1.1.1.430: D-xylose reductase (NADH)

This is an abbreviated version!
For detailed information about D-xylose reductase (NADH), go to the full flat file.

Reaction

Synonyms

CbXR, CT-XR, dsXR, NAD(P)H-dependent D-xylose reductase, NADH-dependent XR, NADPH-preferring xylose reductase, PsXR, XYL1, XYL1.1, XYL1.2, xylose reductase

ECTree

1 Oxidoreductases

1.1 Acting on the CH-OH group of donors

1.1.1 With NAD⁺ or NADP⁺ as acceptor

1.1.1.430 D-xylose reductase (NADH)

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Results	in table
5	Activating Compound
4	AA Sequence
6	Application
7	Cloned(Commentary)
24	Cofactor
1	Crystallization (Commentary)
1	General Information
10	Inhibitors
41	kcat/KM [mM/s]
9	Ki Value [mM]
35	KM Value [mM]
8	Metals/Ions
3	Molecular Weight [Da]
5	Natural Substrates/ Products (Substrates)
21	Organism
5	pH Optimum
2	pH Range
1	pI Value
14	Protein Variants
3	Purification (Commentary)
4	Reaction
18	Reference
2	Specific Activity [micromol/min/mg]
43	Substrates and Products (Substrate)
5	Subunits
23	Synonyms
1	Systematic Name
6	Temperature Optimum [°C]
1	Temperature Range [°C]
6	Temperature Stability [°C]
34	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.1.1.430 - D-xylose reductase (NADH)

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construction of a 3D structural model. The favourable binding modes for both cofactors NAD(H) and NADP(H) are obtained. The cofactor binding site is composed of a hydrophilic pocket, a hydrophobic pocket as well as a linker channel between the aforementioned two pockets. The hydrophilic pocket could recognize the nicotinamide moiety of the cofactors by hydrogen bonding networks, while the hydrophobic pocket functions to position the adenine moiety of the cofactors by hydrophobic and pi-pi stacking interactions. The linker channel contains some key residues for ligand-binding, their mutation could have impact to the catalytic specificity

Scheffersomyces stipitis

740942