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Information on EC 1.1.1.9 - D-xylulose reductase

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EC Tree
     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.9 D-xylulose reductase
IUBMB Comments
Also acts as an L-erythrulose reductase.
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This record set is specific for:
UNIPROT: Q8GR61
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Word Map
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The enzyme appears in viruses and cellular organisms
Reaction Schemes
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xylitol
+
NAD+
=
D-xylulose
+
NADH
+
H+
+
=
+
+
Synonyms
xdh, xylitol dehydrogenase, ioxyl2p, psxdh, tdxyl2p, rpxdh, slsdh, ssxyl2p, mcxdh, xyl2.2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
xylitol dehydrogenase
-
2,3-cis-polyol(DPN) dehydrogenase (C3-5)
-
-
-
-
erythritol dehydrogenase
-
-
-
-
NAD-dependent xylitol dehydrogenase
-
-
-
-
pentitol-DPN dehydrogenase
-
-
-
-
reductase, D-xylulose
-
-
-
-
XDH
-
-
-
-
xylitol dehydrogenase
-
-
-
-
xylitol-2-dehydrogenase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
xylitol:NAD+ 2-oxidoreductase (D-xylulose-forming)
Also acts as an L-erythrulose reductase.
CAS REGISTRY NUMBER
COMMENTARY hide
9028-16-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
xylitol + NADP+
D-xylulose + NADPH + H+
show the reaction diagram
wild-type enzyme shows no activity with NADP+, mutant enzyme D38S/M39R is able to exclusively use NADP+, with no loss of activity
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-
?
additional information
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
wild-type enzyme shows no activity with NADP+, mutant enzyme D38S/M39R is able to exclusively use NADP+, with no loss of activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.348
NAD+
pH 7.0, wild-type enzyme
0.0205
NADP+
pH 7.0, mutant enzyme D38S/M39R
13.7 - 100
xylitol
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
27.2
NAD+
pH 7.0, wild-type enzyme
0.206
NADP+
pH 7.0, mutant enzyme D38S/M39R
17.9 - 24.6
xylitol
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
enzyme XDH depends exclusively on NAD+/NADH as cofactors with a relatively low activity directly limiting the overall conversion process of D-xylose fermentation to ethanol by Gluconobacter oxydans
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q8GR61_GLUOY
262
0
27832
TrEMBL
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, crystal structure of the holoenzyme to 1.9 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D38S/M39R
the mutant enzyme is able to exclusively use NADP+, with no loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene xyl2, overexpression in Gluconobacter strain PXPG, coexpression with the glucose dehydrogenase gene from Bacillus subtilis
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the engineered Gluconobacter oxydans strain PXPG is constructed to coexpress the endogenous XDH gene and the cofactor regeneration glucose dehydrogenase gene from Bacillus subtilis. Activities for both enzymes are more than twofold higher in the Gluconobacter oxydans PXPG than in the wild-type strain. Increasing the XDH activity and the cofactor NADH supply improves the xylitol productivity
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ehrensberger, A.H.; Elling, R.A.; Wilson, D.K.
Structure-guided engineering of xylitol dehydrogenase cosubstrate specificity
Structure
14
567-575
2006
Gluconobacter oxydans (Q8GR61), Gluconobacter oxydans
Manually annotated by BRENDA team
Zhang, J.; Li, S.; Xu, H.; Zhou, P.; Zhang, L.; Ouyang, P.
Purification of xylitol dehydrogenase and improved production of xylitol by increasing XDH activity and NADH supply in Gluconobacter oxydans
J. Agric. Food Chem.
61
2861-2867
2013
Gluconobacter oxydans (Q8GR61), Gluconobacter oxydans, Gluconobacter oxydans NH-10 (Q8GR61)
Manually annotated by BRENDA team