1.1.1.376: L-arabinose 1-dehydrogenase [NAD(P)+]
This is an abbreviated version!
For detailed information about L-arabinose 1-dehydrogenase [NAD(P)+], go to the full flat file.
Reaction
Synonyms
AraDH, HVO_A0330, HVO_B0032, L-arabino-aldose dehydrogenase, L-arabinose 1-dehydrogenase, L-arabinose/D-galactose 1-dehydrogenase, L-AraDH, NAD(P)-dependent L-arabinose 1-dehydrogenase
ECTree
1.1.1.376 L-arabinose 1-dehydrogenase [NAD(P)+]Advanced search results
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results (Substrates Products
Substrates Products on EC 1.1.1.376 - L-arabinose 1-dehydrogenase [NAD(P)+]
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-fucose + NAD+
D-fucono-1,4-lactone + NADH + H+
-
-
-
-
r
D-fucose + NADP+
D-fucono-1,4-lactone + NADPH + H+
-
-
-
-
r
D-galactose + NAD+
D-galactono-1,4-lactone + NADH + H+
-
-
-
-
r
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
-
-
?
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+
?
-
12% activity compared to D-fucose
-
-
?
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+
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+
-
-
-
?
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
-
-
?
