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Information on EC 1.1.1.307 - D-xylose reductase [NAD(P)H]
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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 expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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
best substrates
-
-
r
D-xylose + NADPH + H+
xylitol + NADP+
Thermochaetoides thermophila DSM 1495
best substrates
-
-
r
D-xylose + NADPH + H+
xylitol + NADP+
Thermochaetoides thermophila IMI 039719
best substrates
-
-
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
-
-
?
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
-
-
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
-
-
?
DL-glyceraldehyde + NADPH + H+
glycerol + NADP+
-
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
DL-glyceraldehyde + NADPH + H+
glycerol + NADP+
-
catalytic efficiency is 37fold higher than the catalytic efficiency for D-xylose
-
-
?
L-arabinose + NADPH + H+
L-arabinitol + NADP+
-
catalytic efficiency is 41% of the catalytic efficiency for D-xylose
-
-
?
L-arabinose + NADPH + H+
L-arabinitol + NADP+
-
catalytic efficiency is 2fold higher than the catalytic efficiency for D-xylose
-
-
?
xylitol + NAD(P)+
D-xylose + NAD(P)H + H+
-
-
-
r
xylitol + NADP+
D-xylose + NADPH + H+
-
-
NADPH is the preferred cofactor
-
r
additional information
?
-
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
-
-
-
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
?
-
-
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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-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+
-
-
-
r
D-xylose + NADH + H+
xylitol + NAD+
-
-
-
r
D-xylose + NADH + H+
xylitol + NAD+
-
-
-
r
D-xylose + NADPH + H+
xylitol + NADP+
key enzyme in xylose metabolism
-
-
?
D-xylose + NADPH + H+
xylitol + NADP+
key enzyme in xylose metabolism
-
-
?
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+
-
-
-
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+
-
-
-
r
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
r
D-xylose + NADPH + H+
xylitol + NADP+
-
-
-
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
-
-
?
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
-
-
?
xylitol + NAD(P)+
D-xylose + NAD(P)H + H+
-
-
-
r
xylitol + NADP+
D-xylose + NADPH + H+
-
-
NADPH is the preferred cofactor
-
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
-
active with both NADPH and NADH as coenzyme. The activity with NADH is approximately 70% of that with NADPH for the various aldose substrates. The ratio of activities with NADH and NADPH is approximately constant between pH 5 and 8
NADH
-
catalytic efficiency for NADPH is more than 100fold higher than the catalytic efficiency for NADH
NADH
dual coenzyme specificity, Km for NADPH: 0.0455 mM, Km for NADH: 0.162 mM
NADH
-
prefers NADPH approximately 2fold to NADH, largely due to better apparent binding of the phosphorylated form of the coenzyme
NADH
-
wild-type enzyme prefers NADPH as cofactor. K270M mutation results in a significant increase in the Km values for both NADPH and NADH. K270R mutation increases the Km value for NADPH 25fold, while the Km for NADH only increases two-fold
NADH
-
wild-type enzyme prefers NADPH over NADH. Mutant enzyme K270S/N272P/S271G/R276F shows a 25fold preference toward NADH over NADPH by a factor of about 13fold, or an improvement of about 42fold, as measured by the ratio of the specificity constant kcat/Km coenzyme
NADH
catalytic efficiency is 24.5fold higher with NADPH as coenzyme than with NADH
NADH
the ratio of NADH-linked to NADPH-linked activity is 1.92
NADH
enzyme has dual coenzyme specificity, accepting both NADH and NADPH
NADPH
-
active with both NADPH and NADH as coenzyme. The activity with NADH is approximately 70% of that with NADPH for the various aldose substrates. The ratio of activities with NADH and NADPH is approximately constant between pH 5 and 8
NADPH
-
catalytic efficiency for NADPH is more than 100fold higher than the catalytic efficiency for NADH
NADPH
dual coenzyme specificity, Km for NADPH: 0.0455 mM, Km for NADH: 0.162 mM
NADPH
-
prefers NADPH approximately 2fold to NADH, largely due to better apparent binding of the phosphorylated form of the coenzyme
NADPH
-
wild-type enzyme prefers NADPH as cofactor. K270M mutation results in a significant increase in the Km values for both NADPH and NADH. K270R mutation increases the Km value for NADPH 25fold, while the Km for NADH only increases two-fold
NADPH
-
wild-type enzyme prefers NADPH over NADH. Mutant enzyme K270S/N272P/S271G/R276F shows a 25fold preference toward NADH over NADPH by a factor of about 13fold, or an improvement of about 42fold, as measured by the ratio of the specificity constant kcat/Km coenzyme
NADPH
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. K271R/N273D double mutant displays an altered coenzyme preference with a 16fold improvement in NADH utilization relative to the wild type
NADPH
catalytic efficiency is 24.5fold higher with NADPH as coenzyme than with NADH. Affinity for xylose is 3.6fold higher with NADPH as coenzyme
NADPH
the ratio of NADH-linked to NADPH-linked activity is 1.92
NADPH
-
enzyme has dual coenzyme specificity, accepting both NADH and NADPH
NADPH
enzyme has dual coenzyme specificity, accepting both NADH and NADPH
additional information
-
the enzyme uses both NADPH and NADH but prefers NADPH, the activity with NADPH is about 5fold higher than that with NADH
-
additional information
-
Spathaspora arborariae xylose reductase accepts both NADH and NADPH as co-substrates, gene SpXYL1.1 encodes for a xylose reductase with higher NADH activity compared to other XRs. The NADH-dependent of activity of Xyl1 is 25% compared to NADPH
-
additional information
the enzyme can use either NADH or NADPH as co-substrate, its XR activity with NADH is about 70% of that with NADPH
-
additional information
the enzyme can use either NADH or NADPH as co-substrate, its XR activity with NADH is about 70% of that with NADPH
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
no increase in activity in presence of 1 mM NaCl and 1 mM MgSO4
additional information
-
no requirement for divalent cation is observed
additional information
-
no effect: Na+, K+, NH4+, Mg2+, Ca2+ and Co2+ in the form of the chloride salt in 50 mM Tris, pH 7.0, as well the anions PO43-, SO32-, NO3-, CO32-, citrate and tetraborate in the form of the sodium salt in 50 mM phosphate buffer, pH 7.0
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
gradual inactivation. NADH, ATP or 2'-AMP protects. No protection by D-xylose
NAD+
-
strong inhibition with the NADH-linked reaction, no inhibition of NADPH-linked reaction. NAD+ is a non-competitive inhibitor with respect to xylose and a competitive inhibitor with respect to NADH
NADP+
-
potent inhibitor of both the NADPH- and NADH-linked xylose reduction. Competition with NADPH and non-competitive inhibition with xylose in the NADPH-linked xylose reduction
NADP+
-
2 mM completely abolishes D-xylose reduction. Potent competitive inhibitor, inhibits both the NADH-dependent and the NADPH-dependent activity
additional information
recombinant PsXYL1 in the cells is not inhibited by D-xylose up to 1.5 M. Also, furfural hydroxymethylfurfural, aliphatic acids, and phenolic compounds in the hydrolysates do not inhibit the growth of the microorganisms and PsXYL1 enzyme activity in the cells
-
additional information
-
no effect by 5 mM EDTA, 500 mM sulfate, 5 mM 2-mercaptoethanol
-
additional information
recombinant PsXYL1 in the cells is not inhibited by D-xylose up to 1.5 M. Also, furfural hydroxymethylfurfural, aliphatic acids, and phenolic compounds in the hydrolysates do not inhibit the growth of the microorganisms and PsXYL1 enzyme activity in the cells
-
additional information
-
no inhibition by NAD+. No effect: Na+, K+, NH4+, Mg2+, Ca2+ and Co2+ in the form of the chloride salt in 50 mM Tris, pH 7.0, as well the anions Cl-, PO43-, SO32-, NO3-, CO32-, citrate and tetraborate in the form of the sodium salt in 50 mM phosphate buffer, pH 7.0. Glucose 6-phosphate, fructose 6-phosphate, fructose 1,6-bisphosphate, 6-phosphogluconate, phosphoenolpyruvate, oxaloacetate (5 mM each) have no effect
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.5
6-azido-5,6-dideoxy-5-fluoro-D-glucofuranose
pH 7, 25°C
-
241
D-galactose
Thermochaetoides thermophila
recombinant enzyme, pH 6.5, 30°C, with NADPH
471
D-glucose
Thermochaetoides thermophila
recombinant enzyme, pH 6.5, 30°C, with NADPH
24.56
D-xylose
pH 6.5, 37°C, cosubstrate: NADPH, wild-type enzyme
26.9
D-xylose
native enzyme, pH not specified in the publication, temperature not specified in the publication
38.2
D-xylose
recombinant enzyme, pH not specified in the publication, temperature not specified in the publication
67
D-xylose
mutant K21A/N272D, cosubstrate NADH, pH 6.5, 35°C
76.06
D-xylose
pH 6.5, 37°C, cosubstrate: NADH, mutant enzyme K271R/N273D
76.5
D-xylose
pH 6.5, 37°C, cosubstrate: NADPH, mutant enzyme K271R/N273D
168
D-xylose
-
pH 6.0, cofactor: NADPH, mutant enzyme K270S/N272P/S271G/R276F
291
D-xylose
-
pH 6.0, cofactor: NADH, mutant enzyme K270S/N272P/S271G/R276F
62.5
L-arabinose
Thermochaetoides thermophila
recombinant enzyme, pH 6.5, 30°C, with NADPH
0.119
NADH
Thermochaetoides thermophila
recombinant enzyme, pH 6.5, 30°C, with D-xylose
0.0091
NADPH
recombinant enzyme, pH not specified in the publication, temperature not specified in the publication
0.0141
NADPH
native enzyme, pH not specified in the publication, temperature not specified in the publication
0.135
NADPH
Thermochaetoides thermophila
recombinant enzyme, pH 6.5, 30°C, with D-xylose
additional information
additional information
Thermochaetoides thermophila
Michaelis-Menten kinetics
-
additional information
additional information
-
KM-values determined with crude extracts of native enzyme, mutant enzyme K270M and mutant enzyme K270R
-
additional information
additional information
-
kinetics of wild-type and mutant enzymes, detailed overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
18
5,6-dideoxy-5-fluoro-D-glucofuranose, 5,6-dideoxy-6-fluoro-D-xylo-hexofuranose
-
pH 7, 25°C
-
6.5
D-galactose
Thermochaetoides thermophila
recombinant enzyme, pH 6.5, 30°C, with NADPH
2.7
D-glucose
Thermochaetoides thermophila
recombinant enzyme, pH 6.5, 30°C, with NADPH
2.6
D-xylose
-
pH 6.0, cofactor: NADPH, mutant enzyme K270S/N272P/S271G/R276F
9.2
D-xylose
Thermochaetoides thermophila
recombinant enzyme, pH 6.5, 30°C, with NADPH
12
D-xylose
-
pH 6.0, cofactor: NADH, mutant enzyme K270S/N272P/S271G/R276F
35.2
D-xylose
Thermochaetoides thermophila
recombinant enzyme, pH 6.5, 55°C, with NADPH
25110
D-xylose
pH 6.5, 37°C, cosubstrate: NADH, mutant enzyme K271R/N273D
100900
D-xylose
pH 6.5, 37°C, cosubstrate: NADPH, mutant enzyme K271R/N273D
324000
D-xylose
pH 6.5, 37°C, cosubstrate: NADPH, wild-type enzyme
8.8
L-arabinose
Thermochaetoides thermophila
recombinant enzyme, pH 6.5, 30°C, with NADPH
11.4
NADPH
Thermochaetoides thermophila
recombinant enzyme, pH 6.5, 30°C, with D-xylose
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.6
6-azido-5,6-dideoxy-5-fluoro-D-glucofuranose
pH 7, 25°C
-
0.027
D-galactose
Thermochaetoides thermophila
recombinant enzyme, pH 6.5, 30°C, with NADPH
0.006
D-glucose
Thermochaetoides thermophila
recombinant enzyme, pH 6.5, 30°C, with NADPH
6.2
D-xylose
-
pH 6.0, cofactor: NADPH, mutant enzyme K270S/N272P/S271G/R276F
81.7
D-xylose
-
pH 6.0, cofactor: NADH, mutant enzyme K270S/N272P/S271G/R276F
0.141
L-arabinose
Thermochaetoides thermophila
recombinant enzyme, pH 6.5, 30°C, with NADPH
26.9
NADH
Thermochaetoides thermophila
recombinant enzyme, pH 6.5, 30°C, with D-xylose
84.4
NADPH
Thermochaetoides thermophila
recombinant enzyme, pH 6.5, 30°C, with D-xylose
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.7 - 10.2
recombinant enzyme, pH 7.0, 30°C, with co-expressed GDH
5.12
-
recombinant enzyme expressed in Saccharomyces cerevisiae strain CEN.PK2-1C, co-expressed with xylitol dehydrogenase from Spathaspora passalidarum strain UFMG-CM-Y474, substrate xylose and NADH, pH 6.0, 30°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
6.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 6.5
pH 4.0: about 55% of maximal activity, pH 6.5: about 60% of maximal activity
4 - 7
-
pH 4.0: about 40% of maximal activity, pH 7.0: about 50% of maximal activity
4.5 - 7.5
-
pH 4.5: about 55% of maximal activity, pH 7.5: about 50% of maximal activity
5 - 8
5.5 - 9
-
about 90% of maximal activity at pH 5.5, 60% at pH 9.0, and maximal activity at pH 6.0
5 - 8
active from pH 5 to pH 8, wild-type and double-mutant (K271R/N273D) protein
5 - 8
-
the ratio of activities with NADH and NADPH is approximately constant between pH 5 and 8
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
37
50
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 65
-
25°C: about 55% of maximal activity, 65°C: about 65% of maximal activity
30 - 60
30 - 60
30°C: about 70% of maximal activity, 60°C: about 45% of maximal activity
30 - 60
active from 30°C to 60°C, wild-type and double-mutant (K271R/N273D) protein
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
D-xylose utilization by the oleaginous microalga Chlorella sorokiniana. Compared with the culture in the dark, the consumption of D-xylose increased 2fold under light
brenda
additional information
-
D-xylose utilization by the oleaginous microalga Chlorella sorokiniana. Compared with the culture in the dark, the consumption of D-xylose increased 2fold under light
-
brenda
additional information
-
the organism grows on rice straw hemicellulosic hydrolysate, as the only source of nutrient, optimization of culture conditions for production of xylitol from D-xylose, xylitol dehydrogenase remains constant, whereas the level of xylose reductase decreases when the initial xylose concentration is increased from 30 to 70 g/l, development of enzyme activities, overview
brenda
additional information
Thermochaetoides thermophila
optimal growth temperature of the organism is 50-55°C
brenda
additional information
Thermochaetoides thermophila CBS 144.50
-
optimal growth temperature of the organism is 50-55°C
-
brenda
additional information
Thermochaetoides thermophila DSM 1495
-
optimal growth temperature of the organism is 50-55°C
-
brenda
additional information
Thermochaetoides thermophila IMI 039719
-
optimal growth temperature of the organism is 50-55°C
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
Meyerozyma caribbica and Calamus tenuis xylose reductase have close evolution relationship in Rossmann fold
malfunction
metabolism
physiological function
additional information
malfunction
overexpression of endogenous XR enhances xylitol productivity at 40°C by thermotolerant Kluyveromyces marxianus, high-temperature xylose consumption and xylitol production rates of the mKmXYL1 gene-overexpressing strain are compared to those of the parental strain KCTC17555DELTAURA3
malfunction
-
overexpression of endogenous XR enhances xylitol productivity at 40°C by thermotolerant Kluyveromyces marxianus, high-temperature xylose consumption and xylitol production rates of the mKmXYL1 gene-overexpressing strain are compared to those of the parental strain KCTC17555DELTAURA3
-
malfunction
-
overexpression of endogenous XR enhances xylitol productivity at 40°C by thermotolerant Kluyveromyces marxianus, high-temperature xylose consumption and xylitol production rates of the mKmXYL1 gene-overexpressing strain are compared to those of the parental strain KCTC17555DELTAURA3
-
malfunction
-
overexpression of endogenous XR enhances xylitol productivity at 40°C by thermotolerant Kluyveromyces marxianus, high-temperature xylose consumption and xylitol production rates of the mKmXYL1 gene-overexpressing strain are compared to those of the parental strain KCTC17555DELTAURA3
-
metabolism
-
key enzymes for xylitol production in yeasts are xylose reductase and xylitol dehydrogenase, EC 1.1.1.9, overview
metabolism
-
xylose reductase is the first enzyme in D-xylose metabolism, catalyzing the reduction of D-xylose to xylitol
metabolism
-
D-glucose-induced algal cells exhibit a remarkably increased D-xylose uptake rate. The uptake of D-xylose activates the related metabolic pathway, and the activities of a NAD(P)H-linked xylose reductase XR and NADP+-linked xylitol dehydrogenase XDH are detected in C. sorokiniana. Compared with the culture in the dark, the consumption of D-xylose increases 2fold under light but decreases to the same level with addition of 3-(3,4-dichlorophenyl)-1,1-dimethylurea
metabolism
in anaerobic culture, NAD+ generated in the NAD(P)H-dependent xylose reductase reaction is likely needed in the NAD+-dependent xylitol dehydrogenase reaction, whereas in aerobic culture, the NAD+ generated by oxidation of NADH in the mitochondria is required in the xylitol dehydrogenase reaction, analysis of the relationship between NAD(P)+/NAD(P)H redox balances and metabolisms of xylose or xylitol as carbon sources in aerobic and anaerobic batch cultures of recombinant Saccharomyces cerevisiae in a complex medium containing 20 g/l xylose or 20 g/l xylitol at pH 5.0 and 30°C. Addition of acetaldehyde (an effective oxidizer of NADH) increases the xylitol consumption by the anaerobically cultured strain. Gal2 and Fps1 transport xylitol both inward and outward and play a role in xylitol consumption importing xylitol into the cytosol and exporting it from the cells
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
-
derivatives of D-xylose and D-glucose, in which the hydroxy groups at C-5, and C-5 and C-6 are replaced by fluorine, hydrogen and azide are reduced with up to 3000fold increased catalytic efficiencies. Azide introduced at C-5 or C-6 destabilizes the transition state of reduction of the corresponding hydrogen-substituted aldoses by approx. 4 kJ/mol
metabolism
derivatives of D-xylose and D-glucose, in which the hydroxy groups at C-5, and C-5 and C-6 are replaced by fluorine, hydrogen and azide are reduced with up to 3000fold increased catalytic efficiencies. Azide introduced at C-5 or C-6 destabilizes the transition state of reduction of the corresponding hydrogen-substituted aldoses by approx. 4 kJ/mol
metabolism
-
ordered mechanism in which coenzyme binds first and substrate second
metabolism
-
D-glucose-induced algal cells exhibit a remarkably increased D-xylose uptake rate. The uptake of D-xylose activates the related metabolic pathway, and the activities of a NAD(P)H-linked xylose reductase XR and NADP+-linked xylitol dehydrogenase XDH are detected in C. sorokiniana. Compared with the culture in the dark, the consumption of D-xylose increases 2fold under light but decreases to the same level with addition of 3-(3,4-dichlorophenyl)-1,1-dimethylurea
-
metabolism
-
in anaerobic culture, NAD+ generated in the NAD(P)H-dependent xylose reductase reaction is likely needed in the NAD+-dependent xylitol dehydrogenase reaction, whereas in aerobic culture, the NAD+ generated by oxidation of NADH in the mitochondria is required in the xylitol dehydrogenase reaction, analysis of the relationship between NAD(P)+/NAD(P)H redox balances and metabolisms of xylose or xylitol as carbon sources in aerobic and anaerobic batch cultures of recombinant Saccharomyces cerevisiae in a complex medium containing 20 g/l xylose or 20 g/l xylitol at pH 5.0 and 30°C. Addition of acetaldehyde (an effective oxidizer of NADH) increases the xylitol consumption by the anaerobically cultured strain. Gal2 and Fps1 transport xylitol both inward and outward and play a role in xylitol consumption importing xylitol into the cytosol and exporting it from the cells
-
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
-
in anaerobic culture, NAD+ generated in the NAD(P)H-dependent xylose reductase reaction is likely needed in the NAD+-dependent xylitol dehydrogenase reaction, whereas in aerobic culture, the NAD+ generated by oxidation of NADH in the mitochondria is required in the xylitol dehydrogenase reaction, analysis of the relationship between NAD(P)+/NAD(P)H redox balances and metabolisms of xylose or xylitol as carbon sources in aerobic and anaerobic batch cultures of recombinant Saccharomyces cerevisiae in a complex medium containing 20 g/l xylose or 20 g/l xylitol at pH 5.0 and 30°C. Addition of acetaldehyde (an effective oxidizer of NADH) increases the xylitol consumption by the anaerobically cultured strain. Gal2 and Fps1 transport xylitol both inward and outward and play a role in xylitol consumption importing xylitol into the cytosol and exporting it from the cells
-
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
-
in anaerobic culture, NAD+ generated in the NAD(P)H-dependent xylose reductase reaction is likely needed in the NAD+-dependent xylitol dehydrogenase reaction, whereas in aerobic culture, the NAD+ generated by oxidation of NADH in the mitochondria is required in the xylitol dehydrogenase reaction, analysis of the relationship between NAD(P)+/NAD(P)H redox balances and metabolisms of xylose or xylitol as carbon sources in aerobic and anaerobic batch cultures of recombinant Saccharomyces cerevisiae in a complex medium containing 20 g/l xylose or 20 g/l xylitol at pH 5.0 and 30°C. Addition of acetaldehyde (an effective oxidizer of NADH) increases the xylitol consumption by the anaerobically cultured strain. Gal2 and Fps1 transport xylitol both inward and outward and play a role in xylitol consumption importing xylitol into the cytosol and exporting it from the cells
-
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
-
xylose reductase is the first enzyme in D-xylose metabolism, catalyzing the reduction of D-xylose to xylitol
-
physiological function
Candida intermedia produces two different isoforms. Isoform I is strictly specific for NADPH, isoform II shows similar specificity constants for NADPH and NADH
physiological function
-
isoform ALR1 is strictly specific for NADPH, EC 1.1.1.431, whereas isoform ALR2 utilises NADH and NADPH with similar specificity constants, EC 1.1.1.307
additional information
-
the transportation of D-xylose across the cell membrane of Chlorella sorokiniana is realized by an inducible hexose symporter. The uptake of D-xylose subsequently activates the expression of key catalytic enzymes that enables D-xylose entering central metabolism
additional information
Thermochaetoides thermophila
structure homology modeling based on a XR structure from Candida sp. (CaXR) as template (PDB ID 1SM9), analysis of the architecture of the cofactor binding site. Notable CaXR-to-CtXR replacements include N276T, L277R, R280I and Q283S
additional information
Thermochaetoides thermophila IMI 039719
-
structure homology modeling based on a XR structure from Candida sp. (CaXR) as template (PDB ID 1SM9), analysis of the architecture of the cofactor binding site. Notable CaXR-to-CtXR replacements include N276T, L277R, R280I and Q283S
-
additional information
Thermochaetoides thermophila DSM 1495
-
structure homology modeling based on a XR structure from Candida sp. (CaXR) as template (PDB ID 1SM9), analysis of the architecture of the cofactor binding site. Notable CaXR-to-CtXR replacements include N276T, L277R, R280I and Q283S
-
additional information
-
the transportation of D-xylose across the cell membrane of Chlorella sorokiniana is realized by an inducible hexose symporter. The uptake of D-xylose subsequently activates the expression of key catalytic enzymes that enables D-xylose entering central metabolism
-
additional information
Thermochaetoides thermophila CBS 144.50
-
structure homology modeling based on a XR structure from Candida sp. (CaXR) as template (PDB ID 1SM9), analysis of the architecture of the cofactor binding site. Notable CaXR-to-CtXR replacements include N276T, L277R, R280I and Q283S
-
Show AA Sequence and Transmembrane Helices (2789 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36000
40000
40000
x * 40000, wild-type and double-mutant (K271R/N273D) histidine-tagged protein, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
?
x * 40000, wild-type and double-mutant (K271R/N273D) histidine-tagged protein, SDS-PAGE
?
Thermochaetoides thermophila
x * 39244, sequence calculation, x * 41000, recombinant His-tagged enzyme, SDS-PAGE
?
Thermochaetoides thermophila CBS 144.50
-
x * 39244, sequence calculation, x * 41000, recombinant His-tagged enzyme, SDS-PAGE
-
?
Thermochaetoides thermophila DSM 1495
-
x * 39244, sequence calculation, x * 41000, recombinant His-tagged enzyme, SDS-PAGE
-
?
Thermochaetoides thermophila IMI 039719
-
x * 39244, sequence calculation, x * 41000, recombinant His-tagged enzyme, SDS-PAGE
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structures of enzyme bound to NADP+ and NAD+ show two different protein conformations capable of accommodating the presence or absence of the coenzyme 2'-phosphate group
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C36Y
K271R/N273D
K274M
-
site-directed mutagenesis, the mutant enzyme shows increased activity and altered kinetics compared to the wild-type enzyme
K74M/N276D
-
site-directed mutagenesis, the mutant enzyme shows increased activity and altered kinetics compared to the wild-type enzyme
N272D
-
site-directed mutagenesis, results in strain TMB 3422, the mutation enables the yeast for anaerobic growth on xylose displayed higher aerobic growth rates
N272D/P275Q
-
site-directed mutagenesis, results in strain TMB 3421, the mutations enable the yeast for anaerobic growth on xylose displayed higher aerobic growth rates
N276D
-
site-directed mutagenesis, the mutant enzyme shows increased activity and altered kinetics compared to the wild-type enzyme
P275Q
-
site-directed mutagenesis, results in strain TMB 3423, the mutation enables the yeast for anaerobic growth on xylose displayed higher aerobic growth rates
N272D
-
site-directed mutagenesis, results in strain TMB 3422, the mutation enables the yeast for anaerobic growth on xylose displayed higher aerobic growth rates
-
N272D/P275Q
-
site-directed mutagenesis, results in strain TMB 3421, the mutations enable the yeast for anaerobic growth on xylose displayed higher aerobic growth rates
-
P275Q
-
site-directed mutagenesis, results in strain TMB 3423, the mutation enables the yeast for anaerobic growth on xylose displayed higher aerobic growth rates
-
K21A/N272D
catalytic efficiency is almost 9fold that of the K21A mutant and 2fold that of the wild-type enzyme. Strong preference for NADH over NADPH
K270M
-
mutation results in a significant increase in the Km values for both NADPH and NADH. The kinetic parameters for the NADH-linked reaction catalyzed by the K270M mutant could not even be determined since this mutant could not be saturated with NADH
K270R
-
mutation increases the Km value for NADPH 25fold, while the Km for NADH only increased two-fold
K270S/N272P/S271G/R276F
-
the mutant shows a 25fold preference toward NADH over NADPH by a factor of about 13fold, or an improvement of about 42fold, as measured by the ratio of the specificity constant kcat/Km coenzyme. Compared with the wild-type, the kcat(NADH) is slightly lower, while the kcat(NADPH) decreases by a factor of about 10
K274G
mutant shows an increase in NADH versus NADPH selectivity with only modest alterations of the original NADH-linked xylose specificity and catalytic-centre activity
K274M
mutant shows an increase in NADH versus NADPH selectivity with only modest alterations of the original NADH-linked xylose specificity and catalytic-centre activity
K274R
mutant shows an increase in NADH versus NADPH selectivity with only modest alterations of the original NADH-linked xylose specificity and catalytic-centre activity
K274R/N276D
mutant shows an increase in NADH versus NADPH selectivity with only modest alterations of the original NADH-linked xylose specificity and catalytic-centre activity. Mutant exhibits a 5fold preference for NADH over NADPH
N276D
mutant shows an increase in NADH versus NADPH selectivity with only modest alterations of the original NADH-linked xylose specificity and catalytic-centre activity
R280H
mutant shows an increase in NADH versus NADPH selectivity with only modest alterations of the original NADH-linked xylose specificity and catalytic-centre activity
S275A
mutant shows an increase in NADH versus NADPH selectivity with only modest alterations of the original NADH-linked xylose specificity and catalytic-centre activity
additional information
C36Y
about 2fold increase in activity. The ratios of NADH-linked and NADPH-linked activities are changed from 1.92 to 1.30
C36Y
-
about 2fold increase in activity. The ratios of NADH-linked and NADPH-linked activities are changed from 1.92 to 1.30
-
K271R/N273D
in the double mutant, affinity for NADPH decreases 3.1fold, while affinity for NADH remains relatively unchanged in comparison with the wild-type enzyme. The turnover number increases 1.6fold for the double mutant with NADH and decreases 3.2fold with NADPH relative to the wild-type enzyme. As a consequence, the catalytic efficiency of the double mutant (kcat/Km) increases 1.4fold with NADH and decreases 10.8fold with NADPH relative to the wild-type enzyme. Using the specificity constant (kcat/Km (NADH)/kcat/Km(NADPH)) the coenzyme preference for NADH is improved 16fold in the TeXR K271R/N273D double-mutant enzyme
K271R/N273D
catalytic efficiency of the double mutant increases 1.4fold with NADH and decreases 10.8fold with NADPH relative to the wild-type enzyme
additional information
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xylitol production is increased by expression of codon-optimized Neurospora crassa xylose reductase gene under control of a constitutive glyceraldehyde-3-phosphate dehydrogenase promoter in a Candida tropicalis xylitol dehydrogenase gene (XYL2)-disrupted strain resulting in recombinant strain LNG2, overview
additional information
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xylitol production is increased by expression of codon-optimized Neurospora crassa xylose reductase gene under control of a constitutive glyceraldehyde-3-phosphate dehydrogenase promoter in a Candida tropicalis xylitol dehydrogenase gene (XYL2)-disrupted strain resulting in recombinant strain LNG2, overview
-
additional information
simultaneous optimization of xylose reductase activity and stability using statistical methods is effective as compared to optimisation of the parameters separately, effects of pH and temperature on the activity and stability of xylose reductase from Debaryomyces nepalensis NCYC 3413 are investigated by enzyme assays, and independent variables are optimised using surface response methodology. Enzyme activity and stability are optimised separately and concurrently to decipher the appropriate conditions, method comparisons, overview. Optimized conditions are pH 7.1 and 27°C with predicted responses of specific activity of 72.3 U/mg and half-life time of 566 min. The experimental values (specific activity 50.2 U/mg, half-life time 818 min) are on par with predicted values indicating the significance of the model
additional information
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simultaneous optimization of xylose reductase activity and stability using statistical methods is effective as compared to optimisation of the parameters separately, effects of pH and temperature on the activity and stability of xylose reductase from Debaryomyces nepalensis NCYC 3413 are investigated by enzyme assays, and independent variables are optimised using surface response methodology. Enzyme activity and stability are optimised separately and concurrently to decipher the appropriate conditions, method comparisons, overview. Optimized conditions are pH 7.1 and 27°C with predicted responses of specific activity of 72.3 U/mg and half-life time of 566 min. The experimental values (specific activity 50.2 U/mg, half-life time 818 min) are on par with predicted values indicating the significance of the model
-
additional information
construction of the engineered Kluyveromyces marxianus strain 17555-JBP2 by random multi-copy integration of the mutated KmXYL1 gene exhibits two more copies of mKmXY1 genes and a 9.63fold elevation in transcription of NAD(P)H-dependent XR, optimization of bioreactor fermentation conditions (agitation speed), high-temperature (40°C) xylitol productivity of strain 17555-JBP2, which then shows an 81% improvement relative to the parental strain. Method development and optimization, overview
additional information
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construction of the engineered Kluyveromyces marxianus strain 17555-JBP2 by random multi-copy integration of the mutated KmXYL1 gene exhibits two more copies of mKmXY1 genes and a 9.63fold elevation in transcription of NAD(P)H-dependent XR, optimization of bioreactor fermentation conditions (agitation speed), high-temperature (40°C) xylitol productivity of strain 17555-JBP2, which then shows an 81% improvement relative to the parental strain. Method development and optimization, overview
additional information
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construction of the engineered Kluyveromyces marxianus strain 17555-JBP2 by random multi-copy integration of the mutated KmXYL1 gene exhibits two more copies of mKmXY1 genes and a 9.63fold elevation in transcription of NAD(P)H-dependent XR, optimization of bioreactor fermentation conditions (agitation speed), high-temperature (40°C) xylitol productivity of strain 17555-JBP2, which then shows an 81% improvement relative to the parental strain. Method development and optimization, overview
-
additional information
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construction of the engineered Kluyveromyces marxianus strain 17555-JBP2 by random multi-copy integration of the mutated KmXYL1 gene exhibits two more copies of mKmXY1 genes and a 9.63fold elevation in transcription of NAD(P)H-dependent XR, optimization of bioreactor fermentation conditions (agitation speed), high-temperature (40°C) xylitol productivity of strain 17555-JBP2, which then shows an 81% improvement relative to the parental strain. Method development and optimization, overview
-
additional information
-
construction of the engineered Kluyveromyces marxianus strain 17555-JBP2 by random multi-copy integration of the mutated KmXYL1 gene exhibits two more copies of mKmXY1 genes and a 9.63fold elevation in transcription of NAD(P)H-dependent XR, optimization of bioreactor fermentation conditions (agitation speed), high-temperature (40°C) xylitol productivity of strain 17555-JBP2, which then shows an 81% improvement relative to the parental strain. Method development and optimization, overview
-
additional information
recombinant enzyme expression in Pichia pastoris, coexpression with Bacillus subtilis gene gdh
additional information
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recombinant enzyme expression in Pichia pastoris, coexpression with Bacillus subtilis gene gdh
-
additional information
-
recombinant enzyme expression in Pichia pastoris, coexpression with Bacillus subtilis gene gdh
-
additional information
-
recombinant enzyme expression in Pichia pastoris, coexpression with Bacillus subtilis gene gdh
-
additional information
-
recombinant enzyme expression in Pichia pastoris, coexpression with Bacillus subtilis gene gdh
-
additional information
-
recombinant enzyme expression in Pichia pastoris, coexpression with Bacillus subtilis gene gdh
-
additional information
cells of recombinant Escherichia coli strain BL21(DE3)/pCDFDuet-1-XR-GDH coexpressing xylose reductase (XR) and glucose dehydrogenase (GDH) are immobilized and applied for the production of xylitol from xylose mother liquor (XML). Various immobilization methods are screened and the cross-linking approach with diatomite and polyetherimide as the raw materials and glutaraldehyde as the cross-linking agent is the optimal one, and the recovery activity reached of 80.3% after immobilization. The half-life of immobilized cells is 1.52times to that of free cells. Batch experiments show that the enzyme activity of immobilized cells remains 70.5% of initial activity after 10 batches and the space-time yield of xylitol reaches of 11.5 g/l/h. Method development and optimization, overview
additional information
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coenzyme specificities of the NADPH-preferring xylose reductase and the NAD+-dependent xylitol dehydrogenase, EC 1.1.1.9, 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 improved performance in xylose fermentation
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, XYL2 (EC 1.1.1.9), 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
enhanced production of xylitol from xylose by expression of Bacillus subtilis arabinose:H+ symporter and Scheffersomyces stipitis xylose reductase in recombinant Saccharomyces cerevisiae
additional information
recombinant enzyme expression in differently engineered Saccharomyces cerevisiae strains SCF201 and SCF202, aerobic or anaerobic batch fermentation cultures, measurement of xylitol consumption and ethanol production, analysis of culture condition effects, overview
additional information
recombinant enzyme expression in Pichia pastoris, coexpression with Bacillus subtilis gene gdh, the biotransformation is very efficient with as high as 80% w/w conversion within two hours. The whole cells can be reused for multiple rounds of catalysis without loss of activity. The cells can directly transform D-xylose in a non-detoxified hemicelluloses hydrolysate to xylitol at 70% w/w yield. Recombinant Pichia pastoris expressing xylose reductase could transform D-xylose, either in pure form or in crude hemicelluloses hydrolysate, to bio-xylitol very efficiently. This biocatalytic reaction happens without the external addition of any NAD(P)H, NAD(P)+, and auxiliary substrate as an electron donor. PsXYL1 in the cells is not inhibited by D-xylose up to 1.5 M. About 320 mM xylitol is produced from 400 mM D-xylose (80% conversion), 535 mM xylitol from 750 mM D-xylose (71% conversion), but only about 750 mM xylitol from 1.5 M D-xylose (50% conversion). The reaction with 1.5 M of D-xylose should not be limited by NAD+ since the cells are not recycled
additional information
xylitol is produced from lignocellulosic biomass by a recombinant strain of Saccharomyces cerevisiae strain YPH499-SsXR-AaBGL expressing cytosolic Scheffersomyces stipitis xylose reductase (SsXR), along with Aspergillus aculeatus beta-glucosidase 1 (AaBGL) displayed on the cell surface. The simultaneous co-fermentation of cellobiose/xylose by this strain leads to an about 2.5fold increase in xylitol/xylose ratio compared to the use of a glucose/xylose mixture as a substrate. Further improvement in the xylose uptake by the cell is achieved by a broad evaluation of several homologous and heterologous transporters. Homologous maltose transporter (ScMAL11) shows the best performance in xylose transport and is used to generate the strain YPH499-XRScMAL11-BGL with a significantly improved xylitol production capacity from cellobiose/xylose co-utilization. Method evaluation and optimization, overview
additional information
xylose isomerase (XI, EC 5.3.1.5) and xylose reductase/xylitol dehydrogenase (XR/XDH) pathways are used to confer xylose assimilation capacity to Saccharomyces cerevisiae for achievement of economically viable lignocellulosic ethanol production. XI and/or XR/XDH pathways are introduced into two robust industrial Saccharomyces cerevisiae strains, evaluated in synthetic media and corn cob hemicellulosic hydrolysate, and the results are correlated with the differential enzyme activities found in the xylose-pathway engineered strains. 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. 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%. An advantage of using the XI from Clostridium phytofermentans to attain high ethanol productivities and yields from xylose is proven
additional information
-
recombinant enzyme expression in differently engineered Saccharomyces cerevisiae strains SCF201 and SCF202, aerobic or anaerobic batch fermentation cultures, measurement of xylitol consumption and ethanol production, analysis of culture condition effects, overview
-
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, XYL2 (EC 1.1.1.9), 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
-
xylitol is produced from lignocellulosic biomass by a recombinant strain of Saccharomyces cerevisiae strain YPH499-SsXR-AaBGL expressing cytosolic Scheffersomyces stipitis xylose reductase (SsXR), along with Aspergillus aculeatus beta-glucosidase 1 (AaBGL) displayed on the cell surface. The simultaneous co-fermentation of cellobiose/xylose by this strain leads to an about 2.5fold increase in xylitol/xylose ratio compared to the use of a glucose/xylose mixture as a substrate. Further improvement in the xylose uptake by the cell is achieved by a broad evaluation of several homologous and heterologous transporters. Homologous maltose transporter (ScMAL11) shows the best performance in xylose transport and is used to generate the strain YPH499-XRScMAL11-BGL with a significantly improved xylitol production capacity from cellobiose/xylose co-utilization. Method evaluation and optimization, overview
-
additional information
-
enhanced production of xylitol from xylose by expression of Bacillus subtilis arabinose:H+ symporter and Scheffersomyces stipitis xylose reductase in recombinant Saccharomyces cerevisiae
-
additional information
-
recombinant enzyme expression in Pichia pastoris, coexpression with Bacillus subtilis gene gdh, the biotransformation is very efficient with as high as 80% w/w conversion within two hours. The whole cells can be reused for multiple rounds of catalysis without loss of activity. The cells can directly transform D-xylose in a non-detoxified hemicelluloses hydrolysate to xylitol at 70% w/w yield. Recombinant Pichia pastoris expressing xylose reductase could transform D-xylose, either in pure form or in crude hemicelluloses hydrolysate, to bio-xylitol very efficiently. This biocatalytic reaction happens without the external addition of any NAD(P)H, NAD(P)+, and auxiliary substrate as an electron donor. PsXYL1 in the cells is not inhibited by D-xylose up to 1.5 M. About 320 mM xylitol is produced from 400 mM D-xylose (80% conversion), 535 mM xylitol from 750 mM D-xylose (71% conversion), but only about 750 mM xylitol from 1.5 M D-xylose (50% conversion). The reaction with 1.5 M of D-xylose should not be limited by NAD+ since the cells are not recycled
-
additional information
-
xylose isomerase (XI, EC 5.3.1.5) and xylose reductase/xylitol dehydrogenase (XR/XDH) pathways are used to confer xylose assimilation capacity to Saccharomyces cerevisiae for achievement of economically viable lignocellulosic ethanol production. XI and/or XR/XDH pathways are introduced into two robust industrial Saccharomyces cerevisiae strains, evaluated in synthetic media and corn cob hemicellulosic hydrolysate, and the results are correlated with the differential enzyme activities found in the xylose-pathway engineered strains. 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. 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%. An advantage of using the XI from Clostridium phytofermentans to attain high ethanol productivities and yields from xylose is proven
-
additional information
-
recombinant enzyme expression in differently engineered Saccharomyces cerevisiae strains SCF201 and SCF202, aerobic or anaerobic batch fermentation cultures, measurement of xylitol consumption and ethanol production, analysis of culture condition effects, overview
-
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, XYL2 (EC 1.1.1.9), 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
-
xylitol is produced from lignocellulosic biomass by a recombinant strain of Saccharomyces cerevisiae strain YPH499-SsXR-AaBGL expressing cytosolic Scheffersomyces stipitis xylose reductase (SsXR), along with Aspergillus aculeatus beta-glucosidase 1 (AaBGL) displayed on the cell surface. The simultaneous co-fermentation of cellobiose/xylose by this strain leads to an about 2.5fold increase in xylitol/xylose ratio compared to the use of a glucose/xylose mixture as a substrate. Further improvement in the xylose uptake by the cell is achieved by a broad evaluation of several homologous and heterologous transporters. Homologous maltose transporter (ScMAL11) shows the best performance in xylose transport and is used to generate the strain YPH499-XRScMAL11-BGL with a significantly improved xylitol production capacity from cellobiose/xylose co-utilization. Method evaluation and optimization, overview
-
additional information
-
enhanced production of xylitol from xylose by expression of Bacillus subtilis arabinose:H+ symporter and Scheffersomyces stipitis xylose reductase in recombinant Saccharomyces cerevisiae
-
additional information
-
recombinant enzyme expression in Pichia pastoris, coexpression with Bacillus subtilis gene gdh, the biotransformation is very efficient with as high as 80% w/w conversion within two hours. The whole cells can be reused for multiple rounds of catalysis without loss of activity. The cells can directly transform D-xylose in a non-detoxified hemicelluloses hydrolysate to xylitol at 70% w/w yield. Recombinant Pichia pastoris expressing xylose reductase could transform D-xylose, either in pure form or in crude hemicelluloses hydrolysate, to bio-xylitol very efficiently. This biocatalytic reaction happens without the external addition of any NAD(P)H, NAD(P)+, and auxiliary substrate as an electron donor. PsXYL1 in the cells is not inhibited by D-xylose up to 1.5 M. About 320 mM xylitol is produced from 400 mM D-xylose (80% conversion), 535 mM xylitol from 750 mM D-xylose (71% conversion), but only about 750 mM xylitol from 1.5 M D-xylose (50% conversion). The reaction with 1.5 M of D-xylose should not be limited by NAD+ since the cells are not recycled
-
additional information
-
xylose isomerase (XI, EC 5.3.1.5) and xylose reductase/xylitol dehydrogenase (XR/XDH) pathways are used to confer xylose assimilation capacity to Saccharomyces cerevisiae for achievement of economically viable lignocellulosic ethanol production. XI and/or XR/XDH pathways are introduced into two robust industrial Saccharomyces cerevisiae strains, evaluated in synthetic media and corn cob hemicellulosic hydrolysate, and the results are correlated with the differential enzyme activities found in the xylose-pathway engineered strains. 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. 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%. An advantage of using the XI from Clostridium phytofermentans to attain high ethanol productivities and yields from xylose is proven
-
additional information
-
recombinant enzyme expression in differently engineered Saccharomyces cerevisiae strains SCF201 and SCF202, aerobic or anaerobic batch fermentation cultures, measurement of xylitol consumption and ethanol production, analysis of culture condition effects, overview
-
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, XYL2 (EC 1.1.1.9), 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
-
xylitol is produced from lignocellulosic biomass by a recombinant strain of Saccharomyces cerevisiae strain YPH499-SsXR-AaBGL expressing cytosolic Scheffersomyces stipitis xylose reductase (SsXR), along with Aspergillus aculeatus beta-glucosidase 1 (AaBGL) displayed on the cell surface. The simultaneous co-fermentation of cellobiose/xylose by this strain leads to an about 2.5fold increase in xylitol/xylose ratio compared to the use of a glucose/xylose mixture as a substrate. Further improvement in the xylose uptake by the cell is achieved by a broad evaluation of several homologous and heterologous transporters. Homologous maltose transporter (ScMAL11) shows the best performance in xylose transport and is used to generate the strain YPH499-XRScMAL11-BGL with a significantly improved xylitol production capacity from cellobiose/xylose co-utilization. Method evaluation and optimization, overview
-
additional information
-
enhanced production of xylitol from xylose by expression of Bacillus subtilis arabinose:H+ symporter and Scheffersomyces stipitis xylose reductase in recombinant Saccharomyces cerevisiae
-
additional information
-
recombinant enzyme expression in Pichia pastoris, coexpression with Bacillus subtilis gene gdh, the biotransformation is very efficient with as high as 80% w/w conversion within two hours. The whole cells can be reused for multiple rounds of catalysis without loss of activity. The cells can directly transform D-xylose in a non-detoxified hemicelluloses hydrolysate to xylitol at 70% w/w yield. Recombinant Pichia pastoris expressing xylose reductase could transform D-xylose, either in pure form or in crude hemicelluloses hydrolysate, to bio-xylitol very efficiently. This biocatalytic reaction happens without the external addition of any NAD(P)H, NAD(P)+, and auxiliary substrate as an electron donor. PsXYL1 in the cells is not inhibited by D-xylose up to 1.5 M. About 320 mM xylitol is produced from 400 mM D-xylose (80% conversion), 535 mM xylitol from 750 mM D-xylose (71% conversion), but only about 750 mM xylitol from 1.5 M D-xylose (50% conversion). The reaction with 1.5 M of D-xylose should not be limited by NAD+ since the cells are not recycled
-
additional information
-
xylose isomerase (XI, EC 5.3.1.5) and xylose reductase/xylitol dehydrogenase (XR/XDH) pathways are used to confer xylose assimilation capacity to Saccharomyces cerevisiae for achievement of economically viable lignocellulosic ethanol production. XI and/or XR/XDH pathways are introduced into two robust industrial Saccharomyces cerevisiae strains, evaluated in synthetic media and corn cob hemicellulosic hydrolysate, and the results are correlated with the differential enzyme activities found in the xylose-pathway engineered strains. 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. 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%. An advantage of using the XI from Clostridium phytofermentans to attain high ethanol productivities and yields from xylose is proven
-
additional information
-
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 arborariae 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
Spathaspora arborariae UFMG-HM.19.1AT
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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 arborariae 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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 8
-
below pH 5 and above pH 8.0 the enzyme is inactivated within 3-6 days
286260
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
Thermochaetoides thermophila
purified recombinant His-tagged enzyme, no loss of activity after 3 h at 30°C
55 - 75
Thermochaetoides thermophila
purified recombinant His-tagged enzyme, half-lifes are 1.8 min at 55°C, 4.2 s at 65°C, and 2.8 s at 75°C, respectively
60
additional information
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non-ionic detergents and bovine serum albumin stabilize the enzyme to a significant extent during long-term incubation at 25°C, 30°C or 38°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable enzyme at 25°C in phosphate and Tris buffer of various ionic strengths between pH 6.0 and 7.0
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, immobilized cells highly retain activity compared to free cells after storage for 20 days at 30°C. The immobilized cells maintain over 50% of their original activity after storage for 20 days at 4°C, while the catalytic activity of free cells decreases to approximately 50% after storage for 12 days at 4°C and to 30% after storage for 20 days at 4°C
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
recombinant His-tagged enzyme 25.5fold from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration to near homogeneity
Thermochaetoides thermophila
yeast cell extract is fractionated by biomimetic chromatography using the dye HE-3B (reactive Red 120) as pseudoaffinity ligand coupled to Sepharose CL-4B. In the second step, high-resolution anion-exchange chromatography using Mono Q yields purified isoform ALR2 in overall yieldof 62%
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 (DE3), subloned into the pYES2 vector and transformed into Saccharomyces cerevisiae W303-1A
expression in Escherichia coli
expression in Escherichia coli as a His6-tagged fusion protein in high yield
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expression of histidine-tagged wild type Texr and mutant Texr K271R/N273D in Escherichia coli BL21-Star DE3
expression of single-site mutant xylose reductase from Candida tenuis (CtXR (K274R)) results in recombinant Corynebacterium glutamicum strain CtXR4 that produces 26.5 g/l xylitol at 3.1 g/l*h. To eliminate possible formation of toxic intracellular xylitol phosphate, genes encoding xylulokinase (XylB) and phosphoenolpyruvate-dependent fructose phosphotransferase (PTSfru) are disrupted to yield strain CtXR7
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functional recombinant co-expression of xylose reductase (XR) from Rhizopus oryzae and glucose dehydrogenase (GDH) from Exiguobacterium sibiricum in Escherichia coli strain BL21(DE3)
gene SpXYL1.1, recombinant expression of the enzyme in Saccharomyces cerevisiae strain CEN.PK2-1C (MATa leu2-3112 ura3-52 trp1-289 his3-DELTA1 MAL2-8c SUC2), subcloning in Escherichia coli strain DH5alpha, co-expression with xylitol dehydrogenase from Spathaspora passalidarum strain UFMG-CM-Y474
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gene xr, recombinant enzyme expression in Pichia pastoris strain GS115, coexpression with Bacillus subtilis gene gdh
gene xyl1, random multi-copy integration of the mutated KmXYL1 (mKmXYL1) gene is carried out using thermotolerant yeast Kluyveromyces marxianus strain KCTC17555DELTAURA3, in order to enhance xylitol production. After multi-copy integration, the highest xylitol producing strain is isolated and named Kluyveromyces marxianus 17555-JBP2. This strain exhibits 440% higher xylitol production than the parental strain at 30°C. Quantitative real-time PCR and transcriptome analysis demonstrate that, relative to the parent strain, Kluyveromyces marxianus strain 17555-JBP2 exhibits two more copies of mKmXY1 genes and a 9.63fold elevation in transcription of NAD(P)H-dependent XR
gene xyl1, recombinant enzyme expression in Pichia pastoris strain GS115, coexpression with Bacillus subtilis gene gdh
gene xyl1, recombinant enzyme expression in Saccharomyces cerevisiae strain CA11, isolated from Brazilian cachaca fermentation processes, co-expression with XDH, and xylA gene from Clostridium phytofermentans encoding xylose isomerase
gene xyl1, recombinant enzyme expression in Saccharomyces cerevisiae, different NAM34-4C (MATalpha) strain derivatives' genotypes and phenotypes, e.g. transformants of SCB38 with kanMX DNA or XM1, overview. XM1 is the DNA fragment carrying the genetic structure TDH3p-XYL1-TDH3t-TDH3p-XYL2-TDH3t-TDH3p-XKS1-TDH3t, including TDH3 promoter, TDH3 terminator, Scheffersomyces (Pichia) stipitis genes XYL1 (encoding NAD(P)H-dependent xylose reductase) and XYL2 (encoding NAD+-dependent xylitol dehydrogenase), and the endogenous XKS1 (encoding the Saccharomyces cerevisiae xylulokinase)
gene xyl1, recombinant expression of Xyl1 in Saccharomyces cerevisiae strain YPH499, co-expression with Aspergillus aculeatus beta-glucosidase 1 (AaBGL) and endogenous maltose transporter ScMAL11
gene xyl1, the xylose-metabolic gene XYL1 from Scheffersomyces stipitis are introduced into Saccharomyces cerevisiae
gene, recombinant expression in Saccharomyces cerevisiae strains D452-2 or EBY.VW4000, coexpression with Bacillus subtilis arabinose:H+ symporter (AraE). AraE and XYL1 expression leads to 18fold higher xylitol production compared to control strain D452-2, AraE takes up xylose efficiently and gives the engineered Saccharomyces cerevisiae strain DXXA high xylitol productivity, while the yeast wild-type shows an inefficient transport of xylose. Method optimization, overview
recombinant expression of C-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
Thermochaetoides thermophila
the cofactor preference of Pichia stipitis xylose reductase is altered by site-directed mutagenesis. When the K270R xylose reductase is combined with a metabolic engineering strategy that ensures high xylose utilization capabilities, a recombinant Saccharomyces cerevisiae strain is created that provides a unique combination of high xylose consumption rate, high ethanol yield and low xylitol yield during ethanolic xylose fermentation
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
D-xylose uptake induces the enzyme, together with the NADP+-linked xylitol dehydrogenase, EC 1.1.1.10
formation of xylose reductase in the yeast Candida tropicalis is significantly repressed in cells grown on medium that contains glucose as carbon and energy source, because of the repressive effect of glucose
induction by presence of D-xylose in culture medium
D-xylose uptake induces the enzyme, together with the NADP+-linked xylitol dehydrogenase, EC 1.1.1.10
-
D-xylose uptake induces the enzyme, together with the NADP+-linked xylitol dehydrogenase, EC 1.1.1.10
-
-
formation of xylose reductase in the yeast Candida tropicalis is significantly repressed in cells grown on medium that contains glucose as carbon and energy source, because of the repressive effect of glucose
-
formation of xylose reductase in the yeast Candida tropicalis is significantly repressed in cells grown on medium that contains glucose as carbon and energy source, because of the repressive effect of glucose
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
denaturation buffers of either pH 6.0 or 8.0, containing urea in concentrations of 2, 4, 6, and 8 M, are used and analysed in SDS-PAGE. Optimal solvation of the XylR giving the lowest background of Escherichia coli proteins is performed with 4 M urea at pH 8.0. For renaturation, a set of buffers containing 0, 0.1, 0.5, 1 and 1.5 mM glutathione (red:ox = 1:1) at pH values of 5.0, 6.0, 7.0, and 8.0 are tested. Refolding occurrs at 8°C and its progress is analysed by assaying the volumetric activity in the respective buffers. Best renaturation results are obtained in a 20 mM Tris/HCl buffer at pH 7.0 without glutathione. After 4 days about 70% of the activity of the XylR is recovered. Buffers at pH 8.0 work slightly less efficient compared to that of pH 7.0. At pH 5.0 and 6.0 refolding is drastically reduced. Increasing concentrations of glutathione do not improve renaturation
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
D-xylose is the second most abundant renewable sugar in nature, and its fermentation to ethanol has great economical potential. Unfortunately, Saccharomyces cerevisiae, which has been optimized for ethanol production, cannot utilize xylose efficiently, while D-xylulose, an isomerization product of D-xylose, can be assimilated. A major strategy for constructing xylose-fermenting Saccharomyces cerevisiae is to introduce genes involved in xylose metabolism from other organisms. Xylose reductase and xylitol dehydrogenase (EC 1.1.1.9) from the xylose-fermenting yeast Pichia stipitis are cloned into Saccharomyces cerevisiae to allow xylose fermentation to ethanol. In this case, xylose is converted into xylulose by the sequential actions of two oxidoreductases. First, Pichia stipitis xylose reductase catalyses the reduction of xylose into xylitol with NAD(P)H as co-substrate. Xylitol is then oxidized by PsXDH (Pichia stipitis xylitol dehydrogenase) which uses NAD+ exclusively as co-substrate to yield xylulose. The different coenzyme specificity of the two enzymes xylose reductase and xylitol dehydrogenase, however, creates an intracellular redox imbalance, which results in low ethanol yields and considerable xylitol by-product formation. A mutant is constructed that shows an altered active site that is more unfavorable for NADPH than NADH in terms of both Km and kcat. There are potentials for application of the mutant (K270S/N272P/S271G/R276F) in constructing a more balanced xylose reductase/xylitol dehydrogenase pathway in recombinant xylose-fermenting Saccharomyces cerevisiae strains
synthesis
-
the cofactor preference of Pichia stipitis xylose reductase is altered by site-directed mutagenesis. When the K270R xylose reductase is combined with a metabolic engineering strategy that ensures high xylose utilization capabilities, a recombinant Saccharomyces cerevisiae strain is created that provides a unique combination of high xylose consumption rate, high ethanol yield and low xylitol yield during ethanolic xylose fermentation
synthesis
-
this enzyme is one of the most active xylose reductases and may be used for the in vitro production of xylitol
synthesis
-
expression in Candida glycerinogenes WL2002-5, the recombinant strain produces xylitol from D-xylose using glycerol as a cosubstrate for cell growth and NAD (P) H regeneration. 100 g/L D-xylose is completely converted into xylitol when at least 20 g/l glycerol is used as a co-substrate. The strain accumulates 2.1fold increased xylitol concentration over those cells grown on glucose as co-substrate, with a volumetric productivity of 0.83 g/l/h, and a xylitol yield of 98% xylose
synthesis
-
the microalga Chlorella sorokiniana and provide a target for genetic engineering to improve D-xylose utilization for microalgal lipid production
synthesis
production of bio-xylitol from D-xylose by an engineered Pichia pastoris expressing a recombinant xylose reductase
synthesis
the enzyme can be used for industrial production of xylitol from waste xylose mother liquor. Production of xylitol from xylose mother liquor by immobilized Escherichia coli cells containing xylose reductase and glucose dehydrogenase, overview. The immobilization of Escherichia coli strain BL21(DE3)/ pCDFDuet-1-XR-GDH cells results in an increase of storage stability which can expand its potential applications in industries
synthesis
Escherichia coli expressing XylA synthesizes 13.3 g/l of xylitol during 20 h of cultivation, when D-xylose (50 g/l) and D-glucose (5 g/l) are added to IPTG-induced cells
synthesis
-
the microalga Chlorella sorokiniana and provide a target for genetic engineering to improve D-xylose utilization for microalgal lipid production
-
synthesis
-
production of bio-xylitol from D-xylose by an engineered Pichia pastoris expressing a recombinant xylose reductase
-
synthesis
-
production of bio-xylitol from D-xylose by an engineered Pichia pastoris expressing a recombinant xylose reductase
-
synthesis
-
production of bio-xylitol from D-xylose by an engineered Pichia pastoris expressing a recombinant xylose reductase
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Neuhauser, W.; Haltrich, D.; Kulbe, K.D.; Nidetzky, B.
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brenda
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Verduyn, C.; van Kleef, R.; Frank, J.; Schreuder, H.; van Dijken, J.P.; Scheffers, W.A.
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Biotechnol. Biofuels
2
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Scheffersomyces stipitis
brenda
Fernandes, S.; Tuohy, M.G.; Murray, P.G.
Xylose reductase from the thermophilic fungus Talaromyces emersonii: cloning and heterologous expression of the native gene (Texr) and a double mutant (TexrK271R + N273D) with altered coenzyme specificity
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34
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Rasamsonia emersonii (C5J3R6)
brenda
Gurpilhares, D.B.; Hasmann, F.A.; Pessoa, A.; Roberto, I.C.
The behavior of key enzymes of xylose metabolism on the xylitol production by Candida guilliermondii grown in hemicellulosic hydrolysate
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36
87-93
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Meyerozyma guilliermondii
brenda
Zhang, F.; Qiao, D.; Xu, H.; Liao, C.; Li, S.; Cao, Y.
Cloning, expression, and characterization of xylose reductase with higher activity from Candida tropicalis
J. Microbiol.
47
351-357
2009
Candida tropicalis (A9QVV8), Candida tropicalis SCTCC 300249 (A9QVV8)
brenda
Liang, L.; Zhang, J.; Lin, Z.
Altering coenzyme specificity of Pichia stipitis xylose reductase by the semi-rational approach CASTing
Microb. Cell Fact.
6
36
2007
Scheffersomyces stipitis
brenda
Zeng, Q.K.; Du, H.L.; Wang, J.F.; Wei, D.Q.; Wang, X.N.; Li, Y.X.; Lin, Y.
Reversal of coenzyme specificity and improvement of catalytic efficiency of Pichia stipitis xylose reductase by rational site-directed mutagenesis
Biotechnol. Lett.
31
1025-1029
2009
Scheffersomyces stipitis (P31867)
brenda
Runquist, D.; Hahn-Haegerdal, B.; Bettiga, M.
Increased ethanol productivity in xylose-utilizing Saccharomyces cerevisiae via a randomly mutagenized xylose reductase
Appl. Environ. Microbiol.
76
7796-7802
2010
Saccharomyces cerevisiae, Saccharomyces cerevisiae TMB 3420
brenda
Jeon, W.Y.; Yoon, B.H.; Ko, B.S.; Shim, W.Y.; Kim, J.H.
Xylitol production is increased by expression of codon-optimized Neurospora crassa xylose reductase gene in Candida tropicalis
Bioprocess Biosyst. Eng.
35
191-198
2012
Candida tropicalis, Candida tropicalis ATCC 20336
brenda
Krahulec, S.; Klimacek, M.; Nidetzky, B.
Analysis and prediction of the physiological effects of altered coenzyme specificity in xylose reductase and xylitol dehydrogenase during xylose fermentation by Saccharomyces cerevisiae
J. Biotechnol.
158
192-202
2012
Saccharomyces cerevisiae
brenda
Bolotnikova, O.; Meshcheryakova, O.; Mikhailova, N.; Ginak, A.
Metabolic properties of Pachysolen tannophilus mutants producing xylitol and ethanol from D-xylose
Microbiology
84
485-490
2015
Pachysolen tannophilus, Pachysolen tannophilus 22-Y-1532
-
brenda
Zhang, C.; Zong, H.; Zhuge, B.; Lu, X.; Fang, H.; Zhuge, J.
Production of xylitol from D-xylose by overexpression of xylose reductase in osmotolerant yeast Candida glycerinogenes WL2002-5
Appl. Biochem. Biotechnol.
176
1511-1527
2015
Scheffersomyces stipitis
brenda
Kim, J.S.; Park, J.B.; Jang, S.W.; Ha, S.J.
Enhanced xylitol production by mutant Kluyveromyces marxianus 36907-FMEL1 due to improved xylose reductase activity
Appl. Biochem. Biotechnol.
176
1975-1984
2015
Kluyveromyces marxianus (A0A0H3Y829), Kluyveromyces marxianus, Kluyveromyces marxianus ATCC 36907 (A0A0H3Y829), Kluyveromyces marxianus ATCC 36907
brenda
Zheng, Y.; Yu, X.; Li, T.; Xiong, X.; Chen, S.
Induction of D-xylose uptake and expression of NAD(P)H-linked xylose reductase and NADP+-linked xylitol dehydrogenase in the oleaginous microalga Chlorella sorokiniana
Biotechnol. Biofuels
7
125
2014
Chlorella sorokiniana, Chlorella sorokiniana UTEX 1602
brenda
Tani, T.; Taguchi, H.; Akamatsu, T.
Analysis of metabolisms and transports of xylitol using xylose- and xylitol-assimilating Saccharomyces cerevisiae
J. Biosci. Bioeng.
123
613-620
2017
Scheffersomyces stipitis (P31867), Scheffersomyces stipitis NRRL Y-11545 (P31867), Scheffersomyces stipitis NBRC 10063 (P31867), Scheffersomyces stipitis ATCC 58785 (P31867)
brenda
Park, J.B.; Kim, J.S.; Kweon, D.H.; Kweon, D.H.; Seo, J.H.; Ha, S.J.
Overexpression of endogenous xylose reductase enhanced xylitol productivity at 40C by thermotolerant yeast Kluyveromyces marxianus
Appl. Biochem. Biotechnol.
189
459-470
2019
Kluyveromyces marxianus (W0T4K1), Kluyveromyces marxianus, Kluyveromyces marxianus NBRC 104275 (W0T4K1), Kluyveromyces marxianus BCC 29191 (W0T4K1), Kluyveromyces marxianus DMKU3-1042 (W0T4K1)
brenda
Jo, J.H.; Park, Y.C.; Jin, Y.S.; Seo, J.H.
Construction of efficient xylose-fermenting Saccharomyces cerevisiae through a synthetic isozyme system of xylose reductase from Scheffersomyces stipitis
Biores. Technol.
241
88-94
2017
Scheffersomyces stipitis (P31867), Scheffersomyces stipitis NRRL Y-11545 (P31867), Scheffersomyces stipitis NBRC 10063 (P31867), Scheffersomyces stipitis ATCC 58785 (P31867)
brenda
Jin, L.Q.; Yang, B.; Xu, W.; Chen, X.X.; Jia, D.X.; Liu, Z.Q.; Zheng, Y.G.
Immobilization of recombinant Escherichia coli whole cells harboring xylose reductase and glucose dehydrogenase for xylitol production from xylose mother liquor
Biores. Technol.
285
121344
2019
Rhizopus arrhizus (W5RZ21)
brenda
Guirimand, G.G.Y.; Bamba, T.; Matsuda, M.; Inokuma, K.; Morita, K.; Kitada, Y.; Kobayashi, Y.; Yukawa, T.; Sasaki, K.; Ogino, C.; Hasunuma, T.; Kondo, A.
Combined cell surface display of beta-D-glucosidase (BGL), maltose transporter (MAL11), and overexpression of cytosolic xylose reductase (XR) in Saccharomyces cerevisiae enhance cellobiose/xylose coutilization for xylitol bioproduction from lignocellulosic B
Biotechnol. J.
14
e1800704
2019
Scheffersomyces stipitis (P31867), Scheffersomyces stipitis NRRL Y-11545 (P31867), Scheffersomyces stipitis NBRC 10063 (P31867), Scheffersomyces stipitis ATCC 58785 (P31867)
brenda
Kim, H.; Lee, H.S.; Park, H.; Lee, D.H.; Boles, E.; Chung, D.; Park, Y.C.
Enhanced production of xylitol from xylose by expression of Bacillus subtilis arabinose H+ symporter and Scheffersomyces stipitis xylose reductase in recombinant Saccharomyces cerevisiae
Enzyme Microb. Technol.
107
7-14
2017
Scheffersomyces stipitis (P31867), Scheffersomyces stipitis NRRL Y-11545 (P31867), Scheffersomyces stipitis NBRC 10063 (P31867), Scheffersomyces stipitis ATCC 58785 (P31867)
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
Fermentation
6
72
2020
Spathaspora arborariae, Spathaspora arborariae UFMG-HM.19.1AT
-
brenda
Quehenberger, J.; Reichenbach, T.; Baumann, N.; Rettenbacher, L.; Divne, C.; Spadiut, O.
Kinetics and predicted structure of a novel xylose reductase from Chaetomium thermophilum
Int. J. Mol. Sci.
20
185
2019
Thermochaetoides thermophila (G0SCE7), Thermochaetoides thermophila IMI 039719 (G0SCE7), Thermochaetoides thermophila DSM 1495 (G0SCE7), Thermochaetoides thermophila CBS 144.50 (G0SCE7)
brenda
Louie, T.M.; Louie, K.; DenHartog, S.; Gopishetty, S.; Subramanian, M.; Arnold, M.; Das, S.
Production of bio-xylitol from D-xylose by an engineered Pichia pastoris expressing a recombinant xylose reductase did not require any auxiliary substrate as electron donor
Microb. Cell Fact.
20
50
2021
Scheffersomyces stipitis (P31867), Neurospora crassa (Q7SD67), Neurospora crassa CBS 708.71 (Q7SD67), Neurospora crassa 74-OR23-1A (Q7SD67), Scheffersomyces stipitis NRRL Y-11545 (P31867), Scheffersomyces stipitis NBRC 10063 (P31867), Neurospora crassa DSM 1257 (Q7SD67), Neurospora crassa ATCC 24698 (Q7SD67), Scheffersomyces stipitis ATCC 58785 (P31867), Neurospora crassa FGSC 987 (Q7SD67)
brenda
Malla, S.; Gummadi, S.N.
Simultaneous optimization of activity and stability of xylose reductase from D. nepalensis NCYC 3413 using statistical experimental design
Protein Pept. Lett.
28
489-500
2020
Debaryomyces nepalensis (A0A0M4HL56), Debaryomyces nepalensis NCYC 3413 (A0A0M4HL56)
brenda
Arumugam, N.; Boobalan, T.; Saravanan, S.; Jothi Basu, M.; Arun, A.; Suganya Devi, T.; Kavitha, T.
In silico and in vitro comparison of nicotinamide adenine dinucleotide phosphate dependent xylose reductase Rossmann fold in Debaryomycetaceae yeast family
Biocatal. Agricult. Biotechnol.
24
101508
2020
Meyerozyma caribbica (A0A2Z4P5B1)
-
brenda
Nidetzky, B.; Mayr, P.; Hadwiger, P.; Stuetz, A.
Binding energy and specificity in the catalytic mechanism of yeast aldose reductases
Biochem. J.
344
101-107
1999
Yamadazyma tenuis, [Candida] intermedia (A0A1L0DQY1)
brenda
Petschacher, B.; Leitgeb, S.; Kavanagh, K.L.; Wilson, D.K.; Nidetzky, B.
The coenzyme specificity of Candida tenuis xylose reductase (AKR2B5) explored by site-directed mutagenesis and X-ray crystallography
Biochem. J.
385
75-83
2005
Yamadazyma tenuis (O74237)
brenda
Nidetzky, B.; Brueggler, K.; Kratzer, R.; Mayr, P.
Multiple forms of xylose reductase in Candida intermedia comparison of their functional properties using quantitative structure-activity relationships, steady-state kinetic analysis, and pH studies
J. Agric. Food Chem.
51
7930-7935
2003
[Candida] intermedia
brenda
Suzuki, T.; Yokoyama, S.; Kinoshita, Y.; Yamada, H.; Hatsu, M.; Takamizawa, K.; Kawai, K.
Expression of xyrA gene encoding for D-xylose reductase of Candida tropicalis and production of xylitol in Escherichia coli
J. Biosci. Bioeng.
87
280-284
1999
Candida tropicalis (O13283)
brenda
Mayr, P.; Brueggler, K.; Kulbe, K.D.; Nidetzky, B.
D-Xylose metabolism by Candida intermedia isolation and characterisation of two forms of aldose reductase with different coenzyme specificities
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737
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2000
[Candida] intermedia
brenda
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