1.1.1.307: D-xylose reductase [NAD(P)H]
This is an abbreviated version!
For detailed information about D-xylose reductase [NAD(P)H], go to the full flat file.
Word Map on EC 1.1.1.307
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1.1.1.307
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synthesis
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l-arabinose
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stipitis
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kluyveromyces
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marxianus
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oxygen-limited
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nadph-linked
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reesei
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l-arabitol
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trichoderma
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passalidarum
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scheffersomyces
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spathaspora
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jecorina
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pachysolen
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pentitols
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bioethanol
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hypocrea
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tannophilus
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galactitol
- 1.1.1.307
- synthesis
- l-arabinose
- stipitis
-
kluyveromyces
- marxianus
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oxygen-limited
-
nadph-linked
- reesei
- l-arabitol
- trichoderma
- passalidarum
-
scheffersomyces
- spathaspora
- jecorina
-
pachysolen
- pentitols
-
bioethanol
- hypocrea
- tannophilus
- galactitol
Reaction
Synonyms
AKR2B5, ALR2, CTHT_0056950, CtXR, dsXR, dual specific xylose reductase, KmXYL1, NAD(P)H-dependent D-xylose reductase, NAD(P)H-dependent D-xylose reductase-like protein, NAD(P)H-dependent XR, NAD(P)H-dependent xylose reductase, NAD(P)H-linked xylose reductase, NADH/NADPH-xylose reductase, NADP-dependent xylose reductase, PsXR, PsXYL1, SaXYL1, SpXYL1.1, SsXR, Texr, XR, XYL1, xylose reductase, XylR, XyrA
ECTree
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Substrates Products
Substrates Products on EC 1.1.1.307 - D-xylose reductase [NAD(P)H]
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REACTION DIAGRAM
5,6-dideoxy-6-fluoro-D-xylohexofuranose + NADH + H+
? + NAD+
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-
-
?
6-azido-5,6-dideoxy-D-xylohexofuranose + NADH + H+
? + NAD+
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-
-
?
D-erythrose + NADPH + H+
erythritol + NADP+
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catalytic efficiency is 100fold higher than the catalytic efficiency for D-xylose
-
-
?
D-glucosone + NADPH + H+
D-fructose + NADP+
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catalytic efficiency is 22fold higher than the catalytic efficiency for D-xylose
-
-
?
DL-glyceraldehyde + NADH + H+
glycerol + NAD+
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low activity in direction of glycerol oxidation. At pH 6.0 polyol oxidation is not observed, but between pH 8 and 9 the enzyme oxidizes the polyol
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-
r
L-arabinose + NADH + H+
arabinitol + NAD+
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low activity in direction of arabinitol oxidation. At pH 6.0 polyol oxidation is not observed, but between pH 8 and 9 the enzyme oxidizes the polyol
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-
r
L-arabinose + NADPH + H+
arabinitol + NADP+
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low activity in direction of arabinitol oxidation. At pH 6.0 polyol oxidation is not observed, but between pH 8 and 9 the enzyme oxidizes the polyol
-
-
r
methylglyoxal + NADPH + H+
?
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catalytic efficiency is 20fold higher than the catalytic efficiency for D-xylose
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-
?
phenylglyoxal + NADPH + H+
?
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catalytic efficiency is 17fold higher than the catalytic efficiency for D-xylose
-
-
?
pyridine-2-aldehyde + NADPH + H+
?
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catalytic efficiency is 7fold higher than the catalytic efficiency for D-xylose
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-
?
valeraldehyde + NADPH + H+
?
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catalytic efficiency is 13fold higher than the catalytic efficiency for D-xylose
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-
?
xylosone + NADPH + H+
?
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catalytic efficiency is 20fold higher than the catalytic efficiency for D-xylose
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-
?
5,6-dideoxy-5,6-difluoro-D-glucofuranose + NADH + H+
? + NAD+
-
-
-
?
5,6-dideoxy-5-fluoro-D-glucofuranose + NADH + H+
? + NAD+
-
-
-
?
? + NAD+
-
-
-
-
?
6-azido-5,6-dideoxy-5-fluoro-D-glucofuranose + NADH + H+
? + NAD+
-
-
-
?
?
about 60% of the activity compared to D-xylose
-
-
?
D-arabinose + NADPH + H+
?
about 60% of the activity compared to D-xylose
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-
?
?
about 70% of the activity compared to D-xylose
-
-
?
D-galactose + NADPH + H+
?
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catalytic efficiency is 9.1% of the catalytic efficiency for D-xylose
-
-
?
D-galactose + NADPH + H+
galactitol + NADP+
Thermochaetoides thermophila CBS 144.50
-
-
-
r
D-galactose + NADPH + H+
galactitol + NADP+
Thermochaetoides thermophila DSM 1495
-
-
-
r
D-galactose + NADPH + H+
galactitol + NADP+
Thermochaetoides thermophila IMI 039719
-
-
-
r
?
about 15% of the activity compared to D-xylose
-
-
?
D-glucose + NADPH + H+
?
-
catalytic efficiency is 3.3% of the catalytic efficiency for D-xylose
-
-
?
?
about 90% of the activity compared to D-xylose
-
-
?
D-ribose + NADPH + H+
?
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catalytic efficiency is 41% of the catalytic efficiency for D-xylose
-
-
?
D-xylose + NAD(P)H + H+
xylitol + NAD(P)+
-
xylose reductase, using either NADH or NADPH, reduces D-xylose to xylitol, subsequently xylitol is oxidized to D-xylulose by a NAD+-linked xylulose dehydrogenase, EC 1.1.1.9
-
-
?
D-xylose + NADH + H+
xylitol + NAD+
dual coenzyme specificity, Km for NADPH: 0.0455 mM, Km for NADH: 0.162 mM
-
-
?
D-xylose + NADH + H+
xylitol + NAD+
dual coenzyme specificity, Km for NADPH: 0.0455 mM, Km for NADH: 0.162 mM
-
-
?
D-xylose + NADH + H+
xylitol + NAD+
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catalytic efficiency for NADPH is more than 100fold higher than the catalytic efficiency for NADH
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-
?
D-xylose + NADH + H+
xylitol + NAD+
wild-type TeXR shows dual coenzyme specificity but is preferentially NADPH-dependent, with affinity for NADPH being 1.1fold higher than NADH and catalytic efficiency (kcat/Km) 24.5fold higher with NADPH as coenzyme. Affinity for xylose is 3.6fold higher with NADPH as coenzyme
-
-
?
D-xylose + NADH + H+
xylitol + NAD+
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active with both NADPH and NADH as coenzyme. The activity with NADH is approximately 70% of that with NADPH for the various aldose substrates. Rate of xylitol oxidation is 4% of the rate of D-xylose reduction. At pH 6.0 polyol oxidation is not observed, but between pH 8 and 9 the enzyme oxidizes the polyol
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-
r
D-xylose + NADH + H+
xylitol + NAD+
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wild-type enzyme prefers NADPH over NADH
-
-
?
D-xylose + NADH + H+
xylitol + NAD+
-
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-
r
D-xylose + NADH + H+
xylitol + NAD+
-
-
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r
D-xylose + NADH + H+
xylitol + NAD+
-
-
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r
D-xylose + NADH + H+
xylitol + NAD+
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about 25% of the activity with NADPH
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r
D-xylose + NADH + H+
xylitol + NAD+
Spathaspora arborariae UFMG-HM.19.1AT
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about 25% of the activity with NADPH
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r
D-xylose + NADH + H+
xylitol + NAD+
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dual (NADH and NADPH) coenzyme specificity
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-
?
D-xylose + NADPH + H+
xylitol + NADP+
key enzyme in xylose metabolism
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-
?
D-xylose + NADPH + H+
xylitol + NADP+
dual coenzyme specificity, Km for NADPH: 0.0455 mM, Km for NADH: 0.162 mM
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-
?
D-xylose + NADPH + H+
xylitol + NADP+
key enzyme in xylose metabolism
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-
?
D-xylose + NADPH + H+
xylitol + NADP+
dual coenzyme specificity, Km for NADPH: 0.0455 mM, Km for NADH: 0.162 mM
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-
?
D-xylose + NADPH + H+
xylitol + NADP+
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preferred substrates
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r
D-xylose + NADPH + H+
xylitol + NADP+
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catalytic efficiency for NADPH is more than 100fold higher than the catalytic efficiency for NADH
-
-
?
D-xylose + NADPH + H+
xylitol + NADP+
expression of Texr is inducible by the same carbon sources responsible for the induction of genes encoding enzymes relevant to lignocellulose hydrolysis, suggesting a coordinated expression of intracellular and extracellular enzymes relevant to hydrolysis and metabolism of pentose sugars in Talaromyces emersonii in adaptation to its natural habitat. This indicates a potential advantage in survival and response to a nutrient-poor environment
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-
?
D-xylose + NADPH + H+
xylitol + NADP+
wild-type TeXR shows dual coenzyme specificity but is preferentially NADPH-dependent, with affinity for NADPH being 1.1fold higher than NADH and catalytic efficiency (kcat/Km) 24.5fold higher with NADPH as coenzyme. Affinity for xylose is 3.6fold higher with NADPH as coenzyme
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-
?
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
r
D-xylose + NADPH + H+
xylitol + NADP+
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whereas in most bacteria metabolism of D-xylose proceeds via direct isomerization to D-xylulose, catalysed by xylose isomerase (EC 5.3.1.5), in yeasts this conversion is catalysed by the sequential action of two oxidoreductases: xylose reductase and xylitol dehydrogenase (EC 1.1.1.9)
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-
?
D-xylose + NADPH + H+
xylitol + NADP+
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xylose reductase is one of the key enzymes for xylose fermentation
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-
?
D-xylose + NADPH + H+
xylitol + NADP+
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active with both NADPH and NADH as coenzyme. The activity with NADH is approximately 70% of that with NADPH for the various aldose substrates. Rate of xylitol oxidation is 5% of the rate of D-xylose reduction. At pH 6.0 polyol oxidation is not observed, but between pH 8 and 9 the enzyme oxidizes the polyol
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-
r
D-xylose + NADPH + H+
xylitol + NADP+
-
wild-type enzyme prefers NADPH over NADH
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-
?
D-xylose + NADPH + H+
xylitol + NADP+
-
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r
D-xylose + NADPH + H+
xylitol + NADP+
-
-
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r
D-xylose + NADPH + H+
xylitol + NADP+
-
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r
D-xylose + NADPH + H+
xylitol + NADP+
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NADPH is the preferred cofactor
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r
D-xylose + NADPH + H+
xylitol + NADP+
Spathaspora arborariae UFMG-HM.19.1AT
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NADPH is the preferred cofactor
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r
D-xylose + NADPH + H+
xylitol + NADP+
Thermochaetoides thermophila
best substrates
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r
D-xylose + NADPH + H+
xylitol + NADP+
Thermochaetoides thermophila CBS 144.50
best substrates
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r
D-xylose + NADPH + H+
xylitol + NADP+
Thermochaetoides thermophila DSM 1495
best substrates
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r
D-xylose + NADPH + H+
xylitol + NADP+
Thermochaetoides thermophila IMI 039719
best substrates
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-
r
D-xylose + NADPH + H+
xylitol + NADP+
xylose reductases catalyse the initial reaction in the xylose utilisation pathway, the NAD(P)H dependent reduction of xylose to xylitol
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-
?
D-xylose + NADPH + H+
xylitol + NADP+
-
catalytic efficiency (kcat/Km) in D-xylose reduction at pH 7 is more than 60fold higher than that in xylitol oxidation. The enzyme prefers NADPH approximately 2fold to NADH
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-
r
D-xylose + NADPH + H+
xylitol + NADP+
-
dual (NADH and NADPH) coenzyme specificity
-
-
?
D-xylose + NADPH + H+
xylitol + NADP+
Yamadazyma tenuis CBS 4435
xylose reductases catalyse the initial reaction in the xylose utilisation pathway, the NAD(P)H dependent reduction of xylose to xylitol
-
-
?
glycerol + NADP+
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low activity in direction of glycerol oxidation. At pH 6.0 polyol oxidation is not observed, but between pH 8 and 9 the enzyme oxidizes the polyol
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-
r
DL-glyceraldehyde + NADPH + H+
glycerol + NADP+
-
catalytic efficiency is 37fold higher than the catalytic efficiency for D-xylose
-
-
?
L-arabinitol + NADP+
-
catalytic efficiency is 41% of the catalytic efficiency for D-xylose
-
-
?
L-arabinose + NADPH + H+
L-arabinitol + NADP+
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catalytic efficiency is 2fold higher than the catalytic efficiency for D-xylose
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-
?
xylitol + NAD(P)+
D-xylose + NAD(P)H + H+
-
-
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r
xylitol + NADP+
D-xylose + NADPH + H+
-
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NADPH is the preferred cofactor
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r
?
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Thermochaetoides thermophila
the enzyme exhibits dual cofactor specificity for NADPH and NADH and prefers D-xylose over other pentoses and investigated hexoses. No or poor activity with D-lyxose, D-mannose, L-xylose, and D-arabinose. L-arabinose, being structurally similar to D-xylose, has a kcat/KM value of still 33% of the value for D-xylose, whereas D-galactose and D-glucose result in only 6.3% and 1.3% of the kcat/KM for D-xylose. The difference in the catalytic efficiency is mainly a result from different KM values rather than differences in kcat
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-
-
additional information
?
-
Thermochaetoides thermophila CBS 144.50
the enzyme exhibits dual cofactor specificity for NADPH and NADH and prefers D-xylose over other pentoses and investigated hexoses. No or poor activity with D-lyxose, D-mannose, L-xylose, and D-arabinose. L-arabinose, being structurally similar to D-xylose, has a kcat/KM value of still 33% of the value for D-xylose, whereas D-galactose and D-glucose result in only 6.3% and 1.3% of the kcat/KM for D-xylose. The difference in the catalytic efficiency is mainly a result from different KM values rather than differences in kcat
-
-
-
additional information
?
-
Thermochaetoides thermophila DSM 1495
the enzyme exhibits dual cofactor specificity for NADPH and NADH and prefers D-xylose over other pentoses and investigated hexoses. No or poor activity with D-lyxose, D-mannose, L-xylose, and D-arabinose. L-arabinose, being structurally similar to D-xylose, has a kcat/KM value of still 33% of the value for D-xylose, whereas D-galactose and D-glucose result in only 6.3% and 1.3% of the kcat/KM for D-xylose. The difference in the catalytic efficiency is mainly a result from different KM values rather than differences in kcat
-
-
-
additional information
?
-
Thermochaetoides thermophila IMI 039719
the enzyme exhibits dual cofactor specificity for NADPH and NADH and prefers D-xylose over other pentoses and investigated hexoses. No or poor activity with D-lyxose, D-mannose, L-xylose, and D-arabinose. L-arabinose, being structurally similar to D-xylose, has a kcat/KM value of still 33% of the value for D-xylose, whereas D-galactose and D-glucose result in only 6.3% and 1.3% of the kcat/KM for D-xylose. The difference in the catalytic efficiency is mainly a result from different KM values rather than differences in kcat
-
-
-
additional information
?
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prefers glyceraldehyde, D-erythrose and even some aliphatic and aromatic aldehydes to the pentose sugars D-xylose and L-arabinose. Aldosones such as D-glucosone or D-xylosone are good substrates, whereas the corresponding 2-deoxy-aldose sugars are reduced at hardly detectable rates
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?