essential function during growth on D-galactose
Products: -
Products: -
?
D-galactose + NADP+
D-galactono-1,4-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
D-galactose + NADP+ + H2O
D-galactonate + NADPH + H+
Substrates: the catalytic efficiency for NAD+ is 230 times lower as for NADP+ indicating NADP+ to be the physiological electron acceptor
Products: -
Products: -
?
D-galactose + NADP+ + H2O
D-galactonate + NADPH + H+
Substrates: the catalytic efficiency for NAD+ is 230 times lower as for NADP+ indicating NADP+ to be the physiological electron acceptor
Products: -
Products: -
?
D-talose + NADP+
?
-
Substrates: 12% activity compared to D-fucose
Products: -
Products: -
?
D-xylose + NAD+
?
Substrates: low activity
Products: -
Products: -
?
D-xylose + NADP+
?
Substrates: low activity
Products: -
Products: -
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH + H+
Substrates: -
Products: -
Products: -
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH + H+
Substrates: the enzyme shows high catalytic efficiency for both L-arabinose and D-galactose. The enzyme prefers NADP+ over NAD+
Products: -
Products: -
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH + H+
Substrates: preference of NADP+ over NAD+ is significantly subjected by a pair of Ser37 and Arg38
Products: -
Products: -
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH + H+
Substrates: -
Products: -
Products: -
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH + H+
Substrates: preference of NADP+ over NAD+ is significantly subjected by a pair of Ser37 and Arg38
Products: -
Products: -
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH + H+
Substrates: -
Products: -
Products: -
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH + H+
Substrates: 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
Products: -
Products: -
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH + H+
Substrates: 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
Products: -
Products: -
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH + H+
-
Substrates: 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
Products: -
Products: -
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
Substrates: -
Products: -
Products: -
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
Substrates: first step of L-arabinose metabolism. The enzyme is involved in the metabolism of L-arabinose but not D-galactose
Products: -
Products: -
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
Substrates: the enzyme shows high catalytic efficiency for both L-arabinose and D-galactose. The enzyme prefers NADP+ over NAD+
Products: -
Products: -
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
Substrates: preference of NADP+ over NAD+ is significantly subjected by a pair of Ser37 and Arg38
Products: -
Products: -
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
Substrates: -
Products: -
Products: -
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
Substrates: preference of NADP+ over NAD+ is significantly subjected by a pair of Ser37 and Arg38
Products: -
Products: -
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
Substrates: -
Products: -
Products: -
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
Substrates: 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
Products: -
Products: -
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
Substrates: 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
Products: -
Products: -
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
-
Substrates: 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
Products: -
Products: -
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
-
Substrates: 21% activity compared to D-fucose
Products: -
Products: -
?
L-arabinose + NADP+ + H2O
L-arabinonate + NADPH + H+
Substrates: -
Products: -
Products: -
?
L-arabinose + NADP+ + H2O
L-arabinonate + NADPH + H+
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: 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)
Products: -
Products: -
?
additional information
?
-
Substrates: 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)
Products: -
Products: -
?
additional information
?
-
Substrates: low activity was observed with D-xylose (5%), D-glucose, D-fructose and D-mannose are not oxidized at significant rates
Products: -
Products: -
-
additional information
?
-
Substrates: low activity was observed with D-xylose (5%), D-glucose, D-fructose and D-mannose are not oxidized at significant rates
Products: -
Products: -
-
additional information
?
-
-
Substrates: some minor activity (about 1%) is measured with D-xylose and L-lyxose, while no activity is detected with D-glucose or L-rhamnose
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-arabinose + NAD(P)+
L-arabinono-1,4-lactone + NAD(P)H + H+
Substrates: the enzyme initiates L-arabinose degradation
Products: -
Products: -
?
D-galactose + NADP+
D-galactono-1,4-lactone + NADPH + H+
Substrates: the enzyme has an essential function during growth on D-galactose
Products: -
Products: -
?
D-galactose + NADP+
D-galactono-1,4-lactone + NADPH + H+
Substrates: the enzyme has an essential function during growth on D-galactose
Products: -
Products: -
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH + H+
Substrates: -
Products: -
Products: -
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH + H+
Substrates: -
Products: -
Products: -
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH + H+
Substrates: -
Products: -
Products: -
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
Substrates: -
Products: -
Products: -
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
Substrates: first step of L-arabinose metabolism. The enzyme is involved in the metabolism of L-arabinose but not D-galactose
Products: -
Products: -
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
Substrates: -
Products: -
Products: -
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
Substrates: -
Products: -
Products: -
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
the enzyme catalyzes the oxidation of L-arabinose with both NADP+ and NAD+ as electron acceptor, with a slight preference for NADP+
NAD+
-
the enzyme prefers NADP+ but uses also NAD+ as a cofactor
NAD+
570fold higher affinity with NADP+ (Km: 0.0028 mM) than NAD (Km: 1.586) when L-arabinose is used as a substrate. kcat value for NADP+ is 62.3/s, which is slightly smaller than that for NAD+ (105.9/s)
NAD+
preference of NADP+ over NAD+ is significantly subjected by a pair of Ser37 and Arg38
NAD+
preference of NADP+ over NAD+, wild-type enzyme. Mutant enzyme S37D/R38A shows a complete reversal of coenzyme specificity
NAD+
the catalytic efficiency for NAD+ is 230 times lower as for NADP+ indicating NADP+ to be the physiological electron acceptor
NADP+
the enzyme catalyzes the oxidation of L-arabinose with both NADP+ and NAD+ as electron acceptor, with a slight preference for NADP+
NADP+
-
the enzyme prefers NADP+ but uses also NAD+ as a cofactor
NADP+
570fold higher affinity with NADP+ (Km: 0.0028 mM) than NAD (Km: 1.586) when L-arabinose is used as a substrate. kcat value for NADP+ is 62.3/s, which is slightly smaller than that for NAD+ (105.9/s)
NADP+
preference of NADP+ over NAD+ is significantly subjected by a pair of Ser37 and Arg38
NADP+
preference of NADP+ over NAD+, wild-type enzyme. Mutant enzyme S37D/R38A shows a complete reversal of coenzyme specificity
NADP+
the catalytic efficiency for NAD+ is 230 times lower as for NADP+ indicating NADP+ to be the physiological electron acceptor
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KCl
NaCl
activity is dependent on KCl and NaCl. Maximal activities are obtained at 1.5 M KCl and 1 M NaCl
additional information
KCl
activity is dependent on KCl and NaCl. Maximal activities are obtained at 1.5 M KCl and 1 M NaCl
KCl
maximal activities are obtained at KCl concentrations higher than 1 M
additional information
no significant increase in activity in the presence of MgCl2, MnCl2, ZnCl2, CoCl2, NiCl2, or CaCl2 at final concentrations of 1 mM
additional information
-
no enhancement of activity in presence of divalent cations
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.255
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
0.785
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
1.41
L-arabinose
pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense
28.9
L-arabinose
pH 9.0, 30°C, cofactor: NADP+, mutant enzyme N172A
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
0.77
NAD+
-
L-arabinose as cosubstrate, in 100 mM Tris-HCl, pH 9.0, 23°C
0.05
NADP+
-
L-arabinose as cosubstrate, in 100 mM Tris-HCl, pH 9.0, 23°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
6.1
L-arabinose
pH 9.0, 30°C, cofactor: NAD+, recombinant wild-type enzyme
16.5
L-arabinose
pH 9.0, 30°C, cofactor: NADP+, recombinant wild-type enzyme
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
33.3
L-arabinose
pH 9.0, 30°C, cofactor: NADP+, enzyme purified from Azospirillum brasilense
65.55
L-arabinose
-
with NAD+ as cosubstrate, in 100 mM Tris-HCl, pH 9.0, 23°C
85.73
NAD+
-
L-arabinose as cosubstrate, in 100 mM Tris-HCl, pH 9.0, 23°C
35.45
NADP+
-
L-arabinose as cosubstrate, in 100 mM Tris-HCl, pH 9.0, 23°C