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Information on EC 1.1.1.307 - D-xylose reductase [NAD(P)H]
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EC Tree
1.1.1.307 D-xylose reductase [NAD(P)H]IUBMB Comments
Xylose reductases catalyse the reduction of xylose to xylitol, the initial reaction in the fungal D-xylose degradation pathway. Most of the enzymes exhibit a strict requirement for NADPH [cf. EC 1.1.1.431, D-xylose reductase (NADPH)]. However, a few D-xylose reductases, such as those from Neurospora crassa , Yamadazyma tenuis [2,3], Scheffersomyces stipitis , and the thermophilic fungus Chaetomium thermophilum [4,7], have dual coenzyme specificity, though they still prefer NADPH to NADH. Very rarely the enzyme prefers NADH [cf. EC 1.1.1.430, D-xylose reductase (NADH)].
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Word Map
- 1.1.1.307
- synthesis
- l-arabinose
- stipitis
-
kluyveromyces
- marxianus
-
oxygen-limited
-
nadph-linked
- reesei
- l-arabitol
- trichoderma
- passalidarum
-
scheffersomyces
- spathaspora
- jecorina
-
pachysolen
- pentitols
-
bioethanol
- hypocrea
- tannophilus
- galactitol
The enzyme appears in viruses and cellular organisms
Synonyms
akr2b5, kmxyl1, nad(p)h-dependent xr, nad(p)h-dependent d-xylose reductase, nad(p)h-linked xylose reductase, nadp-dependent xylose reductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CTHT_0056950
CtXR
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
PsXYL1
SaXYL1
SpXYL1.1
SsXR
XYL1
xylose reductase
XylR
NAD(P)H-dependent D-xylose reductase-like protein
Thermochaetoides thermophila
UniProt
NAD(P)H-dependent D-xylose reductase-like protein
Thermochaetoides thermophila CBS 144.50
UniProt
-
NAD(P)H-dependent D-xylose reductase-like protein
Thermochaetoides thermophila DSM 1495
UniProt
-
NAD(P)H-dependent D-xylose reductase-like protein
Thermochaetoides thermophila IMI 039719
UniProt
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
xylitol + NAD(P)+ = D-xylose + NAD(P)H + H+
-
-
-
-
xylitol + NAD(P)+ = D-xylose + NAD(P)H + H+
ordered bi-substrate mechanism in which the coenzyme binds first
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
xylitol:NAD(P)+ oxidoreductase
Xylose reductases catalyse the reduction of xylose to xylitol, the initial reaction in the fungal D-xylose degradation pathway. Most of the enzymes exhibit a strict requirement for NADPH [cf. EC 1.1.1.431, D-xylose reductase (NADPH)]. However, a few D-xylose reductases, such as those from Neurospora crassa [5], Yamadazyma tenuis [2,3], Scheffersomyces stipitis [1], and the thermophilic fungus Chaetomium thermophilum [4,7], have dual coenzyme specificity, though they still prefer NADPH to NADH. Very rarely the enzyme prefers NADH [cf. EC 1.1.1.430, D-xylose reductase (NADH)].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5,6-dideoxy-6-fluoro-D-xylohexofuranose + NADH + H+
? + NAD+
-
-
-
?
6-azido-5,6-dideoxy-D-xylohexofuranose + NADH + H+
? + NAD+
-
-
-
?
D-erythrose + NADPH + H+
erythritol + NADP+
-
catalytic efficiency is 100fold higher than the catalytic efficiency for D-xylose
-
-
?
D-glucosone + NADPH + H+
D-fructose + NADP+
-
catalytic efficiency is 22fold higher than the catalytic efficiency for D-xylose
-
-
?
DL-glyceraldehyde + NADH + H+
glycerol + NAD+
-
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
-
-
r
L-arabinose + NADH + H+
arabinitol + NAD+
-
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
L-arabinose + NADPH + H+
arabinitol + NADP+
-
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+
?
-
catalytic efficiency is 20fold higher than the catalytic efficiency for D-xylose
-
-
?
phenylglyoxal + NADPH + H+
?
-
catalytic efficiency is 17fold higher than the catalytic efficiency for D-xylose
-
-
?
pyridine-2-aldehyde + NADPH + H+
?
-
catalytic efficiency is 7fold higher than the catalytic efficiency for D-xylose
-
-
?
valeraldehyde + NADPH + H+
?
-
catalytic efficiency is 13fold higher than the catalytic efficiency for D-xylose
-
-
?
xylosone + NADPH + H+
?
-
catalytic efficiency is 20fold higher than the catalytic efficiency for D-xylose
-
-
?
5,6-dideoxy-5,6-difluoro-D-glucofuranose + NADH + H+
? + NAD+
-
-
-
?
5,6-dideoxy-5-fluoro-D-glucofuranose + NADH + H+
? + NAD+
-
-
-
?
6-azido-5,6-dideoxy-5-fluoro-D-glucofuranose + NADH + H+
? + NAD+
-
-
-
-
?
6-azido-5,6-dideoxy-5-fluoro-D-glucofuranose + NADH + H+
? + NAD+
-
-
-
?
D-arabinose + NADPH + H+
?
about 60% of the activity compared to D-xylose
-
-
?
D-arabinose + NADPH + H+
?
about 60% of the activity compared to D-xylose
-
-
?
D-galactose + NADPH + H+
?
about 70% of the activity compared to D-xylose
-
-
?
D-galactose + NADPH + H+
?
-
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
D-glucose + NADPH + H+
?
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
-
-
?
D-ribose + NADPH + H+
?
about 90% of the activity compared to D-xylose
-
-
?
D-ribose + NADPH + H+
?
-
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+
-
catalytic efficiency for NADPH is more than 100fold higher than the catalytic efficiency for NADH
-
-
?
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+
-
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
-
-
r
D-xylose + NADH + H+
xylitol + NAD+
-
wild-type enzyme prefers NADPH over NADH
-
-
?
D-xylose + NADH + H+
xylitol + NAD+
-
-
-
r
D-xylose + NADH + H+
xylitol + NAD+
-
-
-
r
D-xylose + NADH + H+
xylitol + NAD+
-
-
-
r
D-xylose + NADH + H+
xylitol + NAD+
-
about 25% of the activity with NADPH
-
-
r
D-xylose + NADH + H+
xylitol + NAD+
Spathaspora arborariae UFMG-HM.19.1AT
-
about 25% of the activity with NADPH
-
-
r
D-xylose + NADH + H+
xylitol + NAD+
-
dual (NADH and NADPH) coenzyme specificity
-
-
?
D-xylose + NADPH + H+
xylitol + NADP+
key enzyme in xylose metabolism
-
-
?
D-xylose + NADPH + H+
xylitol + NADP+
dual coenzyme specificity, Km for NADPH: 0.0455 mM, Km for NADH: 0.162 mM
-
-
?
D-xylose + NADPH + H+
xylitol + NADP+
key enzyme in xylose metabolism
-
-
?
D-xylose + NADPH + H+
xylitol + NADP+
dual coenzyme specificity, Km for NADPH: 0.0455 mM, Km for NADH: 0.162 mM
-
-
?
D-xylose + NADPH + H+
xylitol + NADP+
-
preferred substrates
-
-
r
D-xylose + NADPH + H+
xylitol + NADP+
-
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
-
-
?
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
-
-
?
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
r
D-xylose + NADPH + H+
xylitol + NADP+
-
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)
-
-
?
D-xylose + NADPH + H+
xylitol + NADP+
-
xylose reductase is one of the key enzymes for xylose fermentation
-
-
?
D-xylose + NADPH + H+
xylitol + NADP+
-
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
-
-
r
D-xylose + NADPH + H+
xylitol + NADP+
-
wild-type enzyme prefers NADPH over NADH
-
-
?
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
r
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
r
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
r
D-xylose + NADPH + H+
xylitol + NADP+
-
NADPH is the preferred cofactor
-
-
r
D-xylose + NADPH + H+
xylitol + NADP+
Spathaspora arborariae UFMG-HM.19.1AT
-
NADPH is the preferred cofactor
-
-
r
D-xylose + NADPH + H+
xylitol + NADP+
Thermochaetoides thermophila
best substrates
-
-
r
D-xylose + NADPH + H+
xylitol + NADP+
Thermochaetoides thermophila CBS 144.50