1.1.1.431: D-xylose reductase (NADPH)
This is an abbreviated version!
For detailed information about D-xylose reductase (NADPH), go to the full flat file.
Reaction
Synonyms
ALR1, Cb-XR, CbXR, CtXR, D-xylose reductase, D-xylose reductase 1, D-xylose reductase 2, D-xylose reductase 3, DnXR, GRE3, monospecific xylose reductase, More, msXR, NAD(P)H-dependent D-xylose reductase, NAD(P)H-dependent xylose reductase, NADPH dependent D-xylose reductase, NADPH-dependent D-xylose reductase II,III, NADPH-dependent xylose reductase, NADPH-preferring xylose reductase, NRRL3_10868, SsXR, Texr, TrxR, XR1, XR2, XR3, XRTL, XYL1, xylose reductase, xyr8, XyrA, XyrB
ECTree
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Cofactor
Cofactor on EC 1.1.1.431 - D-xylose reductase (NADPH)
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additional information
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Kluyveromyces marxianus strains expressing Pichia stipitis Psxyl1 genes show reversed cofactor specificity, overview
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NAD(P)H
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dependent on, the wild-type enzyme prefers NADH, while a modified mutant enzyme prefers NADPH in the D-xylose reduction reaction
NADH
kcat of wild-type enzyme increases by a factor of 1.73 when NADPH replaces NADH. kcat for NADPH-dependent reduction of xylose by the mutant D50A is three times that for the corresponding NADH-dependent reaction
NADH
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using a modified iterative protein redesign and optimization workflow, a sets of mutations is identified that change the nicotinamide cofactor specificity of xylose reductase (CbXR) from its physiological preference for NADPH, to the alternate cofactor NADH
NADPH
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dual specific xylose reductase (dsXR) has an about 4fold higher specificity for NADH than NADPH. NADPH-dependent monospecific xylose reductase (msXR) shows non activity with NADH
NADPH
kcat of wild-type enzyme increases by a factor of 1.73 when NADPH replaces NADH. kcat for NADPH-dependent reduction of xylose by the mutant D50A is three times that for the corresponding NADH-dependent reaction
NADPH
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only NADPH-dependent xylose reductase is obtained under the cultivation conditions
NADPH
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using a modified iterative protein redesign and optimization workflow, a sets of mutations is identified that change the nicotinamide cofactor specificity of xylose reductase (CbXR) from its physiological preference for NADPH, to the alternate cofactor NADH
NADPH
enzyme DnXR shows strict dependence on NADPH, specific conformation of bound NADPH in the active site of DnXR, crystal structure analysis, structure-function analysis, overview. A large number of specific nonbonded interactions are involved in the binding. Among these, the side chain of Tyr212 stacks with the nicotinamide ring and hydrogen bond interactions between the side chains of Ser164, Asn165, and Gln186 with the carboxamide group orient the A-side of the nicotinamide group toward the substrate binding cavity
NADPH
the enzyme protein undergoes an open/closed conformation change upon NADPH binding, SsXR structure in complex with the NADPH cofactor, overview