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D-arabitol + NAD+
?
-
-
-
-
?
D-arabitol + NAD+
? + NADH + H+
D-fructose + NADH + H+
D-sorbitol + NAD+
D-fructose + NADH + H+
sorbitol + NAD+
D-mannitol + NAD+
? + NADH + H+
8% of the activity with xylitol
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
D-ribitol + NAD+
D-ribulose + NADH
D-ribulose + NADH
D-ribitol + NAD+
-
-
-
r
D-ribulose + NADH + H+
?
-
-
-
?
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+
-
low activity
-
-
r
D-xylitol + NAD+
D-xylulose + NADH + H+
D-xylulose + NAD+
xylitol + NADH + H+
-
-
-
-
r
D-xylulose + NADH + H+
D-xylitol + NAD+
D-xylulose + NADH + H+
xylitol + NAD+
dihydroxyacetone + NADH
glycerol + NAD+
-
-
-
-
?
erythritol + NAD+
? + NADH + H+
0.77% of the activity with xylitol
-
-
?
erythritol + NAD+
L-erythrulose + NADH
-
-
-
r
galactitol + NAD+
? + NADH + H+
0.98% of the activity with xylitol
-
-
?
glycerol + NAD+
glycerone + NADH + H+
L-arabinitol + NAD+
? + NADH + H+
21% of the activity with xylitol
-
-
?
L-arabitol + NAD+
L-xylulose + NADH + H+
L-erythrulose + NADH
erythritol + NAD+
L-iditol + NAD+
?
-
-
-
-
?
L-sorbose + NADH + H+
?
-
-
-
?
L-threitol + NAD+
? + NADH + H+
L-xylulose + NADH
L-xylitol + NAD+
-
-
-
-
?
meso-erythritol + NAD+
? + NADH + H+
ribitol + NAD+
? + NADH + H+
40% of the activity with xylitol
-
-
?
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+
-
-
-
-
r
D-arabitol + NAD+
? + NADH + H+
-
-
-
-
r
D-fructose + NADH + H+
D-sorbitol + NAD+
-
-
-
-
?
D-fructose + NADH + H+
D-sorbitol + NAD+
-
-
-
r
D-fructose + NADH + H+
sorbitol + NAD+
-
46.4% activity compared to D-xylulose
-
-
r
D-fructose + NADH + H+
sorbitol + NAD+
-
46.4% activity compared to D-xylulose
-
-
r
D-iditol + NAD+
?
-
11.2% of the activity with xylitol
-
-
?
D-iditol + NAD+
?
-
11.2% of the activity with xylitol
-
-
?
D-mannitol + NAD+
?
-
16.1% activity compared to xylitol
-
-
?
D-mannitol + NAD+
?
-
16.1% activity compared to xylitol
-
-
?
D-mannitol + NAD+
?
2.6% activity compared to xylitol
-
-
?
D-mannitol + NAD+
?
2.6% activity compared to xylitol
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
-
r
D-mannitol + NAD+
D-fructose + NADH + H+
low activity compared to xylitol
-
-
r
D-mannitol + NAD+
D-fructose + NADH + H+
-
low activity, reaction of EC 1.1.1.67
-
-
r
D-mannitol + NAD+
D-fructose + NADH + H+
low activity compared to xylitol
-
-
r
D-mannitol + NAD+
D-fructose + NADH + H+
-
-
-
-
r
D-mannitol + NAD+
D-fructose + NADH + H+
-
low activity, reaction of EC 1.1.1.67
-
-
r
D-ribitol + NAD+
D-ribulose + NADH
-
-
-
-
?
D-ribitol + NAD+
D-ribulose + NADH
-
-
-
-
?
D-ribitol + NAD+
D-ribulose + NADH
-
-
-
?
D-ribitol + NAD+
D-ribulose + NADH
-
-
-
-
?
D-ribitol + NAD+
D-ribulose + NADH
-
85% of the rate of xylitol oxidation
-
-
?
D-ribitol + NAD+
D-ribulose + NADH
-
-
-
-
?
D-ribitol + NAD+
D-ribulose + NADH
-
-
-
-
r
D-ribitol + NAD+
D-ribulose + NADH
-
oxidation at 11% of the rate of xylitol oxidation
-
-
?
D-sorbitol + NAD+
? + NADH + H+
-
-
-
?
D-sorbitol + NAD+
? + NADH + H+
-
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
-
-
ir
D-sorbitol + NAD+
D-fructose + NADH + H+
-
-
-
-
r
D-sorbitol + NAD+
D-fructose + NADH + H+
-
-
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
-
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
69% of activity against D-xylitol
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
-
-
-
r
D-sorbitol + NAD+
D-fructose + NADH + H+
-
-
-
-
r
D-sorbitol + NAD+
D-fructose + NADH + H+
-
-
-
r
D-sorbitol + NAD+
D-fructose + NADH + H+
-
-
-
-
r
D-sorbitol + NAD+
D-fructose + NADH + H+
-
-
-
r
D-sorbitol + NAD+
D-fructose + NADH + H+
-
-
-
-
r
D-sorbitol + NAD+
D-fructose + NADH + H+
-
rate of xylitol oxidation at 67%
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
-
-
-
r
D-sorbitol + NAD+
D-fructose + NADH + H+
-
rate of xylitol oxidation at 95%
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
rate of xylitol oxidation at 56%
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
90% of the activity with xylitol
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
71.8% activity compared to xylitol
-
-
r
D-sorbitol + NAD+
D-fructose + NADH + H+
71.8% activity compared to xylitol
-
-
r
D-sorbitol + NAD+
D-fructose + NADH + H+
-
oxidation at about 45%
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
-
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
rate of xylitol oxidation at 118%
-
-
?
D-sorbitol + NAD+
L-sorbose + NADH + H+
-
-
-
-
r
D-sorbitol + NAD+
L-sorbose + NADH + H+
51.3% increased activity compared to xylitol
-
-
?
D-sorbitol + NAD+
L-sorbose + NADH + H+
51.3% increased activity compared to xylitol
-
-
?
D-sorbitol + NAD+
L-sorbose + NADH + H+
-
-
-
-
r
D-sorbitol + NAD+
L-sorbose + NADH + H+
71.8% activity compared to xylitol
-
-
?
D-sorbitol + NAD+
L-sorbose + NADH + H+
71.8% activity compared to xylitol
-
-
?
D-threitol + NAD+
?
-
109% of the activity with xylitol
-
-
?
D-threitol + NAD+
?
-
109% of the activity with xylitol
-
-
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
r
D-xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
r
D-xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
?
D-xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
?
D-xylulose + NADH + H+
D-xylitol + NAD+
-
specific for transferring the 4-pro-R hydrogen of NADH
-
-
r
D-xylulose + NADH + H+
D-xylitol + NAD+
-
-
-
-
r
D-xylulose + NADH + H+
D-xylitol + NAD+
-
-
-
-
?
D-xylulose + NADH + H+
xylitol + NAD+
-
-
-
r
D-xylulose + NADH + H+
xylitol + NAD+
-
-
-
r
D-xylulose + NADH + H+
xylitol + NAD+
-
100% activity
-
-
r
D-xylulose + NADH + H+
xylitol + NAD+
-
100% activity
-
-
r
D-xylulose + NADH + H+
xylitol + NAD+
-
-
-
r
D-xylulose + NADH + H+
xylitol + NAD+
-
-
-
r
D-xylulose + NADH + H+
xylitol + NAD+
-
-
-
r
D-xylulose + NADH + H+
xylitol + NAD+
-
-
-
r
D-xylulose + NADH + H+
xylitol + NAD+
-
-
-
r
D-xylulose + NADH + H+
xylitol + NAD+
-
-
-
-
r
D-xylulose + NADH + H+
xylitol + NAD+
-
-
-
r
D-xylulose + NADH + H+
xylitol + NAD+
-
-
-
-
r
D-xylulose + NADH + H+
xylitol + NAD+
-
-
-
r
D-xylulose + NADH + H+
xylitol + NAD+
-
-
-
r
D-xylulose + NADH + H+
xylitol + NAD+
-
-
-
r
D-xylulose + NADH + H+
xylitol + NAD+
-
-
-
r
D-xylulose + NADH + H+
xylitol + NAD+
-
-
-
r
D-xylulose + NADH + H+
xylitol + NAD+
-
-
-
r
D-xylulose + NADH + H+
xylitol + NAD+
-
-
-
r
glycerol + NAD+
?
-
-
-
-
?
glycerol + NAD+
?
-
poor substrate
-
-
?
glycerol + NAD+
glycerone + NADH + H+
-
low activity
-
-
r
glycerol + NAD+
glycerone + NADH + H+
-
low activity
-
-
r
L-arabitol + NAD+
?
-
-
-
-
?
L-arabitol + NAD+
?
-
-
-
-
?
L-arabitol + NAD+
L-xylulose + NADH + H+
the enzyme also has L-arabitol dehydrogenase activity (20.1% activity compared to xylitol)
-
-
?
L-arabitol + NAD+
L-xylulose + NADH + H+
about 20% activity compared to xylitol, reaction of EC 1.1.1.12
-
-
r
L-arabitol + NAD+
L-xylulose + NADH + H+
the enzyme also has L-arabitol dehydrogenase activity (20.1% activity compared to xylitol)
-
-
?
L-arabitol + NAD+
L-xylulose + NADH + H+
about 20% activity compared to xylitol, reaction of EC 1.1.1.12
-
-
r
L-erythrulose + NADH
erythritol + NAD+
-
reduction at the same rate as D-xylulose
-
-
?
L-erythrulose + NADH
erythritol + NAD+
-
-
-
r
L-threitol + NAD+
? + NADH + H+
0.05% of the activity with xylitol
-
-
?
L-threitol + NAD+
? + NADH + H+
75% of the activity with xylitol
-
-
?
meso-erythritol + NAD+
? + NADH + H+
-
-
-
-
r
meso-erythritol + NAD+
? + NADH + H+
-
-
-
-
r
ribitol + NAD+
?
-
-
-
?
ribitol + NAD+
?
60.1% activity compared to xylitol
-
-
?
ribitol + NAD+
D-ribulose + NADH + H+
-
-
-
r
ribitol + NAD+
D-ribulose + NADH + H+
reaction of EC 1.1.1.56, ribitol 2-dehydrogenase
-
-
?
ribitol + NAD+
D-ribulose + NADH + H+
reaction of EC 1.1.1.56, ribitol 2-dehydrogenase
-
-
?
ribitol + NAD+
D-ribulose + NADH + H+
60.1% activity compared to xylitol
-
-
?
ribitol + NAD+
D-ribulose + NADH + H+
60.1% activity compared to xylitol
-
-
?
sorbitol + NAD+
D-fructose + NADH + H+
-
-
-
-
?
sorbitol + NAD+
D-fructose + NADH + H+
-
153.9% activity compared to xylitol
-
-
r
sorbitol + NAD+
D-fructose + NADH + H+
-
153.9% activity compared to xylitol
-
-
r
Xylitol + NAD+
?
-
-
-
-
?
Xylitol + NAD+
?
-
-
-
-
?
Xylitol + NAD+
?
-
-
-
-
?
Xylitol + NAD+
?
-
inducible pathway of xylose catabolism
-
-
r
Xylitol + NAD+
?
-
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
key enzyme in D-xylose metabolism
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
?, r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
100% activity
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
100% activity
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
?, r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
preferred substrate
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
preferred substrates
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
preferred substrate
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
preferred substrates
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
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
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
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
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
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
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
best substrate
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
100% activity
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
100% activity
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
best substrate
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
?
xylitol + NAD+
L-xylulose + NADH + H+
-
-
-
-
?
xylitol + NAD+
L-xylulose + NADH + H+
-
-
-
-
?
xylitol + NAD+
L-xylulose + NADH + H+
-
-
-
?
xylitol + NADP+
D-xylulose + NADPH + H+
wild-type enzyme shows no activity with NADP+, mutant enzyme D38S/M39R is able to exclusively use NADP+, with no loss of activity
-
-
?
xylitol + NADP+
D-xylulose + NADPH + H+
very low activity with NADP+
-
-
r
xylitol + NADP+
D-xylulose + NADPH + H+
mutant enzyme D205A/I260R shows activity with NADP+
-
-
r
xylitol + NADP+
D-xylulose + NADPH + H+
-
-
-
-
?
xylitol + NADP+
D-xylulose + NADPH + H+
-
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
specific for NAD+
-
-
?
additional information
?
-
-
specific for transferring the 4-pro-R hydrogen of NADH
-
-
?
additional information
?
-
-
specific for NAD+
-
-
?
additional information
?
-
-
specific for NAD+
-
-
?
additional information
?
-
-
no reduction of D-ribose and D-galacturonic acid
-
-
?
additional information
?
-
-
no oxidation of threitol, xylitol, sorbitol, D-iditol
-
-
?
additional information
?
-
-
no reduction of D-ribulose
-
-
?
additional information
?
-
-
no reduction of D/L-xylose
-
-
?
additional information
?
-
-
no substrate: glycerol
-
-
?
additional information
?
-
enzyme XDH depends exclusively on NAD+/NADH as cofactors
-
-
?
additional information
?
-
-
enzyme XDH depends exclusively on NAD+/NADH as cofactors
-
-
?
additional information
?
-
-
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
-
-
-
additional information
?
-
enzyme XDH depends exclusively on NAD+/NADH as cofactors
-
-
?
additional information
?
-
-
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
-
-
-
additional information
?
-
-
no oxidation of threitol, xylitol, sorbitol, D-iditol
-
-
?
additional information
?
-
-
no reduction of D-fructose, L-sorbose and D-tagatose
-
-
?
additional information
?
-
-
specific for polyols of 5 or less carbon bearing cis-hydroxy groups in C2 and C3
-
-
?
additional information
?
-
-
specific for NAD+
-
-
?
additional information
?
-
-
specific for NAD+
-
-
?
additional information
?
-
-
no activity with D-mannitol, erythritol, and D-arabitol. Very low activity with NADP+
-
-
?
additional information
?
-
no activity with D-mannitol, erythritol, and D-arabitol. Very low activity with NADP+
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
no activity with D-mannitol, erythritol, and D-arabitol. Very low activity with NADP+
-
-
?
additional information
?
-
no activity with D-mannitol, erythritol, and D-arabitol. Very low activity with NADP+
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
specific for NAD+
-
-
?
additional information
?
-
-
glucose:xylose ratio of 1:2.5 promotes a 2.7fold increase in activity when compared to a glucose:xylose ratio of 1:25
-
-
?
additional information
?
-
-
specific for NAD+
-
-
?
additional information
?
-
-
no reduction of D/L-xylose
-
-
?
additional information
?
-
-
no reduction of L-xylulose
-
-
?
additional information
?
-
-
no oxidation of ribitol
-
-
?
additional information
?
-
-
no oxidation of inositol, meso-erythritol and D-(+)-arabitol
-
-
?
additional information
?
-
-
no oxidation of mannitol
-
-
?
additional information
?
-
-
specific for NAD+
-
-
?
additional information
?
-
-
no reduction of D/L-xylose
-
-
?
additional information
?
-
-
no reduction of L-xylulose
-
-
?
additional information
?
-
-
no oxidation of ribitol
-
-
?
additional information
?
-
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+
-
-
?
additional information
?
-
-
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+
-
-
?
additional information
?
-
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+
-
-
?
additional information
?
-
-
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+
-
-
?
additional information
?
-
-
investigation of limiting metabolic steps in the utilization of xylose by recombinant Saccharomyces cerevisiae using metabolic engineering
-
-
?
additional information
?
-
-
no oxidation of ribitol
-
-
?
additional information
?
-
-
no oxidation of mannitol
-
-
?
additional information
?
-
-
specific for NAD+
-
-
?
additional information
?
-
-
specific for NAD+
-
-
?
additional information
?
-
-
specific for NAD+
-
-
?
additional information
?
-
-
no reduction of D/L-xylose
-
-
?
additional information
?
-
-
no reduction of L-xylulose
-
-
?
additional information
?
-
-
no oxidation of ribitol
-
-
?
additional information
?
-
-
specific for NAD+
-
-
?
additional information
?
-
-
specific for NAD+
-
-
?
additional information
?
-
-
specific for NAD+
-
-
?
additional information
?
-
-
specific for NAD+
-
-
?
additional information
?
-
-
specific for NAD+
-
-
?
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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
-
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evolution
the enzyme belongs to a medium-chain dehydrogenase/reductase (MDR) superfamily and a subfamily of polyol dehydrogenase, PDH
evolution
the conserved coenzyme binding motif (GxGxxG) and zinc-ADH signature (GHExxGxxxxxGxxV) are observed in the amino acid sequence of RpXDH at position 181-186 and 70-84 and are completely conserved among RpXDH, XDHs, and SDHs from other filamentous fungi and yeasts
evolution
XDH has a TGXXGXXG NAD(H)-binding motif and a YXXXK active site motif, and belongs to the short-chain dehydrogenase/ reductase family
evolution
the enzyme belongs to the medium-chain dehydrogenase/reductase (MDR) superfamily and polyol dehydrogenase (PDH) subfamily. The enzyme contains the typical NAD+-binding motif GxGxxG of MDR family enzymes
evolution
-
the enzyme contains a NAD(P)-binding motif and a classical active site motif belonging to the short-chain dehydrogenase family
evolution
-
the enzyme belongs to a medium-chain dehydrogenase/reductase (MDR) superfamily and a subfamily of polyol dehydrogenase, PDH
-
evolution
-
the enzyme belongs to the medium-chain dehydrogenase/reductase (MDR) superfamily and polyol dehydrogenase (PDH) subfamily. The enzyme contains the typical NAD+-binding motif GxGxxG of MDR family enzymes
-
evolution
-
the conserved coenzyme binding motif (GxGxxG) and zinc-ADH signature (GHExxGxxxxxGxxV) are observed in the amino acid sequence of RpXDH at position 181-186 and 70-84 and are completely conserved among RpXDH, XDHs, and SDHs from other filamentous fungi and yeasts
-
evolution
-
the enzyme contains a NAD(P)-binding motif and a classical active site motif belonging to the short-chain dehydrogenase family
-
evolution
-
XDH has a TGXXGXXG NAD(H)-binding motif and a YXXXK active site motif, and belongs to the short-chain dehydrogenase/ reductase family
-
malfunction
deletin of gene xdhA and gene ladA and or both lead mutants with decreased dehydrogenase activities and increased xylitol production, overview
malfunction
-
deletin of gene xdhA and gene ladA and or both lead mutants with decreased dehydrogenase activities and increased xylitol production, overview
-
metabolism
-
key enzymes for xylitol production in yeasts are xylose reductase and xylitol dehydrogenase, overview
metabolism
-
bioproduction pathway of xylitol, overview
metabolism
the redox balance between xylose reductase (XR) and xylitol dehydrogenase (XDH) is thought to be an important factor in effective xylose fermentation
metabolism
-
in order to overcome xylitol accumulation in Aspergillus carbonarius, a K274R point mutation is introduced into the xylose reductase with the aim of changing the specificity toward NADH. Fermentation with the mutant strain (grown on D-xylose as the sole carbon source) shows a 2.8fold reduction in xylitol accumulation and 4.5fold increase in citric acid production compared to the wild-type strain. The fact that the mutant strain shows decreased xylitol levels is assumed to be associated with the capability of the mutated xylose reductase to use NADH generated by the xylitol dehydrogenase XDH, thus preventing the inhibition of XDH by the high levels of NADH and ensuring the flux of D-xylose through the pathway
metabolism
-
the cofactor imbalance between the NAD(P)H-dependent wild type XR and NAD+-dependent XDH can create an intracellular redox imbalance, leading to an accumulation of NADH and a shortage of NAD+ necessary for the XDH reaction. The likely increase in intracellular xylitol concentration favors xylitol excretion, which reduces the ethanol yield by Saccharomyces cerevisiae
metabolism
xylitol dehydrogenase catalyzes the second step of D-xylose metabolism
metabolism
biosynthesis of xylitol can be achieved from two distinctive routes, one occurs via the activity of NADPH-dependent xylose reductase (XR, EC 1.1.1.307), reducing xylose directly into xylitol. The other one proceeds via formation of the intermediate xylulose through xylose isomerase (XI, EC 5.3.1.5) followed by NADH-dependent reduction via the xylitol dehydrogenase (XDH). Both of the metabolic routes originate from xylose dissimilation and can lead to formation of xylulose-5-phosphtate, the entrance point of pentose phosphate pathway
metabolism
one xylose-assimilating pathway consists of xylose reductase (XR, XYL1) and xylitol dehydrogenase (XDH, XYL2, EC 1.1.1.9) from Scheffersomyces stipitis. XR reduces xylose to xylitol by using NAD(P)H as cofactor and XDH further oxidizes xylitol to xylulose using NAD+. While the XR-XDH pathway can offer higher metabolic fluxes than the xylose isomerase (XI) pathway, it accumulates xylitol which is produced due to cofactor imbalance caused by different cofactor requirement between XR and XDH
metabolism
-
xylitol dehydrogenase catalyzes the second step of D-xylose metabolism
-
metabolism
-
in order to overcome xylitol accumulation in Aspergillus carbonarius, a K274R point mutation is introduced into the xylose reductase with the aim of changing the specificity toward NADH. Fermentation with the mutant strain (grown on D-xylose as the sole carbon source) shows a 2.8fold reduction in xylitol accumulation and 4.5fold increase in citric acid production compared to the wild-type strain. The fact that the mutant strain shows decreased xylitol levels is assumed to be associated with the capability of the mutated xylose reductase to use NADH generated by the xylitol dehydrogenase XDH, thus preventing the inhibition of XDH by the high levels of NADH and ensuring the flux of D-xylose through the pathway
-
metabolism
-
one xylose-assimilating pathway consists of xylose reductase (XR, XYL1) and xylitol dehydrogenase (XDH, XYL2, EC 1.1.1.9) from Scheffersomyces stipitis. XR reduces xylose to xylitol by using NAD(P)H as cofactor and XDH further oxidizes xylitol to xylulose using NAD+. While the XR-XDH pathway can offer higher metabolic fluxes than the xylose isomerase (XI) pathway, it accumulates xylitol which is produced due to cofactor imbalance caused by different cofactor requirement between XR and XDH
-
metabolism
-
biosynthesis of xylitol can be achieved from two distinctive routes, one occurs via the activity of NADPH-dependent xylose reductase (XR, EC 1.1.1.307), reducing xylose directly into xylitol. The other one proceeds via formation of the intermediate xylulose through xylose isomerase (XI, EC 5.3.1.5) followed by NADH-dependent reduction via the xylitol dehydrogenase (XDH). Both of the metabolic routes originate from xylose dissimilation and can lead to formation of xylulose-5-phosphtate, the entrance point of pentose phosphate pathway
-
metabolism
-
one xylose-assimilating pathway consists of xylose reductase (XR, XYL1) and xylitol dehydrogenase (XDH, XYL2, EC 1.1.1.9) from Scheffersomyces stipitis. XR reduces xylose to xylitol by using NAD(P)H as cofactor and XDH further oxidizes xylitol to xylulose using NAD+. While the XR-XDH pathway can offer higher metabolic fluxes than the xylose isomerase (XI) pathway, it accumulates xylitol which is produced due to cofactor imbalance caused by different cofactor requirement between XR and XDH
-
metabolism
-
biosynthesis of xylitol can be achieved from two distinctive routes, one occurs via the activity of NADPH-dependent xylose reductase (XR, EC 1.1.1.307), reducing xylose directly into xylitol. The other one proceeds via formation of the intermediate xylulose through xylose isomerase (XI, EC 5.3.1.5) followed by NADH-dependent reduction via the xylitol dehydrogenase (XDH). Both of the metabolic routes originate from xylose dissimilation and can lead to formation of xylulose-5-phosphtate, the entrance point of pentose phosphate pathway
-
metabolism
-
one xylose-assimilating pathway consists of xylose reductase (XR, XYL1) and xylitol dehydrogenase (XDH, XYL2, EC 1.1.1.9) from Scheffersomyces stipitis. XR reduces xylose to xylitol by using NAD(P)H as cofactor and XDH further oxidizes xylitol to xylulose using NAD+. While the XR-XDH pathway can offer higher metabolic fluxes than the xylose isomerase (XI) pathway, it accumulates xylitol which is produced due to cofactor imbalance caused by different cofactor requirement between XR and XDH
-
metabolism
-
biosynthesis of xylitol can be achieved from two distinctive routes, one occurs via the activity of NADPH-dependent xylose reductase (XR, EC 1.1.1.307), reducing xylose directly into xylitol. The other one proceeds via formation of the intermediate xylulose through xylose isomerase (XI, EC 5.3.1.5) followed by NADH-dependent reduction via the xylitol dehydrogenase (XDH). Both of the metabolic routes originate from xylose dissimilation and can lead to formation of xylulose-5-phosphtate, the entrance point of pentose phosphate pathway
-
metabolism
-
bioproduction pathway of xylitol, overview
-
physiological function
strictly NADPH-dependent XR with mutated strict NADP+-dependent XDH are more effective in increasing bioethanol production and decreasing xylitol accumulation than the NAD+-dependent wild-type XDH, overview
physiological function
enzyme XDH depends exclusively on NAD+/NADH as cofactors with a relatively low activity directly limiting the overall conversion process of D-xylose fermentation to ethanol by Gluconobacter oxydans
physiological function
the organism catabolizes L-arabinose as well as D-glucose and D-xylose. The highest production amounts of ethanol from D-glucose, xylitol from D-xylose, and L-arabitol from L-arabinose were 0.45 g/g D-glucose, 0.60 g/g D-xylose, and 0.61 g/g L-arabinose with 21.7 g/l ethanol, 20.2 g/l xylitol, and 30.3 g/l L-arabitol, respectively. The enzyme has L-arabitol dehydrogenase (LAD) activity and also exhibits broad specificity to polyols, such as xylitol, D-sorbitol, ribitol, and L-arabitol. Xylitol is the preferred substrate
physiological function
-
the organism catabolizes L-arabinose as well as D-glucose and D-xylose. The highest production amounts of ethanol from D-glucose, xylitol from D-xylose, and L-arabitol from L-arabinose were 0.45 g/g D-glucose, 0.60 g/g D-xylose, and 0.61 g/g L-arabinose with 21.7 g/l ethanol, 20.2 g/l xylitol, and 30.3 g/l L-arabitol, respectively. The enzyme has L-arabitol dehydrogenase (LAD) activity and also exhibits broad specificity to polyols, such as xylitol, D-sorbitol, ribitol, and L-arabitol. Xylitol is the preferred substrate
-
physiological function
-
enzyme XDH depends exclusively on NAD+/NADH as cofactors with a relatively low activity directly limiting the overall conversion process of D-xylose fermentation to ethanol by Gluconobacter oxydans
-
additional information
-
XDH depends exclusively on NAD+/NADH as cofactors with a relatively low activity limiting the the overall conversion process, improvement by recombinant expression of enzyme and glucose dehydrogenase cofactor regeneration enzyme
additional information
-
xylitol production of wild-type and mutant strains, overview
additional information
xylitol production of wild-type and mutant strains, overview
additional information
xylitol production of wild-type and mutant strains, overview
additional information
-
xylitol production of wild-type and mutant strains, overview
additional information
enzyme IoXyl2p ahs the conserved domain GxGxxG (Gly188-Gly190-Gly193 in IoXyl2p) for cofactor binding
additional information
-
enzyme IoXyl2p ahs the conserved domain GxGxxG (Gly188-Gly190-Gly193 in IoXyl2p) for cofactor binding
additional information
enzyme TdXyl2p has the conserved domain GxGxxG (Gly176-Gly178-Gly181 in TdXyl2p) for cofactor binding
additional information
-
enzyme TdXyl2p has the conserved domain GxGxxG (Gly176-Gly178-Gly181 in TdXyl2p) for cofactor binding
additional information
-
xylitol production of wild-type and mutant strains, overview
-
additional information
-
xylitol production of wild-type and mutant strains, overview
-
additional information
-
enzyme IoXyl2p ahs the conserved domain GxGxxG (Gly188-Gly190-Gly193 in IoXyl2p) for cofactor binding
-
additional information
-
enzyme TdXyl2p has the conserved domain GxGxxG (Gly176-Gly178-Gly181 in TdXyl2p) for cofactor binding
-
additional information
-
XDH depends exclusively on NAD+/NADH as cofactors with a relatively low activity limiting the the overall conversion process, improvement by recombinant expression of enzyme and glucose dehydrogenase cofactor regeneration enzyme
-
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D202A/L203R/V204S/E205P/S206R
-
site-directed mutagenesis, introduction of multiple site-directed mutations in the coenzyme-binding pocket of Galactocandida mastotermitis XDH to enable activity with NADP+, which is lacking in the wild-type enzyme, genetic metabolic engineering for improvement of xylose metabolism and fermentation in wild-type Saccharomyces cerevisiae strains, which are not able to naturally metabolize D-xylulose, overview
E154C
-
mutant bearing a disrupted Zn2+ binding site: purified preparations show a variable Zn2+ (0.10-0.40 atom/subunit), mutant exhibits a constant catalytic Zn2+ centre activity and does not require exogenous Zn2+ for activity or stability. E154C retains 0.019% and 0.74% of wild-type catalytic efficiency (kcat/Km (sorbitol): 7800/Msec and kcat:161/sec) for NAD+-dependent oxidation of sorbitol at 25°C respectively. The pH profile of kcat/Ksorbitol for E154C decreases below an apparent pK of 9.1, reflecting a shift in pK by about +1.7-1.9 pH units compared with the corresponding pH profiles for wild-type. IC50 (ZnSO4): 0.005 mM
synthesis
-
use of enzyme in a process for producing xylitol from D-glucose
D38S/M39R
the mutant enzyme is able to exclusively use NADP+, with no loss of activity
D205A
site-directed mutagenesis, coenzyme preference of the mutant RpXDH is partially reversed from NAD+ to NADP+
D205A
-
site-directed mutagenesis, coenzyme preference of the mutant RpXDH is partially reversed from NAD+ to NADP+
-
D207A
kcat/Km for NAD+ is 3.6fold lower than wild-type value, kcat/Km for NADP+ is 4.3fold higher than wild-type value
D207A/F209S
kcat/Km for NAD+ is 2.2fold lower than wild-type value, kcat/Km for NADP+ is 745fold higher than wild-type value
D207A/I208R
kcat/Km for NAD+ is 2.5fold lower than wild-type value, kcat/Km for NADP+ is 229fold higher than wild-type value
D207A/I208R/F209S/N211R
kcat/Km for NAD+ is 32.9fold lower than wild-type value, kcat/Km for NADP+ is 4292fold higher than wild-type value, increased thermostability
D207A/I208R/F209T
kcat/Km for NAD+ is 2.4fold lower than wild-type value, kcat/Km for NADP+ is 4754fold higher than wild-type value
D207A/I208R/F209Y
kcat/Km for NAD+ is 6.9fold lowerthan wild-type value, kcat/Km for NADP+ is 788fold higher than wild-type value
F209S
kcat/Km for NAD+ is 1.9fold lower than wild-type value, kcat/Km for NADP+ is 31.4fold higher than wild-type value
I208R
kcat/Km for NAD+ is nearly identical to wild-type value, kcat/Km for NADP+ is 44fold higher than wild-type value
I208R/F209S
kcat/Km for NAD+ is 30.7fold lower than wild-type value, kcat/Km for NADP+ is 1.5fold higher than wild-type value
N211R
kcat/Km for NAD+ is 1.1fold lower than wild-type value, kcat/Km for NADP+ is 7.6fold higher than wild-type value
S96C/S99C/Y102C
-
specific activity (U/min): 1440, half denaturation temperature T1/2 (°C): 46.1, thermal transition temperature Tcd (°C): 47.5
S96C/S99C/Y102C/D207A/I208R/F209S
S96C/S99C/Y102C/D207A/I208R/F209S/N211R
kcat/Km for NAD+ is 26.5fold lower than wild-type value, kcat/Km for NADP+ is 16154fold higher than wild-type value
S96C/S99C/Y102C/E101F
-
specific activity (U/min): 1550, half denaturation temperature T1/2 (°C): 50.9, thermal transition temperature Tcd (°C): 50.5
S96C/S99C/Y102C/F98R
-
specific activity (U/min): 1510, half denaturation temperature T1/2 (°C): 53.1, thermal transition temperature Tcd (°C): 51.7
S96C/S99C/Y102C/F98R/E101F
-
specific activity (U/min): 1620, half denaturation temperature T1/2 (°C): 56.0, thermal transition temperature Tcd (°C): 53.8
S96C/S99C/Y102C/H112D
-
specific activity (U/min): 1360, half denaturation temperature T1/2 (°C): 44.0, thermal transition temperature Tcd (°C): 47.0
S96C/S99C/Y102C/P95S
-
specific activity (U/min): 1220, half denaturation temperature T1/2 (°C): 37.4, thermal transition temperature Tcd (°C): 43.5
S96C/S99CY102C
kcat/Km for NAD+ is 1.1fold lower than wild-type value, kcat/Km for NADP+ is 8.8fold higher than wild-type value
D205A/I206R
the mutant shows cofactor preference for NADP+
D205A/I206R
site-directed mutagenesis, coenzyme preference of the mutant RpXDH is reversed from NAD+ to NADP+
D205A/I206R
-
the mutant shows cofactor preference for NADP+
-
D205A/I206R
-
site-directed mutagenesis, coenzyme preference of the mutant RpXDH is reversed from NAD+ to NADP+
-
D207A/I208R/F209S
kcat/Km for NAD+ is 15.2fold lower than wild-type value, kcat/Km for NADP+ is 4292fold higher than wild-type value, increased thermostability
D207A/I208R/F209S
-
mutant bearing a reversal of coenzyme specificity from NAD+ to NADP+ is introduced into Saccharomyces cerevisiae. kcat/Km (NAD+): 181 l/min/mmol, kcat/Km (NADP+): 2790 l/min/mmol, Km (xylitol in the presence of NAD+): 31.1 mM, NADP+-dependent activity: 0.782 U/mg, NAD+-dependent activity: 0.271 U/mg. In xylose fermentation a large decrease in xylitol and glycerol yield is shown, while the xylose consumption and ethanol yield are decreased
S96C/S99C/Y102C/D207A/I208R/F209S
kcat/Km for NAD+ is 36.7fold lower than wild-type value, kcat/Km for NADP+ 16462is fold higher than wild-type value
S96C/S99C/Y102C/D207A/I208R/F209S
-
mutant bearing a reversal of coenzyme specificity from NAD+ to NADP+ and additional zinc-binding site for thermostability, is introduced into Saccharomyces cerevisiae. kcat/Km (NADP+): 10700 l/min/mmol, Km (xylitol in the presence of NAD+): 111 mM , NADP+-dependent activity: 0.689 U/mg, NAD+-dependent activity: 0.136 U/mg. The xylose consumption and ethanol yield are decreased, and the xylitol yield is increased, because of low XDH activity
additional information
-
generation of xdhA and ladA deletion mutants and double-deletion mutant, that show decreased dehydrogenase activities and increased xylitol production from D-xylose compared to the KBN616 wild-type strain, overview
additional information
generation of xdhA and ladA deletion mutants and double-deletion mutant, that show decreased dehydrogenase activities and increased xylitol production from D-xylose compared to the KBN616 wild-type strain, overview
additional information
-
construction of deletion mutants of xdhA and ladA-xdhA, to generate mutants with decreased dehydrogenase activities and increased xylitol production. Genomic DNA from Aspergillus oryzae strain KBN616 is used as the template for amplification of the three xdhA and ladA inserts. Activities of xylitol dehydrogenase and xylose reductase in the mutant strains, phenotype, overview
additional information
construction of deletion mutants of xdhA and ladA-xdhA, to generate mutants with decreased dehydrogenase activities and increased xylitol production. Genomic DNA from Aspergillus oryzae strain KBN616 is used as the template for amplification of the three xdhA and ladA inserts. Activities of xylitol dehydrogenase and xylose reductase in the mutant strains, phenotype, overview
additional information
construction of deletion mutants of xdhA by homologous transformation, to generate mutants with decreased dehydrogenase activities and increased xylitol production. Gene pyrG is used as a selectable marker. Consumption of D-xylose for xdhA2-1 and ladA2-1 is similar to that of KBN616. Mutant xdhA2-1 displays the highest xylitol productivity. XdhA-disrupted mutant xdhA2-1 exhibits the highest xylitol productivity from D-xylose and is selected for further production of xylitol from oat spelt xylan
additional information
-
construction of deletion mutants of xdhA by homologous transformation, to generate mutants with decreased dehydrogenase activities and increased xylitol production. Gene pyrG is used as a selectable marker. Consumption of D-xylose for xdhA2-1 and ladA2-1 is similar to that of KBN616. Mutant xdhA2-1 displays the highest xylitol productivity. XdhA-disrupted mutant xdhA2-1 exhibits the highest xylitol productivity from D-xylose and is selected for further production of xylitol from oat spelt xylan
additional information
construction of xdhA gene disruption mutant xdhA2-1 by homologous transformation into Aspergillus oryzae strain P5 (DELTApyrG), and pyrG is used as a selectable marker, phenotype, overview
additional information
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construction of xdhA gene disruption mutant xdhA2-1 by homologous transformation into Aspergillus oryzae strain P5 (DELTApyrG), and pyrG is used as a selectable marker, phenotype, overview
additional information
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generation of xdhA and ladA deletion mutants and double-deletion mutant, that show decreased dehydrogenase activities and increased xylitol production from D-xylose compared to the KBN616 wild-type strain, overview
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additional information
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construction of deletion mutants of xdhA and ladA-xdhA, to generate mutants with decreased dehydrogenase activities and increased xylitol production. Genomic DNA from Aspergillus oryzae strain KBN616 is used as the template for amplification of the three xdhA and ladA inserts. Activities of xylitol dehydrogenase and xylose reductase in the mutant strains, phenotype, overview
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additional information
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construction of xdhA gene disruption mutant xdhA2-1 by homologous transformation into Aspergillus oryzae strain P5 (DELTApyrG), and pyrG is used as a selectable marker, phenotype, overview
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additional information
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construction of deletion mutants of xdhA by homologous transformation, to generate mutants with decreased dehydrogenase activities and increased xylitol production. Gene pyrG is used as a selectable marker. Consumption of D-xylose for xdhA2-1 and ladA2-1 is similar to that of KBN616. Mutant xdhA2-1 displays the highest xylitol productivity. XdhA-disrupted mutant xdhA2-1 exhibits the highest xylitol productivity from D-xylose and is selected for further production of xylitol from oat spelt xylan
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additional information
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strain overexpressing enzyme has improved xylitol productivity, production of up to 57g/l xylitol from 225 g/l D-arabitol, via D-xylulose
additional information
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to improve characteristics of xylose fermentation, the recombinant strain Delta xyl1 Delta xyl2-ADelta xyl2-B, with deletions of genes encoding first enzymes of xylose utilization (NAD(P)H-dependent xylose reductase and NAD-dependent xylitol dehydrogenases, respectively), is constructed and used as a recipient for co-overexpression of the Escherichia coli xylA gene coding for xylose isomerase and endogenous XYL3 gene coding for xylulokinase. Recombinant strains display improved ethanol production during the fermentation of xylose
additional information
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recombinant Saccharomyces cerevisiae strain TMB3057 with high activity of both xylose reductase and xylitol dehydrogenase show increased ethanol formation from xylose at the expense of xylitol formation
additional information
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coenzyme specificities of the NADPH-preferring xylose reductase, EC 1.1.1.307, and the NAD+-dependent xylitol dehydrogenase are targeted in previous studies by protein design or evolution with the aim of improving the recycling of NADH or NADPH in their two-step pathway, converting xylose to xylulose. Yeast strains expressing variant pairs of both enzymes that according to in vitro kinetic data are suggested to be much better matched in coenzyme usage than the corresponding pair of wild-type enzymes, exhibit widely varying capabilities for xylose fermentation, bi-substrate kinetic analysis, and statistical analysis, overview. Engineered strains of Saccharomyces cerevisiae have engineered forms of xylose reductase or xylose dehydrogenase and imporved performance in xylose fermentation
additional information
Saccharomyces cerevisiae, the preferred microorganism for large-scale ethanol production, does not naturally consume xylose. Xylose isomerase (XI) and xylose reductase/xylitol dehydrogenase (XR/XDH) pathways are introduced into two robust industrial Saccharomyces cerevisiae strains, PE-2DELTAGRE3 and CA11, evaluated in synthetic media and corn cob hemicellulosic hydrolysate (non-detoxified corn cob hydrolysate) and the results are correlated with the differential enzyme activities found in the xylose-pathway engineered strains, evaluation of xylose fermentation capacity in oxygen-deprived conditions at 30°C and 40°C. Regarding the CA11-derived strains, the XR activity is higher in the strain with both pathways than in the one solely expressing XR/XDH, while the XDH activity at 30°C is higher in the CA11-XR/XDH strain. The sole expression of XI increases the fermentative capacity of both strains in synthetic media at 30°C and 40°C: decreasing xylitol accumulation and improving xylose consumption and ethanol production. Similar results are observed in fermentations of detoxified hydrolysate. However, in the presence of lignocellulosic-derived inhibitors, a positive synergistic effect results from the expression of both XI and XR/XDH, possibly caused by a cofactor equilibrium between the XDH and furan detoxifying enzymes, increasing the ethanol yield by more than 38%. Advantage of using the XI from Clostridium phytofermentans to attain high ethanol productivities and yields from xylose, and the simultaneous utilization of XR/XDH and XI pathways compared to the single expression of XR/XDH or XI improves ethanol production from non-detoxified hemicellulosic hydrolysates
additional information
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Saccharomyces cerevisiae, the preferred microorganism for large-scale ethanol production, does not naturally consume xylose. Xylose isomerase (XI) and xylose reductase/xylitol dehydrogenase (XR/XDH) pathways are introduced into two robust industrial Saccharomyces cerevisiae strains, PE-2DELTAGRE3 and CA11, evaluated in synthetic media and corn cob hemicellulosic hydrolysate (non-detoxified corn cob hydrolysate) and the results are correlated with the differential enzyme activities found in the xylose-pathway engineered strains, evaluation of xylose fermentation capacity in oxygen-deprived conditions at 30°C and 40°C. Regarding the CA11-derived strains, the XR activity is higher in the strain with both pathways than in the one solely expressing XR/XDH, while the XDH activity at 30°C is higher in the CA11-XR/XDH strain. The sole expression of XI increases the fermentative capacity of both strains in synthetic media at 30°C and 40°C: decreasing xylitol accumulation and improving xylose consumption and ethanol production. Similar results are observed in fermentations of detoxified hydrolysate. However, in the presence of lignocellulosic-derived inhibitors, a positive synergistic effect results from the expression of both XI and XR/XDH, possibly caused by a cofactor equilibrium between the XDH and furan detoxifying enzymes, increasing the ethanol yield by more than 38%. Advantage of using the XI from Clostridium phytofermentans to attain high ethanol productivities and yields from xylose, and the simultaneous utilization of XR/XDH and XI pathways compared to the single expression of XR/XDH or XI improves ethanol production from non-detoxified hemicellulosic hydrolysates
additional information
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Saccharomyces cerevisiae, the preferred microorganism for large-scale ethanol production, does not naturally consume xylose. Xylose isomerase (XI) and xylose reductase/xylitol dehydrogenase (XR/XDH) pathways are introduced into two robust industrial Saccharomyces cerevisiae strains, PE-2DELTAGRE3 and CA11, evaluated in synthetic media and corn cob hemicellulosic hydrolysate (non-detoxified corn cob hydrolysate) and the results are correlated with the differential enzyme activities found in the xylose-pathway engineered strains, evaluation of xylose fermentation capacity in oxygen-deprived conditions at 30°C and 40°C. Regarding the CA11-derived strains, the XR activity is higher in the strain with both pathways than in the one solely expressing XR/XDH, while the XDH activity at 30°C is higher in the CA11-XR/XDH strain. The sole expression of XI increases the fermentative capacity of both strains in synthetic media at 30°C and 40°C: decreasing xylitol accumulation and improving xylose consumption and ethanol production. Similar results are observed in fermentations of detoxified hydrolysate. However, in the presence of lignocellulosic-derived inhibitors, a positive synergistic effect results from the expression of both XI and XR/XDH, possibly caused by a cofactor equilibrium between the XDH and furan detoxifying enzymes, increasing the ethanol yield by more than 38%. Advantage of using the XI from Clostridium phytofermentans to attain high ethanol productivities and yields from xylose, and the simultaneous utilization of XR/XDH and XI pathways compared to the single expression of XR/XDH or XI improves ethanol production from non-detoxified hemicellulosic hydrolysates
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additional information
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expression of the xylitol dehydrogenase-encoding gene XYL2 of Pichia stipitis in the transketolase-deficient Saccharomyces cerevisiae strain results in an 8.5fold enhancement of the total amount of the excreted sugar alcohols ribitol and xylitol. The additional introduction of the 2-deoxy-glucose 6-phosphate phosphatase-encoding gene DOG1 into the transketolase-deficient strain expressing the XYL2 gene resulted in a further 1.6fold increase in ribitol production
additional information
engineered Saccharomyces cerevisiae strain DGX23 overexpressing aldose reductase GRE3, xylitol dehydrogenase XYL2, and xylulokinase XYL3 can ferment xylose as well as a mixture of glucose and xylose with higher ethanol yields and productivities than those of an isogenic strain overexpressing xylose reductase XYL1, xylitol dehydrogenase XYL2, and xylulokinase XYL3 under oxygen-limited conditions. Optimized expression levels of GRE3, XYL2, and XYL3 can overcome redox imbalance during xylose fermentation by engineered Saccharomyces cerevisiae under oxygen-limited conditions, anaerobic xylose fermentation
additional information
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engineered Saccharomyces cerevisiae strain DGX23 overexpressing aldose reductase GRE3, xylitol dehydrogenase XYL2, and xylulokinase XYL3 can ferment xylose as well as a mixture of glucose and xylose with higher ethanol yields and productivities than those of an isogenic strain overexpressing xylose reductase XYL1, xylitol dehydrogenase XYL2, and xylulokinase XYL3 under oxygen-limited conditions. Optimized expression levels of GRE3, XYL2, and XYL3 can overcome redox imbalance during xylose fermentation by engineered Saccharomyces cerevisiae under oxygen-limited conditions, anaerobic xylose fermentation
additional information
enzyme XDH is changed from NAD+-dependent to NADP+-dependent, xylitol accumulation is reduced and ethanol production improved using protein engineering for reversing the dependency of XDH from NAD+ to NADP+. Construction of a set of recombinant Saccharomyces cerevisiae carrying a mutated strictly NADPH-dependent XR and NADP+-dependent XDH genes with overexpression of endogenous xylulokinase (XK), effects of complete NADPH/NADP+ recycling on ethanol fermentation and xylitol accumulation, overview. The mutated strains demonstrate 0% and 10% improvement in ethanol production, and reduced xylitol accumulation, ranging 34.4-54.7% compared with the control strain
additional information
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enzyme XDH is changed from NAD+-dependent to NADP+-dependent, xylitol accumulation is reduced and ethanol production improved using protein engineering for reversing the dependency of XDH from NAD+ to NADP+. Construction of a set of recombinant Saccharomyces cerevisiae carrying a mutated strictly NADPH-dependent XR and NADP+-dependent XDH genes with overexpression of endogenous xylulokinase (XK), effects of complete NADPH/NADP+ recycling on ethanol fermentation and xylitol accumulation, overview. The mutated strains demonstrate 0% and 10% improvement in ethanol production, and reduced xylitol accumulation, ranging 34.4-54.7% compared with the control strain
additional information
engineered Sacchyromyces cerevisiae expressing NADPH-linked xylose reductase (XR) and NAD+-linked xylitol dehydrogenase (XDH) produces substantial amounts of the reduced byproducts under anaerobic conditions due to the cofactor difference of XR and XDH. While the additional expression of a water-forming NADH oxidase (NoxE) from Lactococcus lactis in engineered Saccharomyces cerevisiae with the XR/XDH pathway leads to reduced glycerol and xylitol production and increased ethanol yields from xylose, volumetric ethanol productivities by the engineered yeast decrease because of growth defects from the overexpression of noxE. High cell density inoculum for xylose fermentation by strain SR8 expressing noxE, resulting in strain SR8N, shows a higher ethanol yield and lower byproduct yields, and also exhibits a high ethanol productivity during xylose fermentation. Growth defects from noxE overexpression can be overcome in the case of fermenting lignocellulose-derived sugars such as glucose and xylosen
additional information
construction of efficient xylose-fermenting Saccharomyces cerevisiae strain DXS through a synthetic isozyme system of xylose reductase from Scheffersomyces stipitis. The xylose-metabolic genes XYL1 (EC 1.1.1.307), XYL2, and XYL3 (EC 2.7.1.17) from Scheffersomyces stipitis are introduced into Saccharomyces cerevisiae. Construction of control strains SR6 and MM through random integration of the XR (NADPH) or mXR (NADH) expression cassette, respectively, at the multipled elements of the genome of Saccharomyces cerevisiae strain D452-2. Fermentation parameters of engineered Saccharomyces cerevisiae strains in mixed sugar fermentations (glucose and xylose), overview
additional information
efficient uptake and reduction of xylose photoautotrophically in Synechococcus elongatus strain PCC7942 are demonstrated upon introduction of an effective xylose transporter from Escherichia coli (Ec-XylE) and the NADPH-dependent xylose reductase from Candida boidinii (Cb-XR). Simultaneous activation of xylose uptake and matching of cofactor specificity enables an average xylitol yield of 0.9 g/g xylose and a maximum productivity of about 0.15 g/l/day/OD with increased level of xylose supply. High-density conversion of xylose to xylitol using concentrated resting cells further pushes the titer of xylitol formation to 33 g/l in six days with 85% of maximum theoretical yield. Comparison of the efficiencies of the two routes for xylitol biosynthesis, detailed overview
additional information
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construction of efficient xylose-fermenting Saccharomyces cerevisiae strain DXS through a synthetic isozyme system of xylose reductase from Scheffersomyces stipitis. The xylose-metabolic genes XYL1 (EC 1.1.1.307), XYL2, and XYL3 (EC 2.7.1.17) from Scheffersomyces stipitis are introduced into Saccharomyces cerevisiae. Construction of control strains SR6 and MM through random integration of the XR (NADPH) or mXR (NADH) expression cassette, respectively, at the multipled elements of the genome of Saccharomyces cerevisiae strain D452-2. Fermentation parameters of engineered Saccharomyces cerevisiae strains in mixed sugar fermentations (glucose and xylose), overview
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additional information
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engineered Sacchyromyces cerevisiae expressing NADPH-linked xylose reductase (XR) and NAD+-linked xylitol dehydrogenase (XDH) produces substantial amounts of the reduced byproducts under anaerobic conditions due to the cofactor difference of XR and XDH. While the additional expression of a water-forming NADH oxidase (NoxE) from Lactococcus lactis in engineered Saccharomyces cerevisiae with the XR/XDH pathway leads to reduced glycerol and xylitol production and increased ethanol yields from xylose, volumetric ethanol productivities by the engineered yeast decrease because of growth defects from the overexpression of noxE. High cell density inoculum for xylose fermentation by strain SR8 expressing noxE, resulting in strain SR8N, shows a higher ethanol yield and lower byproduct yields, and also exhibits a high ethanol productivity during xylose fermentation. Growth defects from noxE overexpression can be overcome in the case of fermenting lignocellulose-derived sugars such as glucose and xylosen
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additional information
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efficient uptake and reduction of xylose photoautotrophically in Synechococcus elongatus strain PCC7942 are demonstrated upon introduction of an effective xylose transporter from Escherichia coli (Ec-XylE) and the NADPH-dependent xylose reductase from Candida boidinii (Cb-XR). Simultaneous activation of xylose uptake and matching of cofactor specificity enables an average xylitol yield of 0.9 g/g xylose and a maximum productivity of about 0.15 g/l/day/OD with increased level of xylose supply. High-density conversion of xylose to xylitol using concentrated resting cells further pushes the titer of xylitol formation to 33 g/l in six days with 85% of maximum theoretical yield. Comparison of the efficiencies of the two routes for xylitol biosynthesis, detailed overview
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additional information
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construction of efficient xylose-fermenting Saccharomyces cerevisiae strain DXS through a synthetic isozyme system of xylose reductase from Scheffersomyces stipitis. The xylose-metabolic genes XYL1 (EC 1.1.1.307), XYL2, and XYL3 (EC 2.7.1.17) from Scheffersomyces stipitis are introduced into Saccharomyces cerevisiae. Construction of control strains SR6 and MM through random integration of the XR (NADPH) or mXR (NADH) expression cassette, respectively, at the multipled elements of the genome of Saccharomyces cerevisiae strain D452-2. Fermentation parameters of engineered Saccharomyces cerevisiae strains in mixed sugar fermentations (glucose and xylose), overview
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additional information
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efficient uptake and reduction of xylose photoautotrophically in Synechococcus elongatus strain PCC7942 are demonstrated upon introduction of an effective xylose transporter from Escherichia coli (Ec-XylE) and the NADPH-dependent xylose reductase from Candida boidinii (Cb-XR). Simultaneous activation of xylose uptake and matching of cofactor specificity enables an average xylitol yield of 0.9 g/g xylose and a maximum productivity of about 0.15 g/l/day/OD with increased level of xylose supply. High-density conversion of xylose to xylitol using concentrated resting cells further pushes the titer of xylitol formation to 33 g/l in six days with 85% of maximum theoretical yield. Comparison of the efficiencies of the two routes for xylitol biosynthesis, detailed overview
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additional information
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construction of efficient xylose-fermenting Saccharomyces cerevisiae strain DXS through a synthetic isozyme system of xylose reductase from Scheffersomyces stipitis. The xylose-metabolic genes XYL1 (EC 1.1.1.307), XYL2, and XYL3 (EC 2.7.1.17) from Scheffersomyces stipitis are introduced into Saccharomyces cerevisiae. Construction of control strains SR6 and MM through random integration of the XR (NADPH) or mXR (NADH) expression cassette, respectively, at the multipled elements of the genome of Saccharomyces cerevisiae strain D452-2. Fermentation parameters of engineered Saccharomyces cerevisiae strains in mixed sugar fermentations (glucose and xylose), overview
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additional information
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efficient uptake and reduction of xylose photoautotrophically in Synechococcus elongatus strain PCC7942 are demonstrated upon introduction of an effective xylose transporter from Escherichia coli (Ec-XylE) and the NADPH-dependent xylose reductase from Candida boidinii (Cb-XR). Simultaneous activation of xylose uptake and matching of cofactor specificity enables an average xylitol yield of 0.9 g/g xylose and a maximum productivity of about 0.15 g/l/day/OD with increased level of xylose supply. High-density conversion of xylose to xylitol using concentrated resting cells further pushes the titer of xylitol formation to 33 g/l in six days with 85% of maximum theoretical yield. Comparison of the efficiencies of the two routes for xylitol biosynthesis, detailed overview
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additional information
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combination of xylose reductase from Spathaspora arborariae with xylitol dehydrogenase from Spathaspora passalidarum to promote xylose consumption and fermentation into xylitol in Saccharomyces cerevisiae. Recombinant co-expression of Spathaspora arborariae xylose reductase gene (SaXYL1) that accepts both NADH and NADPH as co-substrates, and of Spathaspora passalidarum strain UFMG-HM.19.1AT NADPH-dependent xylose reductase (SpXYL1.1 gene) or the SpXYL2.2 gene from Spathaspora passalidarum strain UFMG-CM-Y474 in a Saccharomyces cerevisiae strain overexpressing the native XKS1 gene encoding xylulokinase, as well as being deleted in the alkaline phosphatase encoded by the PHO13 gene. Strains expressing the Spathaspora enzymes consumes xylose with xylitol as the major fermentation product. Higher specific growth rates, xylose consumption, and xylitol volumetric productivities are obtained by the co-expression of the SaXYL1 and SpXYL2.2 genes, when compared with the co-expression of the NADPH-dependent SpXYL1.1 xylose reductase. During glucose-xylose co-fermentation by the strain with co-expression of the SaXYL1 and SpXYL2.2 genes, both ethanol and xylitol are produced efficiently. Method development and evaluation, detailed overview
additional information
the combinatorial expression of two xylose reductase (XR) genes and two xylitol dehydrogenase (XDH) genes from Spathaspora passalidarum and the heterologous expression of the Piromyces sp. xylose isomerase (XI) gene are induced in Aureobasidium pullulans strain CBS 110374. Overexpression of XYL1.2 (encoding XR) and XYL2.2 (encoding XDH) is the most beneficial for xylose utilization, resulting in a 17.76% increase in consumed xylose compared with the parent strain, whereas the introduction of the Piromyces sp. XI pathway fails to enhance xylose utilization efficiency. Construction of knock-in mutants, method, evaluation of internal redox state, xylose utilization and cell growth of the recombinant strains, pH 5.8, 28°C, comparison the fermentation abilities of the parent strain and the recombinant strains using several carbon sources, overview
additional information
the combinatorial expression of two xylose reductase (XR) genes and two xylitol dehydrogenase (XDH) genes from Spathaspora passalidarum and the heterologous expression of the Piromyces sp. xylose isomerase (XI) gene are induced in Aureobasidium pullulans strain CBS 110374. Overexpression of XYL1.2 (encoding XR) and XYL2.2 (encoding XDH) is the most beneficial for xylose utilization, resulting in a 17.76% increase in consumed xylose compared with the parent strain, whereas the introduction of the Piromyces sp. XI pathway fails to enhance xylose utilization efficiency. Construction of knock-in mutants, method, evaluation of internal redox state, xylose utilization and cell growth of the recombinant strains, pH 5.8, 28°C, comparison the fermentation abilities of the parent strain and the recombinant strains using several carbon sources, overview
additional information
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the combinatorial expression of two xylose reductase (XR) genes and two xylitol dehydrogenase (XDH) genes from Spathaspora passalidarum and the heterologous expression of the Piromyces sp. xylose isomerase (XI) gene are induced in Aureobasidium pullulans strain CBS 110374. Overexpression of XYL1.2 (encoding XR) and XYL2.2 (encoding XDH) is the most beneficial for xylose utilization, resulting in a 17.76% increase in consumed xylose compared with the parent strain, whereas the introduction of the Piromyces sp. XI pathway fails to enhance xylose utilization efficiency. Construction of knock-in mutants, method, evaluation of internal redox state, xylose utilization and cell growth of the recombinant strains, pH 5.8, 28°C, comparison the fermentation abilities of the parent strain and the recombinant strains using several carbon sources, overview
additional information
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the combinatorial expression of two xylose reductase (XR) genes and two xylitol dehydrogenase (XDH) genes from Spathaspora passalidarum and the heterologous expression of the Piromyces sp. xylose isomerase (XI) gene are induced in Aureobasidium pullulans strain CBS 110374. Overexpression of XYL1.2 (encoding XR) and XYL2.2 (encoding XDH) is the most beneficial for xylose utilization, resulting in a 17.76% increase in consumed xylose compared with the parent strain, whereas the introduction of the Piromyces sp. XI pathway fails to enhance xylose utilization efficiency. Construction of knock-in mutants, method, evaluation of internal redox state, xylose utilization and cell growth of the recombinant strains, pH 5.8, 28°C, comparison the fermentation abilities of the parent strain and the recombinant strains using several carbon sources, overview
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additional information
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the combinatorial expression of two xylose reductase (XR) genes and two xylitol dehydrogenase (XDH) genes from Spathaspora passalidarum and the heterologous expression of the Piromyces sp. xylose isomerase (XI) gene are induced in Aureobasidium pullulans strain CBS 110374. Overexpression of XYL1.2 (encoding XR) and XYL2.2 (encoding XDH) is the most beneficial for xylose utilization, resulting in a 17.76% increase in consumed xylose compared with the parent strain, whereas the introduction of the Piromyces sp. XI pathway fails to enhance xylose utilization efficiency. Construction of knock-in mutants, method, evaluation of internal redox state, xylose utilization and cell growth of the recombinant strains, pH 5.8, 28°C, comparison the fermentation abilities of the parent strain and the recombinant strains using several carbon sources, overview
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additional information
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combination of xylose reductase from Spathaspora arborariae with xylitol dehydrogenase from Spathaspora passalidarum to promote xylose consumption and fermentation into xylitol in Saccharomyces cerevisiae. Recombinant co-expression of Spathaspora arborariae xylose reductase gene (SaXYL1) that accepts both NADH and NADPH as co-substrates, and of Spathaspora passalidarum strain UFMG-HM.19.1AT NADPH-dependent xylose reductase (SpXYL1.1 gene) or the SpXYL2.2 gene from Spathaspora passalidarum strain UFMG-CM-Y474 in a Saccharomyces cerevisiae strain overexpressing the native XKS1 gene encoding xylulokinase, as well as being deleted in the alkaline phosphatase encoded by the PHO13 gene. Strains expressing the Spathaspora enzymes consumes xylose with xylitol as the major fermentation product. Higher specific growth rates, xylose consumption, and xylitol volumetric productivities are obtained by the co-expression of the SaXYL1 and SpXYL2.2 genes, when compared with the co-expression of the NADPH-dependent SpXYL1.1 xylose reductase. During glucose-xylose co-fermentation by the strain with co-expression of the SaXYL1 and SpXYL2.2 genes, both ethanol and xylitol are produced efficiently. Method development and evaluation, detailed overview
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[Candida] mogii
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Scheffersomyces stipitis (P22144), Scheffersomyces stipitis
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Ehrensberger, A.H.; Elling, R.A.; Wilson, D.K.
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Scheffersomyces stipitis
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Meyerozyma guilliermondii, Meyerozyma guilliermondii FTI 20037
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Aspergillus oryzae, Aspergillus oryzae (Q86ZV0), Aspergillus oryzae KBN616, Aspergillus oryzae KBN616 (Q86ZV0)
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Scheffersomyces stipitis (P22144), Scheffersomyces stipitis
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Gluconobacter oxydans, Gluconobacter oxydans NH-10
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Rhizomucor pusillus (S6BFC0), Rhizomucor pusillus, Rhizomucor pusillus NBRC 4578 (S6BFC0), Rhizomucor pusillus NBRC 4578
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Scheffersomyces stipitis
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Gluconobacter oxydans, Gluconobacter oxydans CGMCC 1.49
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Purification and characterization of xylitol dehydrogenase with L-arabitol dehydrogenase activity from the newly isolated pentose-fermenting yeast Meyerozyma caribbica 5XY2
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Meyerozyma caribbica, Meyerozyma caribbica (A0A1B4XTS0), Meyerozyma caribbica 5XY2, Meyerozyma caribbica 5XY2 (A0A1B4XTS0)
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Weyda, I.; Luebeck, M.; Ahring, B.K.; Luebeck, P.S.
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Aspergillus carbonarius
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Zhang, C.; Zong, H.; Zhuge, B.; Lu, X.; Fang, H.; Zhuge, J.
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Scheffersomyces stipitis (P22144), Scheffersomyces stipitis
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Xylitol production by NAD+-dependent xylitol dehydrogenase (xdhA)- and L-arabitol-4-dehydrogenase (ladA)-disrupted mutants of Aspergillus oryzae
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Aspergillus oryzae (Q86ZV0), Aspergillus oryzae, Aspergillus oryzae P5 (Q86ZV0)
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Scheffersomyces stipitis (P22144), Scheffersomyces stipitis
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Molecular analysis of NAD+-dependent xylitol dehydrogenase from the zygomycetous fungus Rhizomucor pusillus and reversal of the coenzyme preference
Biosci. Biotechnol. Biochem.
78
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Rhizomucor pusillus (S6BFC0), Rhizomucor pusillus, Rhizomucor pusillus NBRC 4578 (S6BFC0), Rhizomucor pusillus NBRC 4578
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Zhang, J.; Li, S.; Xu, H.; Zhou, P.; Zhang, L.; Ouyang, P.
Purification of xylitol dehydrogenase and improved production of xylitol by increasing XDH activity and NADH supply in Gluconobacter oxydans
J. Agric. Food Chem.
61
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Gluconobacter oxydans (Q8GR61), Gluconobacter oxydans, Gluconobacter oxydans NH-10 (Q8GR61)
brenda
Mahmud, A.; Hattori, K.; Hongwen, C.; Kitamoto, N.; Suzuki, T.; Nakamura, K.; Takamizawa, K.
Xylitol production by NAD+-dependent xylitol dehydrogenase (xdhA)- and L-arabitol-4-dehydrogenase (ladA)-disrupted mutants of Aspergillus oryzae
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115
353-359
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Aspergillus oryzae (Q86ZV0), Aspergillus oryzae, Aspergillus oryzae KBN616 (Q86ZV0)
brenda
Qi, X.H.; Zhu, J.F.; Yun, J.H.; Lin, J.; Qi, Y.L.; Guo, Q.; Xu, H.
Enhanced xylitol production expression of xylitol dehydrogenase from Gluconobacter oxydans and mixed culture of resting cell
J. Biosci. Bioeng.
122
257-262
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Gluconobacter oxydans (A0A141BGH5), Gluconobacter oxydans, Gluconobacter oxydans CGMCC 1.49 (A0A141BGH5), Gluconobacter oxydans CGMCC 1.49
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Tani, T.; Taguchi, H.; Akamatsu, T.
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Scheffersomyces stipitis
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Weyda, I.; Luebeck, M.; Ahring, B.K.; Luebeck, P.S.
Point mutation of the xylose reductase (XR) gene reduces xylitol accumulation and increases citric acid production in Aspergillus carbonarius
J. Ind. Microbiol. Biotechnol.
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Aspergillus carbonarius, Aspergillus carbonarius ITEM 5010
brenda
Zhang, G.C.; Turner, T.L.; Jin, Y.S.
Enhanced xylose fermentation by engineered yeast expressing NADH oxidase through high cell density inoculums
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Scheffersomyces stipitis (P22144), Scheffersomyces stipitis ATCC 58785 (P22144)
brenda
Liu, L.; Zeng, W.; Du, G.; Chen, J.; Zhou, J.
Identification of NAD-dependent xylitol dehydrogenase from Gluconobacter oxydans WSH-003
ACS omega
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Gluconobacter oxydans, Gluconobacter oxydans WSH-003
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Jo, J.H.; Park, Y.C.; Jin, Y.S.; Seo, J.H.
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Scheffersomyces stipitis (P22144), Scheffersomyces stipitis NRRL Y-11545 (P22144), Scheffersomyces stipitis NBRC 10063 (P22144), Scheffersomyces stipitis ATCC 58785 (P22144)
brenda
Cunha, J.T.; Soares, P.O.; Romani, A.; Thevelein, J.M.; Domingues, L.
Xylose fermentation efficiency of industrial Saccharomyces cerevisiae yeast with separate or combined xylose reductase/xylitol dehydrogenase and xylose isomerase pathways
Biotechnol. Biofuels
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2019
Saccharomyces cerevisiae (Q07993), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (Q07993)
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Fan, E.S.; Lu, K.W.; Wen, R.C.; Shen, C.R.
Photosynthetic reduction of xylose to xylitol using cyanobacteria
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Scheffersomyces stipitis (P22144), Scheffersomyces stipitis NRRL Y-11545 (P22144), Scheffersomyces stipitis NBRC 10063 (P22144), Scheffersomyces stipitis ATCC 58785 (P22144)
brenda
Mouro, A.; Santos, A.; Agnolo, D.; Gubert, G.; Bon, E.; Rosa, C.; Fonseca, C.; Stambuk, B.
Combining xylose reductase from Spathaspora arborariae with xylitol dehydrogenase from Spathaspora passalidarum to promote xylose consumption and fermentation into xylitol by Saccharomyces cerevisiae
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2020
Spathaspora passalidarum, Spathaspora passalidarum UFMG-CM-Y474
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Sukpipat, W.; Komeda, H.; Prasertsan, P.; Asano, Y.
Purification and characterization of xylitol dehydrogenase with L-arabitol dehydrogenase activity from the newly isolated pentose-fermenting yeast Meyerozyma caribbica 5XY2
J. Biosci. Bioeng.
123
20-27
2017
Meyerozyma caribbica (A0A1B4XTS0), Meyerozyma caribbica, Meyerozyma caribbica 5XY2 (A0A1B4XTS0), Meyerozyma caribbica 5XY2
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Han, X.; Hu, X.; Zhou, C.; Wang, H.; Li, Q.; Ouyang, Y.; Kuang, X.; Xiao, D.; Xiang, Q.; Yu, X.; Li, X.; Gu, Y.; Zhao, K.; Chen, Q.; Ma, M.
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Pichia kudriavzevii (A0A3S7PMB5), Pichia kudriavzevii, Torulaspora delbrueckii (A0A3S7PMC4), Torulaspora delbrueckii, Scheffersomyces stipitis (P22144), Scheffersomyces stipitis, Pichia kudriavzevii QLB_09 (A0A3S7PMB5), Scheffersomyces stipitis NRRL Y-11545 (P22144), Scheffersomyces stipitis NBRC 10063 (P22144), Scheffersomyces stipitis ATCC 58785 (P22144), Torulaspora delbrueckii BLQ_03 (A0A3S7PMC4)
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Guo, J.; Huang, S.; Chen, Y.; Guo, X.; Xiao, D.
Heterologous expression of Spathaspora passalidarum xylose reductase and xylitol dehydrogenase genes improved xylose fermentation ability of Aureobasidium pullulans
Microb. Cell Fact.
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Spathaspora passalidarum (G3AIB3), Spathaspora passalidarum (G3AIP8), Spathaspora passalidarum, Spathaspora passalidarum 11-Y1 (G3AIB3), Spathaspora passalidarum 11-Y1 (G3AIP8), Spathaspora passalidarum NRRL Y-27907 (G3AIP8)
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