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D-arabitol + NAD+
?
-
Substrates: -
Products: -
?
D-arabitol + NAD+
? + NADH + H+
D-fructose + NADH + H+
D-sorbitol + NAD+
D-fructose + NADH + H+
sorbitol + NAD+
D-mannitol + NAD+
? + NADH + H+
Substrates: 8% of the activity with xylitol
Products: -
?
D-mannitol + NAD+
D-fructose + NADH + H+
D-ribitol + NAD+
D-ribulose + NADH
D-ribulose + NADH
D-ribitol + NAD+
-
Substrates: -
Products: -
r
D-ribulose + NADH + H+
?
Substrates: -
Products: -
?
D-sorbitol + NAD+
? + NADH + H+
D-sorbitol + NAD+
D-fructose + NADH + H+
D-sorbitol + NAD+
L-sorbose + NADH + H+
D-sorbose + NADH + H+
sorbitol + NAD+
-
Substrates: low activity
Products: -
r
D-xylitol + NAD+
D-xylulose + NADH + H+
D-xylulose + NAD+
xylitol + NADH + H+
-
Substrates: -
Products: -
r
D-xylulose + NADH + H+
D-xylitol + NAD+
D-xylulose + NADH + H+
xylitol + NAD+
dihydroxyacetone + NADH
glycerol + NAD+
-
Substrates: -
Products: -
?
erythritol + NAD+
? + NADH + H+
Substrates: 0.77% of the activity with xylitol
Products: -
?
erythritol + NAD+
L-erythrulose + NADH
-
Substrates: -
Products: -
r
galactitol + NAD+
? + NADH + H+
Substrates: 0.98% of the activity with xylitol
Products: -
?
glycerol + NAD+
glycerone + NADH + H+
L-arabinitol + NAD+
? + NADH + H+
Substrates: 21% of the activity with xylitol
Products: -
?
L-arabitol + NAD+
L-xylulose + NADH + H+
L-erythrulose + NADH
erythritol + NAD+
L-iditol + NAD+
?
-
Substrates: -
Products: -
?
L-sorbose + NADH + H+
?
Substrates: -
Products: -
?
L-threitol + NAD+
? + NADH + H+
L-xylulose + NADH
L-xylitol + NAD+
-
Substrates: -
Products: -
?
meso-erythritol + NAD+
? + NADH + H+
ribitol + NAD+
? + NADH + H+
Substrates: 40% of the activity with xylitol
Products: -
?
ribitol + NAD+
D-ribulose + NADH + H+
sorbitol + NAD+
D-fructose + NADH + H+
xylitol + NAD+
D-xylulose + NADH + H+
xylitol + NAD+
L-xylulose + NADH + H+
xylitol + NADP+
D-xylulose + NADPH + H+
additional information
?
-
D-arabitol + NAD+
? + NADH + H+
-
Substrates: -
Products: -
r
D-arabitol + NAD+
? + NADH + H+
-
Substrates: -
Products: -
r
D-fructose + NADH + H+
D-sorbitol + NAD+
-
Substrates: -
Products: -
?
D-fructose + NADH + H+
D-sorbitol + NAD+
Substrates: -
Products: -
r
D-fructose + NADH + H+
sorbitol + NAD+
-
Substrates: 46.4% activity compared to D-xylulose
Products: -
r
D-fructose + NADH + H+
sorbitol + NAD+
-
Substrates: 46.4% activity compared to D-xylulose
Products: -
r
D-iditol + NAD+
?
-
Substrates: 11.2% of the activity with xylitol
Products: -
?
D-iditol + NAD+
?
-
Substrates: 11.2% of the activity with xylitol
Products: -
?
D-mannitol + NAD+
?
-
Substrates: 16.1% activity compared to xylitol
Products: -
?
D-mannitol + NAD+
?
-
Substrates: 16.1% activity compared to xylitol
Products: -
?
D-mannitol + NAD+
?
Substrates: 2.6% activity compared to xylitol
Products: -
?
D-mannitol + NAD+
?
Substrates: 2.6% activity compared to xylitol
Products: -
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
Substrates: -
Products: -
r
D-mannitol + NAD+
D-fructose + NADH + H+
Substrates: low activity compared to xylitol
Products: -
r
D-mannitol + NAD+
D-fructose + NADH + H+
-
Substrates: low activity, reaction of EC 1.1.1.67
Products: -
r
D-mannitol + NAD+
D-fructose + NADH + H+
Substrates: low activity compared to xylitol
Products: -
r
D-mannitol + NAD+
D-fructose + NADH + H+
-
Substrates: -
Products: -
r
D-mannitol + NAD+
D-fructose + NADH + H+
-
Substrates: low activity, reaction of EC 1.1.1.67
Products: -
r
D-ribitol + NAD+
D-ribulose + NADH
-
Substrates: -
Products: -
?
D-ribitol + NAD+
D-ribulose + NADH
-
Substrates: -
Products: -
?
D-ribitol + NAD+
D-ribulose + NADH
-
Substrates: -
Products: -
?
D-ribitol + NAD+
D-ribulose + NADH
-
Substrates: 85% of the rate of xylitol oxidation
Products: -
?
D-ribitol + NAD+
D-ribulose + NADH
-
Substrates: -
Products: -
?
D-ribitol + NAD+
D-ribulose + NADH
-
Substrates: -
Products: -
r
D-ribitol + NAD+
D-ribulose + NADH
-
Substrates: oxidation at 11% of the rate of xylitol oxidation
Products: -
?
D-sorbitol + NAD+
? + NADH + H+
Substrates: -
Products: -
?
D-sorbitol + NAD+
? + NADH + H+
Substrates: -
Products: -
?
D-sorbitol + NAD+
D-fructose + NADH + H+
Substrates: -
Products: -
ir
D-sorbitol + NAD+
D-fructose + NADH + H+
-
Substrates: -
Products: -
r
D-sorbitol + NAD+
D-fructose + NADH + H+
-
Substrates: -
Products: -
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
Substrates: -
Products: -
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
Substrates: 69% of activity against D-xylitol
Products: -
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
Substrates: -
Products: -
r
D-sorbitol + NAD+
D-fructose + NADH + H+
-
Substrates: -
Products: -
r
D-sorbitol + NAD+
D-fructose + NADH + H+
Substrates: -
Products: -
r
D-sorbitol + NAD+
D-fructose + NADH + H+
-
Substrates: -
Products: -
r
D-sorbitol + NAD+
D-fructose + NADH + H+
Substrates: -
Products: -
r
D-sorbitol + NAD+
D-fructose + NADH + H+
-
Substrates: -
Products: -
r
D-sorbitol + NAD+
D-fructose + NADH + H+
-
Substrates: rate of xylitol oxidation at 67%
Products: -
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
Substrates: -
Products: -
r
D-sorbitol + NAD+
D-fructose + NADH + H+
-
Substrates: rate of xylitol oxidation at 95%
Products: -
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
Substrates: rate of xylitol oxidation at 56%
Products: -
?
D-sorbitol + NAD+
D-fructose + NADH + H+
Substrates: 90% of the activity with xylitol
Products: -
?
D-sorbitol + NAD+
D-fructose + NADH + H+
Substrates: 71.8% activity compared to xylitol
Products: -
r
D-sorbitol + NAD+
D-fructose + NADH + H+
Substrates: 71.8% activity compared to xylitol
Products: -
r
D-sorbitol + NAD+
D-fructose + NADH + H+
-
Substrates: oxidation at about 45%
Products: -
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
Substrates: -
Products: -
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
Substrates: rate of xylitol oxidation at 118%
Products: -
?
D-sorbitol + NAD+
L-sorbose + NADH + H+
-
Substrates: -
Products: -
r
D-sorbitol + NAD+
L-sorbose + NADH + H+
Substrates: 51.3% increased activity compared to xylitol
Products: -
?
D-sorbitol + NAD+
L-sorbose + NADH + H+
Substrates: 51.3% increased activity compared to xylitol
Products: -
?
D-sorbitol + NAD+
L-sorbose + NADH + H+
-
Substrates: -
Products: -
r
D-sorbitol + NAD+
L-sorbose + NADH + H+
Substrates: 71.8% activity compared to xylitol
Products: -
?
D-sorbitol + NAD+
L-sorbose + NADH + H+
Substrates: 71.8% activity compared to xylitol
Products: -
?
D-threitol + NAD+
?
-
Substrates: 109% of the activity with xylitol
Products: -
?
D-threitol + NAD+
?
-
Substrates: 109% of the activity with xylitol
Products: -
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
r
D-xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
r
D-xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
?
D-xylulose + NADH + H+
D-xylitol + NAD+
-
Substrates: specific for transferring the 4-pro-R hydrogen of NADH
Products: -
r
D-xylulose + NADH + H+
D-xylitol + NAD+
-
Substrates: -
Products: -
r
D-xylulose + NADH + H+
D-xylitol + NAD+
-
Substrates: -
Products: -
?
D-xylulose + NADH + H+
xylitol + NAD+
-
Substrates: -
Products: -
r
D-xylulose + NADH + H+
xylitol + NAD+
-
Substrates: -
Products: -
r
D-xylulose + NADH + H+
xylitol + NAD+
-
Substrates: 100% activity
Products: -
r
D-xylulose + NADH + H+
xylitol + NAD+
-
Substrates: 100% activity
Products: -
r
D-xylulose + NADH + H+
xylitol + NAD+
-
Substrates: -
Products: -
r
D-xylulose + NADH + H+
xylitol + NAD+
-
Substrates: -
Products: -
r
D-xylulose + NADH + H+
xylitol + NAD+
-
Substrates: -
Products: -
r
D-xylulose + NADH + H+
xylitol + NAD+
-
Substrates: -
Products: -
r
D-xylulose + NADH + H+
xylitol + NAD+
Substrates: -
Products: -
r
D-xylulose + NADH + H+
xylitol + NAD+
-
Substrates: -
Products: -
r
D-xylulose + NADH + H+
xylitol + NAD+
Substrates: -
Products: -
r
D-xylulose + NADH + H+
xylitol + NAD+
-
Substrates: -
Products: -
r
D-xylulose + NADH + H+
xylitol + NAD+
-
Substrates: -
Products: -
r
D-xylulose + NADH + H+
xylitol + NAD+
-
Substrates: -
Products: -
r
D-xylulose + NADH + H+
xylitol + NAD+
Substrates: -
Products: -
r
D-xylulose + NADH + H+
xylitol + NAD+
Substrates: -
Products: -
r
D-xylulose + NADH + H+
xylitol + NAD+
Substrates: -
Products: -
r
D-xylulose + NADH + H+
xylitol + NAD+
Substrates: -
Products: -
r
D-xylulose + NADH + H+
xylitol + NAD+
-
Substrates: -
Products: -
r
glycerol + NAD+
?
-
Substrates: -
Products: -
?
glycerol + NAD+
?
-
Substrates: poor substrate
Products: -
?
glycerol + NAD+
glycerone + NADH + H+
-
Substrates: low activity
Products: -
r
glycerol + NAD+
glycerone + NADH + H+
-
Substrates: low activity
Products: -
r
L-arabitol + NAD+
?
-
Substrates: -
Products: -
?
L-arabitol + NAD+
?
-
Substrates: -
Products: -
?
L-arabitol + NAD+
L-xylulose + NADH + H+
Substrates: the enzyme also has L-arabitol dehydrogenase activity (20.1% activity compared to xylitol)
Products: -
?
L-arabitol + NAD+
L-xylulose + NADH + H+
Substrates: about 20% activity compared to xylitol, reaction of EC 1.1.1.12
Products: -
r
L-arabitol + NAD+
L-xylulose + NADH + H+
Substrates: the enzyme also has L-arabitol dehydrogenase activity (20.1% activity compared to xylitol)
Products: -
?
L-arabitol + NAD+
L-xylulose + NADH + H+
Substrates: about 20% activity compared to xylitol, reaction of EC 1.1.1.12
Products: -
r
L-erythrulose + NADH
erythritol + NAD+
-
Substrates: reduction at the same rate as D-xylulose
Products: -
?
L-erythrulose + NADH
erythritol + NAD+
-
Substrates: -
Products: -
r
L-threitol + NAD+
? + NADH + H+
Substrates: 0.05% of the activity with xylitol
Products: -
?
L-threitol + NAD+
? + NADH + H+
Substrates: 75% of the activity with xylitol
Products: -
?
meso-erythritol + NAD+
? + NADH + H+
-
Substrates: -
Products: -
r
meso-erythritol + NAD+
? + NADH + H+
-
Substrates: -
Products: -
r
ribitol + NAD+
?
Substrates: -
Products: -
?
ribitol + NAD+
?
Substrates: -
Products: -
?
ribitol + NAD+
?
Substrates: -
Products: -
?
ribitol + NAD+
?
Substrates: 60.1% activity compared to xylitol
Products: -
?
ribitol + NAD+
D-ribulose + NADH + H+
Substrates: -
Products: -
r
ribitol + NAD+
D-ribulose + NADH + H+
Substrates: reaction of EC 1.1.1.56, ribitol 2-dehydrogenase
Products: -
?
ribitol + NAD+
D-ribulose + NADH + H+
Substrates: reaction of EC 1.1.1.56, ribitol 2-dehydrogenase
Products: -
?
ribitol + NAD+
D-ribulose + NADH + H+
Substrates: 60.1% activity compared to xylitol
Products: -
?
ribitol + NAD+
D-ribulose + NADH + H+
Substrates: 60.1% activity compared to xylitol
Products: -
?
sorbitol + NAD+
D-fructose + NADH + H+
-
Substrates: -
Products: -
?
sorbitol + NAD+
D-fructose + NADH + H+
-
Substrates: 153.9% activity compared to xylitol
Products: -
r
sorbitol + NAD+
D-fructose + NADH + H+
-
Substrates: 153.9% activity compared to xylitol
Products: -
r
Xylitol + NAD+
?
-
Substrates: -
Products: -
?
Xylitol + NAD+
?
-
Substrates: -
Products: -
?
Xylitol + NAD+
?
-
Substrates: -
Products: -
?
Xylitol + NAD+
?
-
Substrates: inducible pathway of xylose catabolism
Products: -
r
Xylitol + NAD+
?
-
Substrates: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: key enzyme in D-xylose metabolism
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
?, r
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: 100% activity
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: 100% activity
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
?, r
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: preferred substrate
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: preferred substrates
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: preferred substrate
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: preferred substrates
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: a xylose reductase, using either NADH or NADPH, reduces D-xylose to xylitol, subsequently xylitol is oxidized to D-xylulose by the NAD+-linked xylitol dehydrogenase
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: a xylose reductase, using either NADH or NADPH, reduces D-xylose to xylitol, subsequently xylitol is oxidized to D-xylulose by the NAD+-linked xylitol dehydrogenase
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: a xylose reductase, using either NADH or NADPH, reduces D-xylose to xylitol, subsequently xylitol is oxidized to D-xylulose by the NAD+-linked xylitol dehydrogenase
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: best substrate
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: 100% activity
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: 100% activity
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: best substrate
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
r
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
?
xylitol + NAD+
D-xylulose + NADH + H+
-
Substrates: -
Products: -
?
xylitol + NAD+
L-xylulose + NADH + H+
-
Substrates: -
Products: -
?
xylitol + NAD+
L-xylulose + NADH + H+
-
Substrates: -
Products: -
?
xylitol + NAD+
L-xylulose + NADH + H+
Substrates: -
Products: -
?
xylitol + NADP+
D-xylulose + NADPH + H+
Substrates: wild-type enzyme shows no activity with NADP+, mutant enzyme D38S/M39R is able to exclusively use NADP+, with no loss of activity
Products: -
?
xylitol + NADP+
D-xylulose + NADPH + H+
Substrates: very low activity with NADP+
Products: -
r
xylitol + NADP+
D-xylulose + NADPH + H+
Substrates: mutant enzyme D205A/I260R shows activity with NADP+
Products: -
r
xylitol + NADP+
D-xylulose + NADPH + H+
-
Substrates: -
Products: -
?
xylitol + NADP+
D-xylulose + NADPH + H+
Substrates: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is specific for polyols that have a hydroxyl group at the C-2 and C-3 positions in the L- and D-sides, respectively, in the Fischer projection
Products: -
?
additional information
?
-
-
Substrates: the enzyme is specific for polyols that have a hydroxyl group at the C-2 and C-3 positions in the L- and D-sides, respectively, in the Fischer projection
Products: -
?
additional information
?
-
-
Substrates: specific for NAD+
Products: -
?
additional information
?
-
-
Substrates: specific for transferring the 4-pro-R hydrogen of NADH
Products: -
?
additional information
?
-
-
Substrates: specific for NAD+
Products: -
?
additional information
?
-
-
Substrates: specific for NAD+
Products: -
?
additional information
?
-
-
Substrates: no reduction of D-ribose and D-galacturonic acid
Products: -
?
additional information
?
-
-
Substrates: no oxidation of threitol, xylitol, sorbitol, D-iditol
Products: -
?
additional information
?
-
-
Substrates: no reduction of D-ribulose
Products: -
?
additional information
?
-
-
Substrates: no reduction of D/L-xylose
Products: -
?
additional information
?
-
-
Substrates: no substrate: glycerol
Products: -
?
additional information
?
-
Substrates: enzyme XDH depends exclusively on NAD+/NADH as cofactors
Products: -
?
additional information
?
-
-
Substrates: enzyme XDH depends exclusively on NAD+/NADH as cofactors
Products: -
?
additional information
?
-
-
Substrates: the enzyme shows high activity to convert D-sorbitol to D-fructose. The enzyme is highly specific toward D-sorbitol and xylitol, but shows limited activity toward D-mannitol, sorbose, and glycerol. The enzyme shows no activity when glucose, inositol, galactose, mannose, rhamnose, xylose, fructose, glucuronic acid, glucolactone, 2-oxo-L-gulonic acid (2-KLG), gluconic, propanol, isopropanol, methanol, and ethanol are used as substrates
Products: -
-
additional information
?
-
Substrates: enzyme XDH depends exclusively on NAD+/NADH as cofactors
Products: -
?
additional information
?
-
-
Substrates: the enzyme shows high activity to convert D-sorbitol to D-fructose. The enzyme is highly specific toward D-sorbitol and xylitol, but shows limited activity toward D-mannitol, sorbose, and glycerol. The enzyme shows no activity when glucose, inositol, galactose, mannose, rhamnose, xylose, fructose, glucuronic acid, glucolactone, 2-oxo-L-gulonic acid (2-KLG), gluconic, propanol, isopropanol, methanol, and ethanol are used as substrates
Products: -
-
additional information
?
-
-
Substrates: no oxidation of threitol, xylitol, sorbitol, D-iditol
Products: -
?
additional information
?
-
-
Substrates: no reduction of D-fructose, L-sorbose and D-tagatose
Products: -
?
additional information
?
-
-
Substrates: specific for polyols of 5 or less carbon bearing cis-hydroxy groups in C2 and C3
Products: -
?
additional information
?
-
-
Substrates: specific for NAD+
Products: -
?
additional information
?
-
-
Substrates: specific for NAD+
Products: -
?
additional information
?
-
-
Substrates: no activity with D-mannitol, erythritol, and D-arabitol. Very low activity with NADP+
Products: -
?
additional information
?
-
Substrates: no activity with D-mannitol, erythritol, and D-arabitol. Very low activity with NADP+
Products: -
?
additional information
?
-
-
Substrates: the enzyme exhibits broad specificity to polyols, such as xylitol, D-sorbitol, ribitol, and L-arabinitol. Xylitol is the preferred substrate, but native and recombinant enzyme McXDH exhibits relative activities toward L-arabinitol of approximately 20% that toward xylitol. No activity with D-mannitol, erythritol, and D-arabinitol
Products: -
?
additional information
?
-
Substrates: the enzyme exhibits broad specificity to polyols, such as xylitol, D-sorbitol, ribitol, and L-arabinitol. Xylitol is the preferred substrate, but native and recombinant enzyme McXDH exhibits relative activities toward L-arabinitol of approximately 20% that toward xylitol. No activity with D-mannitol, erythritol, and D-arabinitol
Products: -
?
additional information
?
-
Substrates: the enzyme has L-arabitol dehydrogenase (LAD, EC 1.1.1.12) activity and also exhibits broad specificity to polyols, such as xylitol, D-sorbitol, ribitol, and L-arabitol. Xylitol is the preferred substrate
Products: -
-
additional information
?
-
-
Substrates: the enzyme has L-arabitol dehydrogenase (LAD, EC 1.1.1.12) activity and also exhibits broad specificity to polyols, such as xylitol, D-sorbitol, ribitol, and L-arabitol. Xylitol is the preferred substrate
Products: -
-
additional information
?
-
-
Substrates: no activity with D-mannitol, erythritol, and D-arabitol. Very low activity with NADP+
Products: -
?
additional information
?
-
Substrates: no activity with D-mannitol, erythritol, and D-arabitol. Very low activity with NADP+
Products: -
?
additional information
?
-
-
Substrates: the enzyme exhibits broad specificity to polyols, such as xylitol, D-sorbitol, ribitol, and L-arabinitol. Xylitol is the preferred substrate, but native and recombinant enzyme McXDH exhibits relative activities toward L-arabinitol of approximately 20% that toward xylitol. No activity with D-mannitol, erythritol, and D-arabinitol
Products: -
?
additional information
?
-
Substrates: the enzyme exhibits broad specificity to polyols, such as xylitol, D-sorbitol, ribitol, and L-arabinitol. Xylitol is the preferred substrate, but native and recombinant enzyme McXDH exhibits relative activities toward L-arabinitol of approximately 20% that toward xylitol. No activity with D-mannitol, erythritol, and D-arabinitol
Products: -
?
additional information
?
-
Substrates: the enzyme has L-arabitol dehydrogenase (LAD, EC 1.1.1.12) activity and also exhibits broad specificity to polyols, such as xylitol, D-sorbitol, ribitol, and L-arabitol. Xylitol is the preferred substrate
Products: -
-
additional information
?
-
-
Substrates: the enzyme has L-arabitol dehydrogenase (LAD, EC 1.1.1.12) activity and also exhibits broad specificity to polyols, such as xylitol, D-sorbitol, ribitol, and L-arabitol. Xylitol is the preferred substrate
Products: -
-
additional information
?
-
-
Substrates: specific for NAD+
Products: -
?
additional information
?
-
-
Substrates: glucose:xylose ratio of 1:2.5 promotes a 2.7fold increase in activity when compared to a glucose:xylose ratio of 1:25
Products: -
?
additional information
?
-
-
Substrates: specific for NAD+
Products: -
?
additional information
?
-
-
Substrates: no reduction of D/L-xylose
Products: -
?
additional information
?
-
-
Substrates: no reduction of L-xylulose
Products: -
?
additional information
?
-
-
Substrates: no oxidation of ribitol
Products: -
?
additional information
?
-
-
Substrates: no oxidation of inositol, meso-erythritol and D-(+)-arabitol
Products: -
?
additional information
?
-
-
Substrates: no oxidation of mannitol
Products: -
?
additional information
?
-
-
Substrates: specific for NAD+
Products: -
?
additional information
?
-
-
Substrates: no reduction of D/L-xylose
Products: -
?
additional information
?
-
-
Substrates: no reduction of L-xylulose
Products: -
?
additional information
?
-
-
Substrates: no oxidation of ribitol
Products: -
?
additional information
?
-
Substrates: the enzyme shows less than 1% activity with erythritol, galactitol, D-arabitol, L-arabitol, and glycerol, and 3.1% activity with NADP+ compared to NAD+
Products: -
?
additional information
?
-
-
Substrates: the enzyme shows less than 1% activity with erythritol, galactitol, D-arabitol, L-arabitol, and glycerol, and 3.1% activity with NADP+ compared to NAD+
Products: -
?
additional information
?
-
Substrates: the enzyme shows less than 1% activity with erythritol, galactitol, D-arabitol, L-arabitol, and glycerol, and 3.1% activity with NADP+ compared to NAD+
Products: -
?
additional information
?
-
-
Substrates: the enzyme shows less than 1% activity with erythritol, galactitol, D-arabitol, L-arabitol, and glycerol, and 3.1% activity with NADP+ compared to NAD+
Products: -
?
additional information
?
-
-
Substrates: investigation of limiting metabolic steps in the utilization of xylose by recombinant Saccharomyces cerevisiae using metabolic engineering
Products: -
?
additional information
?
-
-
Substrates: no oxidation of ribitol
Products: -
?
additional information
?
-
-
Substrates: no oxidation of mannitol
Products: -
?
additional information
?
-
-
Substrates: specific for NAD+
Products: -
?
additional information
?
-
-
Substrates: specific for NAD+
Products: -
?
additional information
?
-
-
Substrates: specific for NAD+
Products: -
?
additional information
?
-
-
Substrates: no reduction of D/L-xylose
Products: -
?
additional information
?
-
-
Substrates: no reduction of L-xylulose
Products: -
?
additional information
?
-
-
Substrates: no oxidation of ribitol
Products: -
?
additional information
?
-
-
Substrates: specific for NAD+
Products: -
?
additional information
?
-
-
Substrates: specific for NAD+
Products: -
?
additional information
?
-
-
Substrates: specific for NAD+
Products: -
?
additional information
?
-
-
Substrates: specific for NAD+
Products: -
?
additional information
?
-
-
Substrates: specific for NAD+
Products: -
?
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Adenocarcinoma
Acquired xanthine dehydrogenase expression shortens survival in patients with resected adenocarcinoma of lung.
Arthralgia
[Xanthinuria type 1 in a woman with arthralgias: a combined clinical and molecular genetic investigation].
Arthritis, Rheumatoid
Xanthine dehydrogenase deficiency with novel sequence variations presenting as rheumatoid arthritis in a 78-year-old patient.
Atherosclerosis
Associations of hypertension and its complications with variations in the xanthine dehydrogenase gene.
Bacterial Infections
Role of xanthine dehydrogenase and aging on the innate immune response of Drosophila.
Breast Neoplasms
Low levels of both xanthine dehydrogenase and cellular retinol binding protein are responsible for retinoic acid deficiency in malignant human mammary epithelial cells.
Breast Neoplasms
Xanthine dehydrogenase as a prognostic biomarker related to tumor immunology in hepatocellular carcinoma.
Carcinoma
Xanthine dehydrogenase as a prognostic biomarker related to tumor immunology in hepatocellular carcinoma.
Carcinoma, Hepatocellular
Metabolism of xylitol and glucose in rats bearing hepatocellular.
Carcinoma, Hepatocellular
Xanthine dehydrogenase as a prognostic biomarker related to tumor immunology in hepatocellular carcinoma.
Carcinoma, Hepatocellular
Xanthine dehydrogenase downregulation promotes TGF? signaling and cancer stem cell-related gene expression in hepatocellular carcinoma.
Crohn Disease
Influences of XDH genotype by gene-gene interactions with SUCLA2 for thiopurine-induced leukopenia in Korean patients with Crohn's disease.
Crohn Disease
P702. Influences of XDH genotype on thiopurine-induced leukopenia in Korean patients with Crohn's disease determined by gene-gene interactions.
d-xylulose reductase deficiency
Gout, uric acid and purine metabolism in paediatric nephrology.
d-xylulose reductase deficiency
Purine and pyrimidine metabolites in children's urine.
d-xylulose reductase deficiency
The RNAi-Mediated Silencing of Xanthine Dehydrogenase Impairs Growth and Fertility and Accelerates Leaf Senescence in Transgenic Arabidopsis Plants.
d-xylulose reductase deficiency
Xanthine dehydrogenase deficiency with novel sequence variations presenting as rheumatoid arthritis in a 78-year-old patient.
Dehydration
The plant Mo-hydroxylases aldehyde oxidase and xanthine dehydrogenase have distinct reactive oxygen species signatures and are induced by drought and abscisic acid.
Drug-Related Side Effects and Adverse Reactions
Novel pharmacogenetic markers for treatment outcome in azathioprine-treated inflammatory bowel disease.
Drug-Related Side Effects and Adverse Reactions
Polymorphism of genes involved in purine metabolism (XDH, AOX1, MOCOS) in kidney transplant recipients receiving azathioprine.
Genetic Diseases, Inborn
Assignment of human xanthine dehydrogenase gene to chromosome 2p22.
Hydrocephalus
Gene expression analysis of the development of congenital hydrocephalus in the H-Tx rat.
Hypertension
Association between Serum Urate and Risk of Hypertension in Menopausal Women with XDH Gene.
Hypertension
Association between xanthine dehydrogenase tag single nucleotide polymorphisms and essential hypertension.
Hypertension
Associations of hypertension and its complications with variations in the xanthine dehydrogenase gene.
Infections
Role of xanthine dehydrogenase and aging on the innate immune response of Drosophila.
Inflammatory Bowel Diseases
AOX1 and XDH Enzymes Genotyping and its Effect on Clinical Response to Azathioprine in Inflammatory Bowel Disease Patients Among Jordanian Population.
Leukopenia
Influences of XDH genotype by gene-gene interactions with SUCLA2 for thiopurine-induced leukopenia in Korean patients with Crohn's disease.
Leukopenia
P702. Influences of XDH genotype on thiopurine-induced leukopenia in Korean patients with Crohn's disease determined by gene-gene interactions.
Lung Injury
Abdominal paracentesis drainage protects rats against severe acute pancreatitis-associated lung injury by reducing the mobilization of intestinal XDH/XOD.
Lung Neoplasms
Acquired xanthine dehydrogenase expression shortens survival in patients with resected adenocarcinoma of lung.
Lung Neoplasms
Genomic signatures defining responsiveness to allopurinol and combination therapy for lung cancer identified by systems therapeutics analyses.
Lung Neoplasms
Xanthine dehydrogenase as a prognostic biomarker related to tumor immunology in hepatocellular carcinoma.
Melanosis
Allopurinol-induced melanism in the tiger salamander (Ambystoma tigrinum nebulosum).
Meningioma
Lead exposure, polymorphisms in genes related to oxidative stress, and risk of adult brain tumors.
Meningioma
Risk of meningioma and common variation in genes related to innate immunity.
Mesothelioma
Xanthine dehydrogenase as a prognostic biomarker related to tumor immunology in hepatocellular carcinoma.
Muscle Spasticity
Xanthine dehydrogenase (XDH): episodic evolution of a "neutral" protein.
Neoplasm Metastasis
Acquired xanthine dehydrogenase expression shortens survival in patients with resected adenocarcinoma of lung.
Neoplasms
A pan-cancer study of the transcriptional regulation of uricogenesis in human tumours: pathological and pharmacological correlates.
Neoplasms
Acquired xanthine dehydrogenase expression shortens survival in patients with resected adenocarcinoma of lung.
Neoplasms
Conversion of xanthine dehydrogenase to xanthine oxidase as a possible marker for hypoxia in tumours and normal tissues.
Neoplasms
Effect of environmental nitric oxides on the antitumor resistance of rats.
Neoplasms
Genomic signatures defining responsiveness to allopurinol and combination therapy for lung cancer identified by systems therapeutics analyses.
Neoplasms
Low levels of both xanthine dehydrogenase and cellular retinol binding protein are responsible for retinoic acid deficiency in malignant human mammary epithelial cells.
Neoplasms
Metabolism of xylitol and glucose in rats bearing hepatocellular.
Neoplasms
Reductive activation of doxorubicin by xanthine dehydrogenase from EMT6 mouse mammary carcinoma tumors.
Neoplasms
Targeted knock-in mice expressing the oxidase-fixed form of xanthine oxidoreductase favor tumor growth.
Neoplasms
Xanthine dehydrogenase as a prognostic biomarker related to tumor immunology in hepatocellular carcinoma.
Neoplasms
Xanthine dehydrogenase downregulation promotes TGF? signaling and cancer stem cell-related gene expression in hepatocellular carcinoma.
Nephrolithiasis
Mutational analysis of the xanthine dehydrogenase gene in a Turkish family with autosomal recessive classical xanthinuria.
Neutropenia
Pathway genes and metabolites in thiopurine therapy in Korean children with acute lymphoblastic leukaemia.
Obesity
Body mass index is independently associated with xanthine oxidase activity in overweight/obese population.
Obesity
Hepatocyte-Specific Ablation or Whole-Body Inhibition of Xanthine Oxidoreductase in Mice Corrects Obesity-Induced Systemic Hyperuricemia Without Improving Metabolic Abnormalities.
Ovarian Neoplasms
Xanthine dehydrogenase as a prognostic biomarker related to tumor immunology in hepatocellular carcinoma.
Pancreatitis
Mobilization of xanthine oxidase from the gastrointestinal tract in acute pancreatitis.
Renal Insufficiency
A mouse model of early-onset renal failure due to a xanthine dehydrogenase nonsense mutation.
Renal Insufficiency
[New antihyperuricemic medicine: febuxostat, Puricase, etc]
Reperfusion Injury
Mechanisms of gastrointestinal ischemia-reperfusion injury and potential therapeutic interventions: a review and its implications in the horse.
Spinal Cord Injuries
Xanthine oxidase in experimental spinal cord injury.
Stomach Neoplasms
Genetic variants in XDH are associated with prognosis for gastric cancer in a Chinese population.
Stomach Neoplasms
Xanthine dehydrogenase as a prognostic biomarker related to tumor immunology in hepatocellular carcinoma.
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19.8
D-fructose
at pH 7.0 and 30°C
0.7
D-ribulose
35°C, pH 7.5, native enzyme
0.00492 - 31.5
D-sorbitol
0.9
L-sorbose
35°C, pH 7.5, native enzyme
additional information
additional information
-
0.00492
D-sorbitol
-
pH 12.0, 30°C, recombinant enzyme
3
D-sorbitol
-
kcat/Km (sorbitol): 9500/Msec
4
D-sorbitol
35°C, pH 7.5, native enzyme
21.2
D-sorbitol
at pH 7.0 and 30°C
21.2
D-sorbitol
pH 7.0, 30°C, native enzyme
31.5
D-sorbitol
at pH 7.0 and 30°C
31.5
D-sorbitol
native enzyme, pH 9.0, 35°C
12
D-xylitol
-
pH 8.2, 22°C
0.66
D-xylulose
-
-
2
D-xylulose
35°C, pH 7.5, native enzyme
8.25
D-xylulose
at pH 7.0 and 30°C
10
D-xylulose
-
25°C, pH 9.0
43.9
D-xylulose
-
at pH 5.0 and 35°C
31.1
L-arabitol
at pH 7.0 and 30°C
31.1
L-arabitol
pH 7.0, 30°C, native enzyme
132
L-arabitol
pH 7.0, 30°C, recombinant enzyme
0.027
NAD+
native enzyme, at pH 7.0 and 30°C
0.027
NAD+
native enzyme, pH 9.0, 35°C
0.1
NAD+
pH 7.0, 30°C, recombinant enzyme, with xylitol
0.11
NAD+
at pH 7.0 and 30°C
0.11
NAD+
pH 7.0, 30°C, native enzyme, with xylitol
0.152
NAD+
pH 9.0, 35°C, mutant enzyme D207A/I208R/F209Y
0.162
NAD+
pH 9.0, 35°C, mutant enzyme D207A/F209S
0.186
NAD+
recombinant enzyme, at pH 7.0 and 30°C
0.186
NAD+
recombinant wild-type enzyme, pH 9.0, 35°C
0.265
NAD+
pH 9.0, 35°C, mutant enzyme D207A/I208R/F209T
0.348
NAD+
pH 7.0, wild-type enzyme
0.381
NAD+
pH 9.0, 35°, wild-type enzyme
0.403
NAD+
pH 9.0, 35°C, mutant enzyme D207A
0.498
NAD+
pH 9.0, 35°C, mutant enzyme I208R
0.52
NAD+
-
recombinant enzyme, pH 9.0, 35°C
0.538
NAD+
pH 9.0, 35°C, mutant enzyme N211R
0.568
NAD+
pH 9.0, 35°C, mutant enzyme D207A/I208R
0.665
NAD+
pH 9.0, 35°C, mutant enzyme I208R/F209S
0.739
NAD+
pH 9.0, 35°C, mutant enzyme S96C/S99CY102C
0.848
NAD+
pH 9.0, 35°C, mutant enzyme F209S
1.3
NAD+
pH 9.0, 35°C, mutant enzyme D207A/I208R/F209S
7.6
NAD+
pH 9.0, 35°C, mutant enzym S96C/S99C/Y102C/D207A/I208R/F209S/N211R
13.5
NAD+
mutant enzyme D205A, at pH 7.0 and 30°C
13.5
NAD+
recombinant mutant D205A, pH 9.0, 35°C
17.3
NAD+
pH 9.0, 35°C, mutant enzyme D207A/I208R/F209S/N211R
23.5
NAD+
pH 9.0, 35°C, mutant enzyme S96C/S99C/Y102C/D207A/I208R/F209S
32.37
NAD+
recombinant wild-type enzyme, pH 9.0, 35°C
34.3
NAD+
mutant enzyme D205A/I206R, at pH 7.0 and 30°C
34.3
NAD+
recombinant mutant D205A/I206R, pH 9.0, 35°C
107.3
NAD+
-
at pH 7.0 and 30°C
290
NAD+
-
mutant E154C, kcat/Km (NAD+): 4100/Msec
430
NAD+
-
kcat/Km (NAD+): 370000/Msec
500
NAD+
-
kcat/Km (NAD+): 57000/Msec
0.037
NADH
-
-
36.4
NADH
-
at pH 5.0 and 35°C
0.0205
NADP+
pH 7.0, mutant enzyme D38S/M39R
0.638
NADP+
pH 9.0, 35°C, mutant enzyme D207A/I208R/F209T
0.712
NADP+
mutant enzyme D205A/I206R, at pH 7.0 and 30°C
0.731
NADP+
pH 9.0, 35°C, mutant enzyme D207A/I208R/F209Y
0.897
NADP+
pH 9.0, 35°C, mutant enzyme D207A/I208R/F209S
1.04
NADP+
pH 9.0, 35°C, mutant enzym S96C/S99C/Y102C/D207A/I208R/F209S/N211R
1.18
NADP+
pH 9.0, 35°C, mutant enzyme S96C/S99C/Y102C/D207A/I208R/F209S
1.38
NADP+
pH 9.0, 35°C, mutant enzyme D207A/I208R/F209S/N211R
2.54
NADP+
mutant enzyme D205A, at pH 7.0 and 30°C
7.28
NADP+
pH 7.0, 30°C, native enzyme, with xylitol
9.19
NADP+
pH 9.0, 35°C, mutant enzyme I208R/F209S
9.56
NADP+
pH 9.0, 35°C, mutant enzyme S96C/S99CY102C
9.96
NADP+
pH 9.0, 35°C, mutant enzyme D207A/F209S
10.2
NADP+
recombinant enzyme, at pH 7.0 and 30°C
11.3
NADP+
pH 9.0, 35°C, mutant enzyme D207A/I208R
21.1
NADP+
pH 9.0, 35°C, mutant enzyme I208R
28.9
NADP+
pH 9.0, 35°C, mutant enzyme F209S
56.5
NADP+
pH 9.0, 35°C, mutant enzyme N211R
120
NADP+
pH 9.0, 35°C, mutant enzyme D207A
170
NADP+
pH 9.0, 35°, wild-type enzyme
15.8
ribitol
at pH 7.0 and 30°C
15.8
ribitol
pH 7.0, 30°C, native enzyme
149
ribitol
at pH 7.0 and 30°C
149
ribitol
native enzyme, pH 9.0, 35°C
21
sorbitol
-
kcat/Km (sorbitol): 7800/Msec
785
sorbitol
-
mutant E154C, kcat/Km (sorbitol): 1.5/Msec
0.039
xylitol
-
-
0.1
xylitol
recombinant enzyme, pH 7.0, 30°C
0.11
xylitol
native enzyme, pH 7.0, 30°C
0.638
xylitol
pH 9.0, 35°C, cofactor: NADP+, mutant enzyme D207A/I208R/F209T
0.731
xylitol
pH 9.0, 35°C, cofactor: NADP+, mutant enzyme D207A/I208R/F209Y
0.897
xylitol
pH 9.0, 35°C, cofactor: NADP+, mutant enzyme D207A/I208R/F209S
1.04
xylitol
pH 9.0, 35°C, cofactor: NADP+, mutant enzyme S96C/S99C/Y102C/D207A/I208R/F209S/N211R
1.18
xylitol
pH 9.0, 35°C, cofactor: NADP+, mutant enzyme S96C/S99C/Y102C/D207A/I208R/F209S
1.38
xylitol
pH 9.0, 35°C, cofactor: NADP+, mutant enzyme D207A/I208R/F209S/N211R
4
xylitol
35°C, pH 7.5, native enzyme
4 - 5.4
xylitol
pH 9.0, 35°C, cofactor: NAD+, mutant enzyme I208R/F209S
5.2
xylitol
35°C, pH 7.5, recombinant enzyme
7.83
xylitol
native enzyme, at pH 7.0 and 30°C
7.83
xylitol
native enzyme, pH 9.0, 35°C, with NAD+
9.56
xylitol
pH 9.0, 35°C, cofactor: NADP+, mutant enzyme S96C/S99CY102C
9.96
xylitol
pH 9.0, 35°C, cofactor: NADP+, mutant enzyme D207A/F209S
10.1
xylitol
recombinant enzyme, at pH 7.0 and 30°C
10.1
xylitol
recombinant wild-type enzyme, pH 9.0, 35°C, with NAD+
10.38
xylitol
pH 7.0, 30°C, recombinant enzyme
12.1
xylitol
pH 9.5, 25°C
13.7
xylitol
pH 7.0, cofactor: NAD+, wild-type enzyme
15.4
xylitol
recombinant enzyme, pH 7.0, 30°C
16
xylitol
pH 7.0, 30°C, recombinant enzyme
16
xylitol
native enzyme, pH 7.0, 30°C
16.1
xylitol
at pH 7.0 and 30°C
16.1
xylitol
pH 7.0, 30°C, native enzyme
17.64
xylitol
pH 7.0, 30°C, recombinant enzyme
20.96
xylitol
pH 7.0, 30°C, recombinant enzyme
21.7
xylitol
pH 9.0, 35°, cofactor: NAD+, wild-type enzyme
21.7
xylitol
-
wild-type XDH: kcat/Km (NAD+): 2760 l/min/mmol, kcat/Km (NADP+): 2790 l/min/mmol
22.2
xylitol
pH 9.0, 35°C, cofactor: NAD+, mutant enzyme D207A
24.2
xylitol
pH 9.0, 35°C, cofactor: NAD+, mutant enzyme D207A/I208R
27.4
xylitol
pH 9.0, 35°C, cofactor: NAD+, mutant enzyme N211R
29.5
xylitol
pH 9.0, 35°C, cofactor: NAD+, mutant enzyme I208R
30.3
xylitol
pH 9.0, 35°C, cofactor: NAD+, mutant enzyme S96C/S99CY102C
31.1
xylitol
-
mutant D207A/I208R/F209S: kcat/Km (NAD+): 181 l/min/mmol, kcat/Km (NADP+): 0.65 l/min/mmol
34.1
xylitol
pH 9.0, 35°C, cofactor: NAD+, mutant enzyme F209S
45.2
xylitol
pH 9.0, 35°C, cofactor: NAD+, mutant enzyme D207A/F209S
50.1
xylitol
pH 9.0, 35°C, cofactor: NAD+, mutant enzyme D207A/I208R/F209Y
55.7
xylitol
pH 9.0, 35°C, cofactor: NAD+, mutant enzyme D207A/I208R/F209S
66.7
xylitol
mutant enzyme D205A, with NAD+ as cosubstrate, at pH 7.0 and 30°C
66.7
xylitol
recombinant mutant D205A, pH 9.0, 35°C, with NAD+
86
xylitol
-
recombinant enzyme, pH 9.0, 35°C
97.8
xylitol
pH 9.0, 35°C, cofactor: NAD+, mutant enzyme D207A/I208R/F209T
100
xylitol
pH 7.0, cofactor: NADP+ mutant enzyme D38S/M39R
111
xylitol
-
mutant S96C/S99C/Y102C/D207A/I208R/F209S: kcat/Km (NADP+): 10700 l/min/mmol
130
xylitol
mutant enzyme D205A/I206R, with NADP+ as cosubstrate, at pH 7.0 and 30°C
175.5
xylitol
-
at pH 7.0 and 30°C
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
steady-state kinetic analysis of wild-type and mutant enzymes, overview
-
additional information
additional information
-
kinetics of mutant enzymes in engineered strains, detailed overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
920
D-fructose
-
25°C, pH 7.5, Tris-HCl
74
D-ribulose
35°C, pH 7.5, native enzyme
216
L-sorbose
35°C, pH 7.5, native enzyme
2 - 8
D-sorbitol
-
-
8.28
D-sorbitol
at pH 7.0 and 30°C
8.28
D-sorbitol
pH 7.0, 30°C, native enzyme
114
D-sorbitol
-
25°C, pH 7.5, Tris-HCl
528
D-sorbitol
35°C, pH 7.5, native enzyme
302.9
D-xylulose
35°C, pH 7.5, native enzyme
1500
D-xylulose
-
25°C, pH 7.5, Tris-HCl
1800
D-xylulose
-
25°C, pH 7.5, potassium phosphate
3.35
L-arabitol
at pH 7.0 and 30°C
3.35
L-arabitol
pH 7.0, 30°C, native enzyme
0.052 - 2.1
NAD+
pH 9.0, 35°C, mutant enzyme D207A/I208R
0.5
NAD+
pH 9.0, 35°C, mutant enzym S96C/S99C/Y102C/D207A/I208R/F209S/N211R
1
NAD+
pH 9.0, 35°C, mutant enzyme D207A/I208R/F209Y
1
NAD+
pH 9.0, 35°C, mutant enzyme I208R/F209S
1.16
NAD+
mutant enzyme D205A/I206R, at pH 7.0 and 30°C
1.16
NAD+
recombinant mutant D205A/I206R, pH 9.0, 35°C
3.33
NAD+
pH 9.0, 35°C, mutant enzyme D207A/F209S
4
NAD+
pH 9.0, 35°C, mutant enzyme D207A/I208R/F209S
5.17
NAD+
pH 9.0, 35°C, mutant enzyme D207A
5.17
NAD+
pH 9.0, 35°C, mutant enzyme D207A/I208R/F209T
5.18
NAD+
mutant enzyme D205A, at pH 7.0 and 30°C
5.18
NAD+
recombinant mutant D205A, pH 9.0, 35°C
6.35
NAD+
recombinant enzyme, at pH 7.0 and 30°C
6.35
NAD+
recombinant wild-type enzyme, pH 9.0, 35°C
10.33
NAD+
pH 9.0, 35°C, mutant enzyme D207A/I208R
13.17
NAD+
pH 9.0, 35°C, mutant enzym S96C/S99C/Y102C/D207A/I208R/F209S/N211R
16.9
NAD+
pH 9.0, 35°C, mutant enzyme N211R
17.5
NAD+
pH 9.0, 35°, wild-type enzyme
18
NAD+
pH 9.0, 35°C, mutant enzyme D207A/I208R/F209S/N211R
18.5
NAD+
pH 7.0, 30°C, native enzyme, with xylitol
20.33
NAD+
pH 9.0, 35°C, mutant enzyme F209S
22.83
NAD+
pH 9.0, 35°C, mutant enzyme N211R
23.8
NAD+
pH 9.0, 35°C, mutant enzyme I208R
23.83
NAD+
pH 9.0, 35°C, mutant enzyme D207A/I208R/F209S/N211R
27.2
NAD+
pH 7.0, wild-type enzyme
29.5
NAD+
pH 9.0, 35°C, mutant enzyme S96C/S99C/Y102C/D207A/I208R/F209S
30.33
NAD+
pH 9.0, 35°C, mutant enzyme S96C/S99CY102C
0.017
NADP+
pH 9.0, 35°C, mutant enzyme D207A/I208R/F209T
0.145
NADP+
pH 9.0, 35°C, mutant enzyme I208R/F209S
0.185
NADP+
recombinant enzyme, at pH 7.0 and 30°C
0.206
NADP+
pH 7.0, mutant enzyme D38S/M39R
0.33
NADP+
mutant enzyme D205A, at pH 7.0 and 30°C
0.4
NADP+
mutant enzyme D205A/I206R, at pH 7.0 and 30°C
0.91
NADP+
pH 9.0, 35°C, mutant enzyme S96C/S99CY102C
1.83
NADP+
pH 9.0, 35°, wild-type enzyme
2 - 8
NADP+
pH 9.0, 35°C, mutant enzyme D207A/I208R
3.27
NADP+
pH 7.0, 30°C, native enzyme, with xylitol
4.67
NADP+
pH 9.0, 35°C, mutant enzyme N211R
5.7
NADP+
pH 9.0, 35°C, mutant enzyme D207A
6.17
NADP+
pH 9.0, 35°C, mutant enzyme D207A/I208R/F209Y
8
NADP+
pH 9.0, 35°C, mutant enzyme D207A/F209S
9.83
NADP+
pH 9.0, 35°C, mutant enzyme F209S
10
NADP+
pH 9.0, 35°C, mutant enzyme I208R
32.83
NADP+
pH 9.0, 35°C, mutant enzyme D207A/I208R/F209T
41.7
NADP+
pH 9.0, 35°C, mutant enzyme D207A/I208R/F209S
64
NADP+
pH 9.0, 35°C, mutant enzyme D207A/I208R/F209S/N211R
183.3
NADP+
pH 9.0, 35°C, mutant enzym S96C/S99C/Y102C/D207A/I208R/F209S/N211R
210
NADP+
pH 9.0, 35°C, mutant enzyme S96C/S99C/Y102C/D207A/I208R/F209S
4.48
ribitol
pH 7.0, 30°C, native enzyme
4.5
ribitol
at pH 7.0 and 30°C
1.19
sorbitol
-
mutant E154C
1.12
xylitol
recombinant enzyme, pH 7.0, 30°C
2 - 3.7
xylitol
recombinant mutant D205A/I206R, pH 9.0, 35°C, with NAD+
11.1
xylitol
recombinant wild-type enzyme, pH 9.0, 35°C, with NAD+
13.28
xylitol
pH 7.0, 30°C, recombinant enzyme
15.015
xylitol
pH 7.0, 30°C, recombinant enzyme
17.9
xylitol
pH 7.0, cofactor: NADP+mutant enzyme D38S/M39R
18
xylitol
at pH 7.0 and 30°C
18
xylitol
pH 7.0, 30°C, native enzyme
19.62
xylitol
pH 7.0, 30°C, recombinant enzyme
19.7
xylitol
recombinant mutant D205A, pH 9.0, 35°C, with NAD+
24.6
xylitol
pH 7.0, cofactor: NAD+, wild-type enzyme
143
xylitol
-
25°C, pH 7.5, Tris-HCl
170
xylitol
-
25°C, pH 7.5, potassium phosphate
2115
xylitol
35°C, pH 7.5, recombinant enzyme
2644
xylitol
35°C, pH 7.5, native enzyme
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