1.1.1.307: D-xylose reductase [NAD(P)H]
This is an abbreviated version!
For detailed information about D-xylose reductase [NAD(P)H], go to the full flat file.
Word Map on EC 1.1.1.307
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1.1.1.307
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synthesis
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l-arabinose
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stipitis
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kluyveromyces
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marxianus
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oxygen-limited
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nadph-linked
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reesei
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l-arabitol
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trichoderma
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passalidarum
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scheffersomyces
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spathaspora
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jecorina
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pachysolen
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pentitols
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bioethanol
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hypocrea
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tannophilus
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galactitol
- 1.1.1.307
- synthesis
- l-arabinose
- stipitis
-
kluyveromyces
- marxianus
-
oxygen-limited
-
nadph-linked
- reesei
- l-arabitol
- trichoderma
- passalidarum
-
scheffersomyces
- spathaspora
- jecorina
-
pachysolen
- pentitols
-
bioethanol
- hypocrea
- tannophilus
- galactitol
Reaction
Synonyms
AKR2B5, ALR2, CTHT_0056950, CtXR, dsXR, dual specific xylose reductase, KmXYL1, NAD(P)H-dependent D-xylose reductase, NAD(P)H-dependent D-xylose reductase-like protein, NAD(P)H-dependent XR, NAD(P)H-dependent xylose reductase, NAD(P)H-linked xylose reductase, NADH/NADPH-xylose reductase, NADP-dependent xylose reductase, PsXR, PsXYL1, SaXYL1, SpXYL1.1, SsXR, Texr, XR, XYL1, xylose reductase, XylR, XyrA
ECTree
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Cofactor
Cofactor on EC 1.1.1.307 - D-xylose reductase [NAD(P)H]
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NADH
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active with both NADPH and NADH as coenzyme. The activity with NADH is approximately 70% of that with NADPH for the various aldose substrates. The ratio of activities with NADH and NADPH is approximately constant between pH 5 and 8
NADH
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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
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prefers NADPH approximately 2fold to NADH, largely due to better apparent binding of the phosphorylated form of the coenzyme
NADH
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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
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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
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active with both NADPH and NADH as coenzyme. The activity with NADH is approximately 70% of that with NADPH for the various aldose substrates. The ratio of activities with NADH and NADPH is approximately constant between pH 5 and 8
NADPH
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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
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prefers NADPH approximately 2fold to NADH, largely due to better apparent binding of the phosphorylated form of the coenzyme
NADPH
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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
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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
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enzyme has dual coenzyme specificity, accepting both NADH and NADPH
NADPH
enzyme has dual coenzyme specificity, accepting both NADH and NADPH
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the enzyme uses both NADPH and NADH but prefers NADPH, the activity with NADPH is about 5fold higher than that with NADH
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additional information
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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
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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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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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