1.1.1.9: D-xylulose reductase
This is an abbreviated version!
For detailed information about D-xylulose reductase, go to the full flat file.
Word Map on EC 1.1.1.9
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1.1.1.9
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xanthine
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xylose
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stipitis
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pichia
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xylulokinase
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uric
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lignocellulosic
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pentose
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candida
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molybdenum
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xylose-fermenting
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allopurinol
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hypoxanthine
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xanthinuria
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xylose-utilizing
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hydrolysate
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l-arabitol
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guilliermondii
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bagasse
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bioethanol
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l-arabinose
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hemicellulosic
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marxianus
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scheffersomyces
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rosy
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d-sorbitol
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oxygen-limited
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l-xylulose
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mocos
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tannophilus
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oxydans
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ribitol
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molecular biology
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gluconobacter
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pachysolen
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pseudoobscura
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sulfurase
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shehatae
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synthesis
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biotechnology
- 1.1.1.9
- xanthine
- xylose
- stipitis
- pichia
- xylulokinase
-
uric
-
lignocellulosic
- pentose
- candida
- molybdenum
-
xylose-fermenting
- allopurinol
- hypoxanthine
-
xanthinuria
-
xylose-utilizing
- hydrolysate
- l-arabitol
- guilliermondii
- bagasse
-
bioethanol
- l-arabinose
-
hemicellulosic
- marxianus
- scheffersomyces
-
rosy
- d-sorbitol
-
oxygen-limited
- l-xylulose
- mocos
- tannophilus
- oxydans
- ribitol
- molecular biology
- gluconobacter
- pachysolen
- pseudoobscura
-
sulfurase
- shehatae
- synthesis
- biotechnology
Reaction
Synonyms
2,3-cis-polyol(DPN) dehydrogenase (C3-5), D-xylulose reductase A, erythritol dehydrogenase, GmXDH, IoXyl2p, McXDH, More, NAD+-dependent XDH, NAD+-dependent xylitol dehydrogenase, NAD+-linked xylitol dehydrogenase, NAD-dependent xylitol dehydrogenase, NADH-dependent XDH, NADH-dependent xylitol dehydrogenase, nicotinamide adenine dinucleotide-dependent xylitol dehydrogenase 2, pentitol-DPN dehydrogenase, Ps-XDH, PsXDH, reductase, D-xylulose, RpXDH, slSDH, SpXYL2.2, SsXyl2p, TdXyl2p, XDH, XDH-Y25, xdhA, XL2, XYL2, XYL2.1, XYL2.2, xylitol dehydrogenase, xylitol dehydrogenase 2, xylitol-2-dehydrogenase
ECTree
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Metals Ions
Metals Ions on EC 1.1.1.9 - D-xylulose reductase
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Co2+
Cu2+
Mg2+
Mn2+
Zn2+
additional information
Zn2+
required, the zinc ADH signature and conserved coenzyme binding motif are observed in the amino acid sequence of McXDH at positions 65-76 and 183-188 and are completely conserved among McXDH and XDHs from other yeasts and filamentous fungi
Zn2+
1 mM, 62% of the activity with Mg2+. The deduced XDH gene product possesses the Zn2+-containing ADH signature sequence [GHE]xx[G]xxxxx[G]xx[V] and the catalytic Zn2+-binding site Cys41, His66, Glu67, and Glu152
Zn2+
required, the conserved coenzyme binding motif (GxGxxG) and zinc-ADH signature (GHExxGxxxxxGxxV) are observed in the amino acid sequence of RpXDH at position 181-186 and 70-84. The ligand binding residues for catalytic zinc (residue C46, H71, E72, and E157) and structural zinc (residue C101, C104, C107, and C115) are found in the RpXDH sequence
additional information
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no significant effect by Ni2+, Ca2+, Fe2+, and Cr3+ at 0.5 mM. 5 mM EDTA elicits no obvious effect on NAD-dependent xylitol dehydrogenase 2, indicating that the enzyme does not require a chelator for its activity
additional information
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no activation by Zn2+, Cu2+, Ca2+, Ni2+, Co2+, Fe2+
additional information
after incubation with ZnSO4, ZnCl2, FeCl2, and CuCl2, 40, 37, 30, and 25%, respectively, of the activity of the metal-free enzyme is restored. Poorer effects by Fe3+, Cd2+, and Ca2+, while Ni2+, Mn2+, Co2+, Mg2+, K+, and Na+ do not exert restorative effects
additional information
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after incubation with ZnSO4, ZnCl2, FeCl2, and CuCl2, 40, 37, 30, and 25%, respectively, of the activity of the metal-free enzyme is restored. Poorer effects by Fe3+, Cd2+, and Ca2+, while Ni2+, Mn2+, Co2+, Mg2+, K+, and Na+ do not exert restorative effects
additional information
KCl has not a strong effect on the enzyme activity at 0.1-1.0
additional information
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KCl has not a strong effect on the enzyme activity at 0.1-1.0
additional information
activity is not significantly stimulated by Ba2+, Ca2+, Fe2+, Hg2+, or K+
additional information
LiCl, NaCl, MgCl2, MgSO4, ZnCl2, ZnCl4, SnCl2, NiCl2, BaCl2, and PbCl2 do not affect the enzyme activity at 1 mM
additional information
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LiCl, NaCl, MgCl2, MgSO4, ZnCl2, ZnCl4, SnCl2, NiCl2, BaCl2, and PbCl2 do not affect the enzyme activity at 1 mM