Information on EC 1.1.1.9 - D-xylulose reductase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
1.1.1.9
-
RECOMMENDED NAME
GeneOntology No.
D-xylulose reductase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
xylitol + NAD+ = D-xylulose + NADH + H+
show the reaction diagram
-
-
-
-
xylitol + NAD+ = D-xylulose + NADH + H+
show the reaction diagram
it is concluded that the enzyme reaction follows the mechanism where coenzyme binds first and leaves last. Therefore, dissociation of D-xylulose-NADH complex is suggested to be the rate-limiting step
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
xylitol degradation
-
-
degradation of sugar alcohols
-
-
Pentose and glucuronate interconversions
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
xylitol:NAD+ 2-oxidoreductase (D-xylulose-forming)
Also acts as an L-erythrulose reductase.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2,3-cis-polyol(DPN) dehydrogenase (C3-5)
-
-
-
-
erythritol dehydrogenase
-
-
-
-
NAD-dependent xylitol dehydrogenase
-
-
-
-
NAD-dependent xylitol dehydrogenase
-
-
NAD-dependent xylitol dehydrogenase
Aeribacillus pallidus Y25
-
-
-
pentitol-DPN dehydrogenase
-
-
-
-
reductase, D-xylulose
-
-
-
-
slSDH
-
-
XDH
-
-
-
-
XDH
Aspergillus oryzae KBN616
-
-
-
XDH-Y25
Aeribacillus pallidus Y25
-
-
-
xdhA
-
gene name
xdhA
Aspergillus oryzae KBN616
-
gene name
-
xylitol dehydrogenase
-
-
-
-
xylitol dehydrogenase
-
-
xylitol dehydrogenase
Aspergillus oryzae KBN616
-
-
-
xylitol dehydrogenase
-
-
xylitol dehydrogenase
-
-
xylitol dehydrogenase
Meyerozyma guilliermondii FTI, Meyerozyma guilliermondii FTI 20037
-
-
-
xylitol dehydrogenase
-
-
xylitol dehydrogenase
-
-
xylitol dehydrogenase
-
-
xylitol dehydrogenase
-
-
xylitol-2-dehydrogenase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9028-16-4
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain Y25
-
-
Manually annotated by BRENDA team
Aeribacillus pallidus Y25
strain Y25
-
-
Manually annotated by BRENDA team
expression in Escherichia coli
SwissProt
Manually annotated by BRENDA team
gene xdhA
-
-
Manually annotated by BRENDA team
Aspergillus oryzae KBN616
gene xdhA
-
-
Manually annotated by BRENDA team
strain F-3
-
-
Manually annotated by BRENDA team
Candida diddensiae F-3
strain F-3
-
-
Manually annotated by BRENDA team
expressed in Escherichia coli
-
-
Manually annotated by BRENDA team
recombinant enzyme
-
-
Manually annotated by BRENDA team
CBS 4435
-
-
Manually annotated by BRENDA team
Candida tenuis CBS 4435
CBS 4435
-
-
Manually annotated by BRENDA team
strain Y-456
-
-
Manually annotated by BRENDA team
Candida tropicalis Y-456
strain Y-456
-
-
Manually annotated by BRENDA team
isolated from soil, China
-
-
Manually annotated by BRENDA team
strain ATCC 621
-
-
Manually annotated by BRENDA team
Gluconobacter oxydans NH-10
isolated from soil, China
-
-
Manually annotated by BRENDA team
strain Y-488
-
-
Manually annotated by BRENDA team
Kluyveromyces marxianus Y-488
strain Y-488
-
-
Manually annotated by BRENDA team
fed-batch growth, controlled pH 6.0
-
-
Manually annotated by BRENDA team
FTI 20037, ATCC 201935
-
-
Manually annotated by BRENDA team
growth in pretreated sugarcane bagasse hydrolysate
-
-
Manually annotated by BRENDA team
growth in sugar cane bagasse hydrolysate
-
-
Manually annotated by BRENDA team
strain Y-1017
-
-
Manually annotated by BRENDA team
Meyerozyma guilliermondii FTI 20037
FTI 20037
-
-
Manually annotated by BRENDA team
Meyerozyma guilliermondii Y-1017
strain Y-1017
-
-
Manually annotated by BRENDA team
strain Boidin et Adzet
-
-
Manually annotated by BRENDA team
strain CFN42
UniProt
Manually annotated by BRENDA team
strain Y-1632
-
-
Manually annotated by BRENDA team
Scheffersomyces shehatae Y-1632
strain Y-1632
-
-
Manually annotated by BRENDA team
expressed in Saccharomyces cerevisiae
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
deletin of gene xdhA and gene ladA and or both lead mutants with decreased dehydrogenase activities and increased xylitol production, overview
malfunction
Aspergillus oryzae KBN616
-
deletin of gene xdhA and gene ladA and or both lead mutants with decreased dehydrogenase activities and increased xylitol production, overview
-
metabolism
-
key enzymes for xylitol production in yeasts are xylose reductase and xylitol dehydrogenase, overview
metabolism
-
bioproduction pathway of xylitol, overview
metabolism
Gluconobacter oxydans NH-10
-
bioproduction pathway of xylitol, overview
-
additional information
-
XDH depends exclusively on NAD+/NADH as cofactors with a relatively low activity limiting the the overall conversion process, improvement by recombinant expression of enzyme and glucose dehydrogenase cofactor regeneration enzyme
additional information
Gluconobacter oxydans NH-10
-
XDH depends exclusively on NAD+/NADH as cofactors with a relatively low activity limiting the the overall conversion process, improvement by recombinant expression of enzyme and glucose dehydrogenase cofactor regeneration enzyme
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-arabitol + NAD+
?
show the reaction diagram
-
-
-
-
?
D-arabitol + NAD+
? + NADH + H+
show the reaction diagram
Gluconobacter oxydans, Gluconobacter oxydans NH-10
-
-
-
r
D-fructose + NADH + H+
D-sorbitol + NAD+
show the reaction diagram
-
-
-
-
D-iditol + NAD+
?
show the reaction diagram
Aeribacillus pallidus, Aeribacillus pallidus Y25
-
11.2% of the activity with xylitol
-
-
?
D-mannitol + NAD+
D-fructose + NADH + H+
show the reaction diagram
Gluconobacter oxydans, Gluconobacter oxydans NH-10
-
-
-
r
D-mannitol + NAD+
? + NADH + H+
show the reaction diagram
8% of the activity with xylitol
-
?
D-ribitol + NAD+
D-ribulose + NADH
show the reaction diagram
-
-
-
-
D-ribitol + NAD+
D-ribulose + NADH
show the reaction diagram
-
-
-
-
D-ribitol + NAD+
D-ribulose + NADH
show the reaction diagram
-
-
-
-
D-ribitol + NAD+
D-ribulose + NADH
show the reaction diagram
-
-
-
-
D-ribitol + NAD+
D-ribulose + NADH
show the reaction diagram
-
-
-
r
D-ribitol + NAD+
D-ribulose + NADH
show the reaction diagram
-
85% of the rate of xylitol oxidation
-
-
D-ribitol + NAD+
D-ribulose + NADH
show the reaction diagram
-
oxidation at 11% of the rate of xylitol oxidation
-
-
D-ribulose + NADH
D-ribitol + NAD+
show the reaction diagram
-
-
-
r
D-ribulose + NADH + H+
?
show the reaction diagram
-
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
show the reaction diagram
-
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
show the reaction diagram
-
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
show the reaction diagram
-
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
show the reaction diagram
-
-
-
r
D-sorbitol + NAD+
D-fructose + NADH + H+
show the reaction diagram
-
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
show the reaction diagram
-
-
-
r
D-sorbitol + NAD+
D-fructose + NADH + H+
show the reaction diagram
-
-
ir
D-sorbitol + NAD+
D-fructose + NADH + H+
show the reaction diagram
-
rate of xylitol oxidation at 67%
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
show the reaction diagram
-
oxidation at about 45%
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
show the reaction diagram
-
rate of xylitol oxidation at 95%
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
show the reaction diagram
-
rate of xylitol oxidation at 56%
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
show the reaction diagram
-
rate of xylitol oxidation at 118%
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
show the reaction diagram
-
69% of activity against D-xylitol
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
show the reaction diagram
90% of the activity with xylitol
-
?
D-sorbitol + NAD+
L-sorbose + NADH + H+
show the reaction diagram
Gluconobacter oxydans, Gluconobacter oxydans NH-10
-
-
-
r
D-threitol + NAD+
?
show the reaction diagram
Aeribacillus pallidus, Aeribacillus pallidus Y25
-
109% of the activity with xylitol
-
-
?
D-xylitol + NAD+
D-xylulose + NADH
show the reaction diagram
-
-
-
?
D-xylitol + NAD+
D-xylulose + NADH
show the reaction diagram
-
-
-
?
D-xylitol + NAD+
D-xylulose + NADH
show the reaction diagram
-
-
-
r
D-xylitol + NAD+
D-xylulose + NADH
show the reaction diagram
-
-
-
?
D-xylitol + NAD+
D-xylulose + NADH
show the reaction diagram
-
-
-
?
D-xylitol + NAD+
D-xylulose + NADH
show the reaction diagram
-
-
-
?
D-xylitol + NAD+
D-xylulose + NADH
show the reaction diagram
-
-
-
r
D-xylitol + NAD+
D-xylulose + NADH
show the reaction diagram
Kluyveromyces marxianus Y-488, Candida silvanorum VGI-II, Meyerozyma guilliermondii Y-1017, Candida diddensiae F-3, Candida tropicalis Y-456, Scheffersomyces stipitis Y-2160, Scheffersomyces shehatae Y-1632
-
-
-
?
D-xylulose + NAD+
xylitol + NADH + H+
show the reaction diagram
-
-
-
r
D-xylulose + NADH + H+
xylitol + NAD+
show the reaction diagram
-
-
-
r
D-xylulose + NADH + H+
xylitol + NAD+
show the reaction diagram
-
-
-
r
D-xylulose + NADH + H+
xylitol + NAD+
show the reaction diagram
-
-
-
r
D-xylulose + NADH + H+
xylitol + NAD+
show the reaction diagram
-
-
-
r
D-xylulose + NADH + H+
xylitol + NAD+
show the reaction diagram
-
-
-
r
D-xylulose + NADH + H+
xylitol + NAD+
show the reaction diagram
-
-
-
r
D-xylulose + NADH + H+
xylitol + NAD+
show the reaction diagram
-
-
-
r
D-xylulose + NADH + H+
xylitol + NAD+
show the reaction diagram
-
-
-
r
D-xylulose + NADH + H+
D-xylitol + NAD+
show the reaction diagram
-
-
-
?
D-xylulose + NADH + H+
D-xylitol + NAD+
show the reaction diagram
-
-
-
r
D-xylulose + NADH + H+
D-xylitol + NAD+
show the reaction diagram
-
specific for transferring the 4-pro-R hydrogen of NADH
-
r
dihydroxyacetone + NADH
glycerol + NAD+
show the reaction diagram
-
-
-
-
erythritol + NAD+
L-erythrulose + NADH
show the reaction diagram
-
-
-
r
erythritol + NAD+
? + NADH + H+
show the reaction diagram
0.77% of the activity with xylitol
-
?
galactitol + NAD+
? + NADH + H+
show the reaction diagram
0.98% of the activity with xylitol
-
?
glycerol + NAD+
?
show the reaction diagram
-
-
-
-
?
glycerol + NAD+
?
show the reaction diagram
-
poor substrate
-
-
?
L-arabinitol + NAD+
? + NADH + H+
show the reaction diagram
21% of the activity with xylitol
-
?
L-arabitol + NAD+
?
show the reaction diagram
-
-
-
-
?
L-arabitol + NAD+
?
show the reaction diagram
-
-
-
-
?
L-erythrulose + NADH
erythritol + NAD+
show the reaction diagram
-
-
-
r
L-erythrulose + NADH
erythritol + NAD+
show the reaction diagram
-
reduction at the same rate as D-xylulose
-
-
L-iditol + NAD+
?
show the reaction diagram
-
-
-
-
?
L-sorbose + NADH + H+
?
show the reaction diagram
-
-
-
?
L-threitol + NAD+
? + NADH + H+
show the reaction diagram
0.05% of the activity with xylitol, 75% of the activity with xylitol
-
?
L-xylulose + NADH
L-xylitol + NAD+
show the reaction diagram
-
-
-
?
ribitol + NAD+
?
show the reaction diagram
-
-
-
?
ribitol + NAD+
? + NADH + H+
show the reaction diagram
40% of the activity with xylitol
-
?
sorbitol + NAD+
D-fructose + NADH + H+
show the reaction diagram
-
-
-
?
Xylitol + NAD+
?
show the reaction diagram
-
-
-
-
-
Xylitol + NAD+
?
show the reaction diagram
-
-
-
-
-
Xylitol + NAD+
?
show the reaction diagram
-
-
-
-
-
Xylitol + NAD+
?
show the reaction diagram
-
inducible pathway of xylose catabolism
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
-
-
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
-
-
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
-
-
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
-
-
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
-
-
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
-
-
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
-
-
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
key enzyme in D-xylose metabolism
-
?
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
a xylose reductase, using either NADH or NADPH, reduces D-xylose to xylitol, subsequently xylitol is oxidized to D-xylulose by the NAD+-linked xylitol dehydrogenase
-
?
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
a xylose reductase, using either NADH or NADPH, reduces D-xylose to xylitol, subsequently xylitol is oxidized to D-xylulose by the NAD+-linked xylitol dehydrogenase
-
?
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
Meyerozyma guilliermondii FTI
-
a xylose reductase, using either NADH or NADPH, reduces D-xylose to xylitol, subsequently xylitol is oxidized to D-xylulose by the NAD+-linked xylitol dehydrogenase
-
?
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
Aspergillus oryzae KBN616
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
Meyerozyma guilliermondii FTI 20037
-
a xylose reductase, using either NADH or NADPH, reduces D-xylose to xylitol, subsequently xylitol is oxidized to D-xylulose by the NAD+-linked xylitol dehydrogenase
-
?
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
Gluconobacter oxydans NH-10
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
Candida tenuis CBS 4435
-
-
-
-
xylitol + NAD+
L-xylulose + NADH + H+
show the reaction diagram
Aeribacillus pallidus, Aeribacillus pallidus Y25
-
-
-
?
xylitol + NAD+
D-xylose + NADH + H+
show the reaction diagram
Meyerozyma guilliermondii, Meyerozyma guilliermondii FTI, Meyerozyma guilliermondii FTI 20037
-
-
-
?
xylitol + NADP+
D-xylulose + NADPH + H+
show the reaction diagram
-
-
-
xylitol + NADP+
D-xylulose + NADPH + 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
-
?
meso-erythritol + NAD+
? + NADH + H+
show the reaction diagram
Gluconobacter oxydans, Gluconobacter oxydans NH-10
-
-
-
r
additional information
?
-
-
no reduction of D-ribose and D-galacturonic acid, no oxidation of threitol, xylitol, sorbitol, D-iditol
-
-
?
additional information
?
-
-
no oxidation of threitol, xylitol, sorbitol, D-iditol, no reduction of D-fructose, L-sorbose and D-tagatose, specific for polyols of 5 or less carbon bearing cis-hydroxy groups in C2 and C3
-
-
?
additional information
?
-
-
no reduction of D-ribulose, no reduction of D/L-xylose
-
-
?
additional information
?
-
-
no reduction of D/L-xylose
-
-
?
additional information
?
-
-
no reduction of L-xylulose
-
-
?
additional information
?
-
-
no oxidation of inositol, meso-erythritol and D-(+)-arabitol
-
-
?
additional information
?
-
-
no oxidation of ribitol
-
-
?
additional information
?
-
-
no oxidation of ribitol
-
-
?
additional information
?
-
-
no oxidation of mannitol
-
-
?
additional information
?
-
-
no oxidation of mannitol
-
-
?
additional information
?
-
-
no substrate: glycerol
-
-
-
additional information
?
-
-
specific for transferring the 4-pro-R hydrogen of NADH
-
-
-
additional information
?
-
-
glucose:xylose ratio of 1:2.5 promotes a 2.7fold increase in activity when compared to a glucose:xylose ratio of 1:25
-
-
-
additional information
?
-
-
investigation of limiting metabolic steps in the utilization of xylose by recombinant Saccharomyces cerevisiae using metabolic engineering
-
-
-
additional information
?
-
-
the enzyme is specific for polyols that have a hydroxyl group at the C-2 and C-3 positions in the L- and D-sides, respectively, in the Fischer projection
-
-
-
additional information
?
-
Kluyveromyces marxianus Y-488, Candida silvanorum VGI-II, Meyerozyma guilliermondii Y-1017, Candida diddensiae F-3, Candida tropicalis Y-456, Scheffersomyces stipitis Y-2160
-
specific for NAD+
-
-
-
additional information
?
-
Aeribacillus pallidus Y25
-
the enzyme is specific for polyols that have a hydroxyl group at the C-2 and C-3 positions in the L- and D-sides, respectively, in the Fischer projection
-
-
-
additional information
?
-
Scheffersomyces shehatae Y-1632
-
specific for NAD+
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Xylitol + NAD+
?
show the reaction diagram
-
-
-
-
-
Xylitol + NAD+
?
show the reaction diagram
-
-
-
-
-
Xylitol + NAD+
?
show the reaction diagram
-
-
-
-
-
Xylitol + NAD+
?
show the reaction diagram
-
inducible pathway of xylose catabolism
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
key enzyme in D-xylose metabolism
-
?
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
a xylose reductase, using either NADH or NADPH, reduces D-xylose to xylitol, subsequently xylitol is oxidized to D-xylulose by the NAD+-linked xylitol dehydrogenase
-
?
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
a xylose reductase, using either NADH or NADPH, reduces D-xylose to xylitol, subsequently xylitol is oxidized to D-xylulose by the NAD+-linked xylitol dehydrogenase
-
?
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
Meyerozyma guilliermondii FTI
-
a xylose reductase, using either NADH or NADPH, reduces D-xylose to xylitol, subsequently xylitol is oxidized to D-xylulose by the NAD+-linked xylitol dehydrogenase
-
?
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
Aspergillus oryzae KBN616
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
Meyerozyma guilliermondii FTI 20037
-
a xylose reductase, using either NADH or NADPH, reduces D-xylose to xylitol, subsequently xylitol is oxidized to D-xylulose by the NAD+-linked xylitol dehydrogenase
-
?
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
Gluconobacter oxydans NH-10
-
-
-
r
additional information
?
-
-
glucose:xylose ratio of 1:2.5 promotes a 2.7fold increase in activity when compared to a glucose:xylose ratio of 1:25
-
-
-
additional information
?
-
-
investigation of limiting metabolic steps in the utilization of xylose by recombinant Saccharomyces cerevisiae using metabolic engineering
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
stereochemistry of hydrogen transfer from xylitol, ribitol or sorbitol to NAD+ is of the (R)- or A-type
NAD+
-
xylitol oxidation favors NAD+ over NADP+, but xylulose reduction favors NADPH over NADH
NAD+
no activity with NADP+
NAD+
kcat/Km for wild-type enzyme is 2760/min*mM
NAD+
NAD+ specificity is largely conferred by Asp38, which interacts with the hydroxyls of the adenosine ribose
NAD+
-
dependent on, the wild-type enzyme prefers NAD+, while a modified mutant enzyme is also able to utilize NADP+ in the D-xylitol oxidation reaction
NAD+
the deduced XDH gene product possesses an NAD-binding glycine-rich Rossmann fold domain [GXGXXG] present in MDR superfamily
NADH
no activity with NADPH
NADP+
-
xylitol oxidation favors NAD+ over NADP+, but xylulose reduction favores NADPH over NADH
NADP+
kcat/Km for wild-type enzyme is 0.65/min*mM
NADP+
wild-type enzyme shows no activity with NADP+, mutant enzyme D38S/M39R is able to exclusively use NADP+, with no loss of activity
NADP+
-
the wild-type enzyme prefers NAD+, while a modified mutant enzyme is also able to utilize NADP+ in the D-xylitol oxidation reaction
additional information
-
at high concentrations of xylitol 1.5% as effective as NAD+; no activity with NADP+; no activity with NADPH
-
additional information
-
at high concentrations of xylitol 1.5% as effective as NAD+; no activity with NADP+; no activity with NADPH
-
additional information
-
at high concentrations of xylitol 1.5% as effective as NAD+; no activity with NADP+; very low activity with NADPH
-
additional information
-
no oxidation of ribitol or sorbitol with NADP+
-
additional information
activity with NADP+ is 4% of the activity with NAD+
-
additional information
-
XDH depends exclusively on NAD+/NADH as cofactors with a relatively low activity
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
1 mM, 18% of the activity with Mg2+
Co2+
1 mM, 38% of the activity with Mg2+
Cu2+
1 mM, 51% of the activity with Mg2+
KCl
-
slight activation
Mg2+
-
activation at high concentration
Mg2+
or Mn2+, required
Mn2+
-
requirement
Mn2+
or Mg2+, required. At 1 mM, 108% of the activity with Mg2+
NaCl
-
activation
NH4Cl
-
activation
Zn2+
-
0.9 molecules per subunit
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
MnCl2
-
10 mM, increase of activity by 100%
additional information
-
no evidence for metal requirement
additional information
-
no activation by Zn2+, Cu2+, Ca2+, Ni2+, Co2+, Fe2+
additional information
-
no significant content of Mg2+
additional information
activity is not significantly stimulated by Ba2+, Ca2+, Fe2+, Hg2+, or K+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CaCl2
-
1 mM, 70% inhibition
CaCl2
-
10 mM, 8% inhibition
CuSO4
-
10 mM, no residual activity
cysteine
-
at 294 mM
D-xylulose
-
high concentration
D-xylulose
-
-
EDTA
-
dialysis overnight, 80% residual activity
EDTA
1-10 mM, strong inhibition
HgCl2
-
complete inhibition
iodoacetate
-
complete inhibition
MgCl2
-
10 mM, 4% inhibition
NaCl
-
at 160 mM
NH4Cl
-
at 310 mM
NiCl2
-
1 mM, complete inhibition
Pb(CH3COO)2
-
-
PCMB
-
complete inhibition
Zn2+
-
exogenous Zn2+ (added as ZnSO4) in the concentration range 1-100 microM is a strong irreversible inhibitor of wild-type and mutant E154C
ZnSO4
-
complete inhibition
additional information
-
no inhibition by EDTA or iodoacetate
-
additional information
-
not inhibitory: MgCl2, ZnCl2, CoCl2, CuCl2 at 1 mM, EDTA at 10 mM
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cysteine
-
of partially purified preparation
cysteine
-
slight activation
D-glucose
-
induces activity
D-Lyxose
-
induces activity
D-xylose
-
induces activity
D-xylose
-
induces activity
D-xylose
-
induces activity
glycerol
-
induces activity
glycine
-
slight activation
GSH
-
activation
L-arabinose
-
induces activity
Sodium acetate
-
1 g/l in reaction medium, about 15% increase of activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.7
D-ribulose
35C, pH 7.5, native enzyme
4
D-sorbitol
35C, pH 7.5, native enzyme
30
D-sorbitol
-
-
12
D-xylitol
-
pH 8.2, 22C
94
D-xylitol
-
-
0.66
D-xylulose
-
-
1.1
D-xylulose
-
-
2
D-xylulose
35C, pH 7.5, native enzyme
10
D-xylulose
-
25C, pH 9.0
0.038
NAD+
-
-
0.14
NAD+
-
-
0.152
NAD+
pH 9.0, 35C, mutant enzyme D207A/I208R/F209Y
0.162
NAD+
pH 9.0, 35C, mutant enzyme D207A/F209S
0.25
NAD+
pH 9.5, 25C
0.265
NAD+
pH 9.0, 35C, mutant enzyme D207A/I208R/F209T
0.348
NAD+
pH 7.0, wild-type enzyme
0.381
NAD+
pH 9.0, 35, wild-type enzyme
0.403
NAD+
pH 9.0, 35C, mutant enzyme D207A
0.498
NAD+
pH 9.0, 35C, mutant enzyme I208R
0.538
NAD+
pH 9.0, 35C, mutant enzyme N211R
0.568
NAD+
pH 9.0, 35C, mutant enzyme D207A/I208R
0.665
NAD+
pH 9.0, 35C, mutant enzyme I208R/F209S
0.739
NAD+
pH 9.0, 35C, mutant enzyme S96C/S99CY102C
0.848
NAD+
pH 9.0, 35C, mutant enzyme F209S
1.3
NAD+
pH 9.0, 35C, mutant enzyme D207A/I208R/F209S
7.6
NAD+
pH 9.0, 35C, mutant enzym S96C/S99C/Y102C/D207A/I208R/F209S/N211R
17.3
NAD+
pH 9.0, 35C, mutant enzyme D207A/I208R/F209S/N211R
23.5
NAD+
pH 9.0, 35C, mutant enzyme S96C/S99C/Y102C/D207A/I208R/F209S
290
NAD+
-
mutant E154C, kcat/Km (NAD+): 4100/Msec
323
NAD+
-
pH 8.2, 22C
430
NAD+
-
kcat/Km (NAD+): 370000/Msec
500
NAD+
-
kcat/Km (NAD+): 57000/Msec
0.0205
NADP+
pH 7.0, mutant enzyme D38S/M39R
0.638
NADP+
pH 9.0, 35C, mutant enzyme D207A/I208R/F209T
0.731
NADP+
pH 9.0, 35C, mutant enzyme D207A/I208R/F209Y
0.897
NADP+
pH 9.0, 35C, mutant enzyme D207A/I208R/F209S
1.04
NADP+
pH 9.0, 35C, mutant enzym S96C/S99C/Y102C/D207A/I208R/F209S/N211R
1.18
NADP+
pH 9.0, 35C, mutant enzyme S96C/S99C/Y102C/D207A/I208R/F209S
1.38
NADP+
pH 9.0, 35C, mutant enzyme D207A/I208R/F209S/N211R
9.19
NADP+
pH 9.0, 35C, mutant enzyme I208R/F209S
9.56
NADP+
pH 9.0, 35C, mutant enzyme S96C/S99CY102C
9.96
NADP+
pH 9.0, 35C, mutant enzyme D207A/F209S
11.3
NADP+
pH 9.0, 35C, mutant enzyme D207A/I208R
21.1
NADP+
pH 9.0, 35C, mutant enzyme I208R
28.9
NADP+
pH 9.0, 35C, mutant enzyme F209S
56.5
NADP+
pH 9.0, 35C, mutant enzyme N211R
120
NADP+
pH 9.0, 35C, mutant enzyme D207A
170
NADP+
pH 9.0, 35, wild-type enzyme
496
ribitol
-
-
0.16
sorbitol
-
-
3
sorbitol
-
kcat/Km (sorbitol): 9500/Msec
21
sorbitol
-
kcat/Km (sorbitol): 7800/Msec
785
sorbitol
-
mutant E154C, kcat/Km (sorbitol): 1.5/Msec
0.039
xylitol
-
-
0.638
xylitol
pH 9.0, 35C, cofactor: NADP+, mutant enzyme D207A/I208R/F209T
0.731
xylitol
pH 9.0, 35C, cofactor: NADP+, mutant enzyme D207A/I208R/F209Y
0.897
xylitol
pH 9.0, 35C, cofactor: NADP+, mutant enzyme D207A/I208R/F209S
1.04
xylitol
pH 9.0, 35C, cofactor: NADP+, mutant enzyme S96C/S99C/Y102C/D207A/I208R/F209S/N211R
1.18
xylitol
pH 9.0, 35C, cofactor: NADP+, mutant enzyme S96C/S99C/Y102C/D207A/I208R/F209S
1.38
xylitol
pH 9.0, 35C, cofactor: NADP+, mutant enzyme D207A/I208R/F209S/N211R
4
xylitol
35C, pH 7.5, native enzyme
4 - 5.4
xylitol
pH 9.0, 35C, cofactor: NAD+, mutant enzyme I208R/F209S
5.2
xylitol
35C, pH 7.5, recombinant enzyme
7.1
xylitol
-
-
9.56
xylitol
pH 9.0, 35C, cofactor: NADP+, mutant enzyme S96C/S99CY102C
9.96
xylitol
pH 9.0, 35C, cofactor: NADP+, mutant enzyme D207A/F209S
12.1
xylitol
pH 9.5, 25C
12.6
xylitol
-
-
13.7
xylitol
pH 7.0, cofactor: NAD+, wild-type enzyme
16.4
xylitol
-
-
18.5
xylitol
-
-
21.7
xylitol
pH 9.0, 35, cofactor: NAD+, wild-type enzyme
21.7
xylitol
-
wild-type XDH: kcat/Km (NAD+): 2760 l/min/mmol, kcat/Km (NADP+): 2790 l/min/mmol
22.2
xylitol
pH 9.0, 35C, cofactor: NAD+, mutant enzyme D207A
24.2
xylitol
pH 9.0, 35C, cofactor: NAD+, mutant enzyme D207A/I208R
27.4
xylitol
pH 9.0, 35C, cofactor: NAD+, mutant enzyme N211R
29.5
xylitol
pH 9.0, 35C, cofactor: NAD+, mutant enzyme I208R
30.3
xylitol
pH 9.0, 35C, cofactor: NAD+, mutant enzyme S96C/S99CY102C
31.1
xylitol
-
mutant D207A/I208R/F209S: kcat/Km (NAD+): 181 l/min/mmol, kcat/Km (NADP+): 0.65 l/min/mmol
34.1
xylitol
pH 9.0, 35C, cofactor: NAD+, mutant enzyme F209S
45.2
xylitol
pH 9.0, 35C, cofactor: NAD+, mutant enzyme D207A/F209S
49.8
xylitol
-
-
50.1
xylitol
pH 9.0, 35C, cofactor: NAD+, mutant enzyme D207A/I208R/F209Y
55.7
xylitol
pH 9.0, 35C, cofactor: NAD+, mutant enzyme D207A/I208R/F209S
97.8
xylitol
pH 9.0, 35C, cofactor: NAD+, mutant enzyme D207A/I208R/F209T
100
xylitol
pH 7.0, cofactor: NADP+ mutant enzyme D38S/M39R
111
xylitol
-
mutant S96C/S99C/Y102C/D207A/I208R/F209S: kcat/Km (NADP+): 10700 l/min/mmol
13.8
xylulose
-
-
0.9
L-sorbose
35C, pH 7.5, native enzyme
additional information
additional information
-
steady-state kinetic analysis of wild-type and mutant enzymes, overview
-
additional information
additional information
-
kinetics of mutant enzymes in engineered strains, detailed overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
920
D-fructose
Candida sp. HA 167
-
25C, pH 7.5, Tris-HCl
74
D-ribulose
Blastobotrys adeninivorans
Q6KAV2
35C, pH 7.5, native enzyme
114
D-sorbitol
Candida sp. HA 167
-
25C, pH 7.5, Tris-HCl
528
D-sorbitol
Blastobotrys adeninivorans
Q6KAV2
35C, pH 7.5, native enzyme
302.9
D-xylulose
Blastobotrys adeninivorans
Q6KAV2
35C, pH 7.5, native enzyme
1500
D-xylulose
Candida sp. HA 167
-
25C, pH 7.5, Tris-HCl
1800
D-xylulose
Candida sp. HA 167
-
25C, pH 7.5, potassium phosphate
216
L-sorbose
Blastobotrys adeninivorans
Q6KAV2
35C, pH 7.5, native enzyme
0.052 - 2.1
NAD+
Scheffersomyces stipitis
P22144
pH 9.0, 35C, mutant enzyme D207A/I208R
0.5
NAD+
Scheffersomyces stipitis
P22144
pH 9.0, 35C, mutant enzym S96C/S99C/Y102C/D207A/I208R/F209S/N211R
1
NAD+
Scheffersomyces stipitis
P22144
pH 9.0, 35C, mutant enzyme D207A/I208R/F209Y; pH 9.0, 35C, mutant enzyme I208R/F209S
3.33
NAD+
Scheffersomyces stipitis
P22144
pH 9.0, 35C, mutant enzyme D207A/F209S
4
NAD+
Scheffersomyces stipitis
P22144
pH 9.0, 35C, mutant enzyme D207A/I208R/F209S
5.17
NAD+
Scheffersomyces stipitis
P22144
pH 9.0, 35C, mutant enzyme D207A; pH 9.0, 35C, mutant enzyme D207A/I208R/F209T
10.33
NAD+
Scheffersomyces stipitis
P22144
pH 9.0, 35C, mutant enzyme D207A/I208R
13.17
NAD+
Scheffersomyces stipitis
P22144
pH 9.0, 35C, mutant enzym S96C/S99C/Y102C/D207A/I208R/F209S/N211R
16.9
NAD+
Scheffersomyces stipitis
P22144
pH 9.0, 35C, mutant enzyme N211R
17.5
NAD+
Scheffersomyces stipitis
P22144
pH 9.0, 35, wild-type enzyme
18
NAD+
Scheffersomyces stipitis
P22144
pH 9.0, 35C, mutant enzyme D207A/I208R/F209S/N211R
20.33
NAD+
Scheffersomyces stipitis
P22144
pH 9.0, 35C, mutant enzyme F209S
22.83
NAD+
Scheffersomyces stipitis
P22144
pH 9.0, 35C, mutant enzyme N211R
23.8
NAD+
Scheffersomyces stipitis
P22144
pH 9.0, 35C, mutant enzyme I208R
23.83
NAD+
Scheffersomyces stipitis
P22144
pH 9.0, 35C, mutant enzyme D207A/I208R/F209S/N211R
27.2
NAD+
Gluconobacter oxydans
Q8GR61
pH 7.0, wild-type enzyme
29.5
NAD+
Scheffersomyces stipitis
P22144
pH 9.0, 35C, mutant enzyme S96C/S99C/Y102C/D207A/I208R/F209S
30.33
NAD+
Scheffersomyces stipitis
P22144
pH 9.0, 35C, mutant enzyme S96C/S99CY102C
0.017
NADP+
Scheffersomyces stipitis
P22144
pH 9.0, 35C, mutant enzyme D207A/I208R/F209T
0.145
NADP+
Scheffersomyces stipitis
P22144
pH 9.0, 35C, mutant enzyme I208R/F209S
0.206
NADP+
Gluconobacter oxydans
Q8GR61
pH 7.0, mutant enzyme D38S/M39R
0.91
NADP+
Scheffersomyces stipitis
P22144
pH 9.0, 35C, mutant enzyme S96C/S99CY102C
1.83
NADP+
Scheffersomyces stipitis
P22144
pH 9.0, 35, wild-type enzyme
2 - 8
NADP+
Scheffersomyces stipitis
P22144
pH 9.0, 35C, mutant enzyme D207A/I208R
4.67
NADP+
Scheffersomyces stipitis
P22144
pH 9.0, 35C, mutant enzyme N211R
5.7
NADP+
Scheffersomyces stipitis
P22144
pH 9.0, 35C, mutant enzyme D207A
6.17
NADP+
Scheffersomyces stipitis
P22144
pH 9.0, 35C, mutant enzyme D207A/I208R/F209Y
8
NADP+
Scheffersomyces stipitis
P22144
pH 9.0, 35C, mutant enzyme D207A/F209S
9.83
NADP+
Scheffersomyces stipitis
P22144
pH 9.0, 35C, mutant enzyme F209S
10
NADP+
Scheffersomyces stipitis
P22144
pH 9.0, 35C, mutant enzyme I208R
32.83
NADP+
Scheffersomyces stipitis
P22144
pH 9.0, 35C, mutant enzyme D207A/I208R/F209T
41.7
NADP+
Scheffersomyces stipitis
P22144
pH 9.0, 35C, mutant enzyme D207A/I208R/F209S
64
NADP+
Scheffersomyces stipitis
P22144
pH 9.0, 35C, mutant enzyme D207A/I208R/F209S/N211R
183.3
NADP+
Scheffersomyces stipitis
P22144
pH 9.0, 35C, mutant enzym S96C/S99C/Y102C/D207A/I208R/F209S/N211R
210
NADP+
Scheffersomyces stipitis
P22144
pH 9.0, 35C, mutant enzyme S96C/S99C/Y102C/D207A/I208R/F209S
1.19
sorbitol
Candida sp. HA 167
-
mutant E154C
2 - 8
sorbitol
Ovis aries
-
-
161
sorbitol
Candida sp. HA 167
-
-
17.9
xylitol
Gluconobacter oxydans
Q8GR61
pH 7.0, cofactor: NADP+mutant enzyme D38S/M39R
24.6
xylitol
Gluconobacter oxydans
Q8GR61
pH 7.0, cofactor: NAD+, wild-type enzyme
143
xylitol
Candida sp. HA 167
-
25C, pH 7.5, Tris-HCl
170
xylitol
Candida sp. HA 167
-
25C, pH 7.5, potassium phosphate
2115
xylitol
Blastobotrys adeninivorans
Q6KAV2
35C, pH 7.5, recombinant enzyme
2644
xylitol
Blastobotrys adeninivorans
Q6KAV2
35C, pH 7.5, native enzyme
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10
D-xylulose
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.005
ZnSO4
Candida sp. HA 167
-
value identical for wildtype and for mutant E154C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.15 - 0.18
-
depending on nitrogen source in culture medium
0.76
-
purified native enzyme, pH 11.0, 30C, substrate meso-erythritol
2.16
-
specific activity of recombinant Saccharomyces cerevisiae strain TMB3057
6.74
-
purified native enzyme, pH 11.0, 30C, substrate D-arabitol
12.89
-
purified native enzyme, pH 11.0, 30C, substrate D-mannitol
102.5
-
purified native enzyme, pH 11.0, 30C, substrate xylitol
113
-
substrate D-xylitol, pH 10, 30C
156.1
-
purified native enzyme, pH 11.0, 30C, substrate D-sorbitol
180.4
-
purified native enzyme, pH 5.0, 30C, substrate D-fructose
220
-
substrate D-sorbitol, pH 10, 30C
250
-
pH 8.4, 30C
564
-
purified native enzyme, pH 5.0, 30C, substrate D-xylulose
additional information
-
-
additional information
-
-
additional information
specific activity of wild-type and mutant enzymes
additional information
-
specific activity (U/min): 1110 (wild-type), 1440 (mutant S96C/S99C/Y102C), 1220 (mutant S96C/S99C/Y102C/P95S), 1510 (mutant S96C/S99C/Y102C/F98R), 1550 (mutant S96C/S99C/Y102C/E101F), 1360 (mutant S96C/S99C/Y102C/H112D), 1620 (mutant S96C/S99C/Y102C/F98R/E101F)
additional information
-
wild-type: NADP+-dependent activity: 0.005 U/mg, NAD+-dependent activity: 1.654 U/mg, mutant D207A/I208R/F209S: NADP+-dependent activity: 0.782 U/mg, NAD+-dependent activity: 0.271 U/mg, mutant S96C/S99C/Y102C/D207A/I208R/F209S: NADP+-dependent activity: 0.698 U/mg, NAD+-dependent activity: 0.136 U/mg
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5
-
reduction of D-xylulose
5.5
-
reduction reaction
6.7
-
reduction of erythrulose
7
-
substrate reduction
7
-
assay at
7
-
assay at
7.2
-
xylitol formation
7.5
native and recombinant enzyme
8.6
-
oxidation of erythritol
8.6
-
D-xylulose formation
9.1 - 10
-
substrate oxidation, plateau
10.5 - 11
-
oxidation reaction
11
-
oxidation of xylitol
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 8
-
about 75% of maximal reduction activity at pH 4.0 and 8.0
4 - 8
-
reduction reaction, activity range
8.7 - 10.5
-
about 80% of maximal oxidation activity at pH 8.7 and 10.5
9 - 10
-
fully active
9 - 12
-
oxidation reaction, activity range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
assay at
30
-
reduction reaction
35
native and recombinant enzyme
35
-
oxidation reaction
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 50
-
20C: about 50% of maximal activity, 50C: about 50% of maximal activity
20 - 55
-
activity range, profile overview
35 - 68
-
about half-maximal activity at 35C and 68C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
the organism grows on rice straw hemicellulosic hydrolysate, as the only source of nutrient, optimization of culture conditions for production of xylitol from D-xylose, xylitol dehydrogenase remains constant, whereas the level of xylose reductase decreases when the initial xylose concentration is increased from 30 to 70 g/l, development of enzyme activities, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
no activity in membrane fraction
-
Manually annotated by BRENDA team
additional information
Aeribacillus pallidus Y25
-
no activity in membrane fraction
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
72000
native enzyme, gel filtration, non-denaturing PAGE
667227
80000
recombinant enzyme, gel filtration, non-denaturing PAGE
667227
82000
-
gel filtration
246417
94000
-
PAGE
655092
120000
-
gel filtration
246421
130000
-
PAGE
246420
135000
gel filtration
710975
142000
-
PAGE
246420
155000
-
PAGE
246420
160000
-
gel filtration
655221
160000
-
gel filtration, protein is a homotetramer
684974
172000
-
gel filtration
246418
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 27800, deduced from genen sequence, x * 27000, SDS-PAGE
?
x * 38197, deduced from gene sequence, x * 36500, SDS-PAGE
?
-
x * 28000, SDS-PAGE
?
Aeribacillus pallidus Y25
-
x * 28000, SDS-PAGE
-
dimer
-
2 * 40000, SDS-PAGE
dimer
-
2 * 48000, SDS-PAGE
dimer
2 * 40300, calculated from sequence
homotetramer
-
4 * 38000, SDS-PAGE
homotetramer
-
gel filtration
tetramer
-
2 * 40400 + 2 * 41800, SDS-PAGE
tetramer
-
4 * 40000, SDS-PAGE
tetramer
4 * 35858, calculated, 4 * 34000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, crystal structure of the holoenzyme to 1.9 A resolution
multi-template homology modeling. The structural model of XDH obtained consists of a classical alpha/beta Rossmann fold pattern commonly found in the MDR family, which is organized into two beta-barrel domains, the coenzyme-binding residues 163-300 and catalytic residues 1-162, 301-364
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 7
-
24 h, fully stable
655092
6.8 - 7.4
-
90% of maximal activity retained at pH 6.8 and 7.4 at 2C
246415
7
-
24 h stable at 2C
246415
7 - 9
-
stable
246421
7.2 - 7.9
stable
667227
8 - 10
-
4C, 60 min, stable
686433
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 40
-
10 min, 2.5 mM NAD+, stable
686433
20
-
at room temperature, the enzyme is inactivated within 2 days
686433
25
-
and below stable
246421
30
-
1 h, completely stable
655092
40
half-life 120 min
710975
50
-
1 h, no residual activity
655092
50
-
10 min, 2.5 mM NAD+, about 50% loss of activity
686433
53.1
half denaturation temperature
710975
60
-
complete inactivation within 5 min
246421
60
-
10 min, 2.5 mM NAD+, about 80% loss of activity
686433
additional information
-
wild-type: half denaturation temperature T1/2 (C): 35.2, thermal transition temperature Tcd (C): 43.0
687872
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
crude water extract from liver acetone-powder unstable
-
freezing/thawing inactivates, 8 cycles lead to 89% loss of activity and 11 cycles to complete inactivation
-
2-mercaptoethanol stabilizes during purification
-
EDTA stabilizes during purification
-
30C, pH 6-7, 24 h, fully stable
-
freezing/thawing inactivates, 8 cycles lead to 89% loss of activity and 11 cycles to complete inactivation
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acetone
-
stable to precipitation with 50% v/v
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10C, acetone precipitate stable for weeks
-
0C, partially purified stable for weeks
-
2C, 90% of maximal activity retained at pH 6.8 and 7.4 after 24 h
-
-15C, 60% loss of activity after 1 month
-
-2C, purified stable for a month
-
0C, 34% loss of activity within a month
-
-20C, stable with 50% v/v glycerol
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
-
using affinity chromatography and preparative gel filtration
-
native enzyme 469fold from sstrain NH-10 by ammonium sulfate fractionation, two different steps of anion exchange chromatography, and gel filtration
-
optimized extraction by cetyl trimethyl ammonium bromide reversed micelles
-
recombinant enzmye
using Ni-NTA chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expressed in Escherichia coli
-
expressed in Escherichia coli JM 109
-
expression of the engineered D202A/L203R/V204S/E205P/S206R mutant enzyme fron Galactocandida mastotermitis with altered cofactor specificity, co-expression with a mutant NADPH-specific xylulose reductase from Candida tenuis in Saccharomyces cerevisiae, the transformed strain shows up to 50% decreased glycerol yield without increase in ethanol during xylose fermentation, overview
-
overexpression of the enzyme in Saccharomyces cerevisiae strain CEN.PK 113-7D under control of the constitutive TDH3 promoter, co-expression with xylose reductase from Candida tenuis
-
gene xdhA, coexpression of gene xdhA and cofactor regeneration enzyme, i.e. glucose dehydrogenase gene gdh from Bacillus subtilis, in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain JM109
-
expression in Escherichia coli
overexpression in Saccharomyces cerevisiae
-
expressed as a His-tagged fusion protein in Escherichia coli
-
expressed in transketolase-deficient Saccharomyces cerevisiae strain (W303/tkl1 tkl2/2C)
-
expression in Escherichia coli
genes XYL2 (D207A/I208R/F209S) and XYL2 (S96C/S99C/Y102C/D207A/I208R/F209S) are introduced into Saccharomyces cerevisiae, which already contain the Pichia stipitis XYL1 gene (encoding xylose reductase) and the endogenously overexpressed XKS1 gene (encoding xylulokinase)
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D202A/L203R/V204S/E205P/S206R
-
site-directed mutagenesis, introduction of multiple site-directed mutations in the coenzyme-binding pocket of Galactocandida mastotermitis XDH to enable activity with NADP+, which is lacking in the wild-type enzyme, genetic metabolic engineering for improvement of xylose metabolism and fermentation in wild-type Saccharomyces cerevisiae strains, which are not able to naturally metabolize D-xylulose, overview
E154C
-
mutant bearing a disrupted Zn2+ binding site: purified preparations show a variable Zn2+ (0.10-0.40 atom/subunit), mutant exhibits a constant catalytic Zn2+ centre activity and does not require exogenous Zn2+ for activity or stability. E154C retains 0.019% and 0.74% of wild-type catalytic efficiency (kcat/Km (sorbitol): 7800/Msec and kcat:161/sec) for NAD+-dependent oxidation of sorbitol at 25C respectively. The pH profile of kcat/Ksorbitol for E154C decreases below an apparent pK of 9.1, reflecting a shift in pK by about +1.7-1.9 pH units compared with the corresponding pH profiles for wild-type. IC50 (ZnSO4): 0.005 mM
synthesis
-
use of enzyme in a process for producing xylitol from D-glucose
D207A
kcat/Km for NAD+ is 3.6fold lower than wild-type value, kcat/Km for NADP+ is 4.3fold higher than wild-type value
D207A/F209S
kcat/Km for NAD+ is 2.2fold lower than wild-type value, kcat/Km for NADP+ is 745fold higher than wild-type value
D207A/I208R
kcat/Km for NAD+ is 2.5fold lower than wild-type value, kcat/Km for NADP+ is 229fold higher than wild-type value
D207A/I208R/F209S
kcat/Km for NAD+ is 15.2fold lower than wild-type value, kcat/Km for NADP+ is 4292fold higher than wild-type value, increased thermostability
D207A/I208R/F209S
-
mutant bearing a reversal of coenzyme specificity from NAD+ to NADP+ is introduced into Saccharomyces cerevisiae. kcat/Km (NAD+): 181 l/min/mmol, kcat/Km (NADP+): 2790 l/min/mmol, Km (xylitol in the presence of NAD+): 31.1 mM, NADP+-dependent activity: 0.782 U/mg, NAD+-dependent activity: 0.271 U/mg. In xylose fermentation a large decrease in xylitol and glycerol yield is shown, while the xylose consumption and ethanol yield are decreased
D207A/I208R/F209S/N211R
kcat/Km for NAD+ is 32.9fold lower than wild-type value, kcat/Km for NADP+ is 4292fold higher than wild-type value, increased thermostability
D207A/I208R/F209T
kcat/Km for NAD+ is 2.4fold lower than wild-type value, kcat/Km for NADP+ is 4754fold higher than wild-type value
D207A/I208R/F209Y
kcat/Km for NAD+ is 6.9fold lowerthan wild-type value, kcat/Km for NADP+ is 788fold higher than wild-type value
F209S
kcat/Km for NAD+ is 1.9fold lower than wild-type value, kcat/Km for NADP+ is 31.4fold higher than wild-type value
I208R
kcat/Km for NAD+ is nearly identical to wild-type value, kcat/Km for NADP+ is 44fold higher than wild-type value
N211R
kcat/Km for NAD+ is 1.1fold lower than wild-type value, kcat/Km for NADP+ is 7.6fold higher than wild-type value
S96C/S99C/Y102C
-
specific activity (U/min): 1440, half denaturation temperature T1/2 (C): 46.1, thermal transition temperature Tcd (C): 47.5
S96C/S99C/Y102C/D207A/I208R/F209S
kcat/Km for NAD+ is 36.7fold lower than wild-type value, kcat/Km for NADP+ 16462is fold higher than wild-type value
S96C/S99C/Y102C/D207A/I208R/F209S
-
mutant bearing a reversal of coenzyme specificity from NAD+ to NADP+ and additional zinc-binding site for thermostability, is introduced into Saccharomyces cerevisiae. kcat/Km (NADP+): 10700 l/min/mmol, Km (xylitol in the presence of NAD+): 111 mM , NADP+-dependent activity: 0.689 U/mg, NAD+-dependent activity: 0.136 U/mg. The xylose consumption and ethanol yield are decreased, and the xylitol yield is increased, because of low XDH activity
S96C/S99C/Y102C/D207A/I208R/F209S/N211R
kcat/Km for NAD+ is 26.5fold lower than wild-type value, kcat/Km for NADP+ is 16154fold higher than wild-type value
S96C/S99C/Y102C/E101F
-
specific activity (U/min): 1550, half denaturation temperature T1/2 (C): 50.9, thermal transition temperature Tcd (C): 50.5
S96C/S99C/Y102C/F98R
-
specific activity (U/min): 1510, half denaturation temperature T1/2 (C): 53.1, thermal transition temperature Tcd (C): 51.7
S96C/S99C/Y102C/F98R/E101F
-
specific activity (U/min): 1620, half denaturation temperature T1/2 (C): 56.0, thermal transition temperature Tcd (C): 53.8
S96C/S99C/Y102C/H112D
-
specific activity (U/min): 1360, half denaturation temperature T1/2 (C): 44.0, thermal transition temperature Tcd (C): 47.0
S96C/S99C/Y102C/P95S
-
specific activity (U/min): 1220, half denaturation temperature T1/2 (C): 37.4, thermal transition temperature Tcd (C): 43.5
S96C/S99CY102C
kcat/Km for NAD+ is 1.1fold lower than wild-type value, kcat/Km for NADP+ is 8.8fold higher than wild-type value
additional information
-
generation of xdhA and ladA deletion mutants and double-deletion mutant, that show decreased dehydrogenase activities and increased xylitol production from D-xylose compared to the KBN616 wild-type strain, overview
additional information
Aspergillus oryzae KBN616
-
generation of xdhA and ladA deletion mutants and double-deletion mutant, that show decreased dehydrogenase activities and increased xylitol production from D-xylose compared to the KBN616 wild-type strain, overview
-
D38S/M39R
the mutant enzyme is able to exclusively use NADP+, with no loss of activity
additional information
-
strain overexpressing enzyme has improved xylitol productivity, production of up to 57g/l xylitol from 225 g/l D-arabitol, via D-xylulose
additional information
-
to improve characteristics of xylose fermentation, the recombinant strain Delta xyl1 Delta xyl2-ADelta xyl2-B, with deletions of genes encoding first enzymes of xylose utilization (NAD(P)H-dependent xylose reductase and NAD-dependent xylitol dehydrogenases, respectively), is constructed and used as a recipient for co-overexpression of the Escherichia coli xylA gene coding for xylose isomerase and endogenous XYL3 gene coding for xylulokinase. Recombinant strains display improved ethanol production during the fermentation of xylose
additional information
-
recombinant Saccharomyces cerevisiae strain TMB3057 with high activity of both xylose reductase and xylitol dehydrogenase show increased ethanol formation from xylose at the expense of xylitol formation
additional information
-
coenzyme specificities of the NADPH-preferring xylose reductase, EC 1.1.1.307, and the NAD+-dependent xylitol dehydrogenase are targeted in previous studies by protein design or evolution with the aim of improving the recycling of NADH or NADPH in their two-step pathway, converting xylose to xylulose. Yeast strains expressing variant pairs of both enzymes that according to in vitro kinetic data are suggested to be much better matched in coenzyme usage than the corresponding pair of wild-type enzymes, exhibit widely varying capabilities for xylose fermentation, bi-substrate kinetic analysis, and statistical analysis, overview. Engineered strains of Saccharomyces cerevisiae have engineered forms of xylose reductase or xylose dehydrogenase and imporved performance in xylose fermentation
I208R/F209S
kcat/Km for NAD+ is 30.7fold lower than wild-type value, kcat/Km for NADP+ is 1.5fold higher than wild-type value
additional information
-
expression of the xylitol dehydrogenase-encoding gene XYL2 of Pichia stipitis in the transketolase-deficient Saccharomyces cerevisiae strain results in an 8.5fold enhancement of the total amount of the excreted sugar alcohols ribitol and xylitol. The additional introduction of the 2-deoxy-glucose 6-phosphate phosphatase-encoding gene DOG1 into the transketolase-deficient strain expressing the XYL2 gene resulted in a further 1.6fold increase in ribitol production
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
the productivity and yield of xylitol fermentation by the XYL2-disrupted mutant are remarkably enhanced by screening suitable cosubstrates and optimizing the process
biotechnology
-
strain overexpressing enzyme has improved xylitol productivity, production of up to 57g/l xylitol from 225 g/l D-arabitol, via D-xylulose
synthesis
-
Gluconobacter oxydans strain NH-10 is useful for production of xylitol from D-arabitol via D-xylulose
synthesis
Gluconobacter oxydans NH-10
-
Gluconobacter oxydans strain NH-10 is useful for production of xylitol from D-arabitol via D-xylulose
-
biotechnology
-
pretreatment of sugarcane bagasse hydrolysate to eliminate toxic compounds unsuitable for use as growth medium in xylitol production. Optimization of adsorption time, type of acid used, concentration and charcoal leads to a high ratio of xylose reductase, EC1.1.1.21, to xylitol dehydrogenase, EC1.1.1.9, of 4.5
biotechnology
-
cells previously grown in sugar cane bagasse hemicellulosic hydrolysate are effective in enhancing xylitol production by keeping the xylose reductase (EC 1.1.1.21) activity at high levels, reducing the xylitol dehydrogenase (EC 1.1.1.9) activity and increasing xylitol volumetric productivity (26.5%) with respect to the inoculum cultivated in semidefined medium.Therefore, inoculum adaptation to sugar cane bagasse hemicellulosic hydrolysate is an important strategy to improve xylitol productivity
synthesis
-
use of enzyme in production of xylitol from bagasse hydrolysate, enzyme activity is higher in medium containing acetic acid than in control medium
synthesis
-
optimization of xylitol production, using fed-batch process and controlled pH 6.0 gives maximum enzyme activity
synthesis
-
the enzyme is useful for xylitol bioproduction, profiles, overview
synthesis
Meyerozyma guilliermondii FTI, Meyerozyma guilliermondii FTI 20037
-
the enzyme is useful for xylitol bioproduction, profiles, overview
-
molecular biology
-
a high thermostability of PsXDH is obtained by subsequent site-directed mutagenesis of the structural zinc-binding loop. The best mutant in this study (C4/F98R/E101F) shows a 10.8 C higher thermal transition temperature and 20.8 C higher half denaturation temperature (T1/2) compared with wild-type
synthesis
-
use of enzyme in xylose fermentation, metabolic flux partitioning from xylitol to xylulose depends on aeration and enzyme activity, increased aeration results in less xylitol accumulation and more xylulose accumulation, increase in enzyme activity can reduce xylitol formation