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 ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Metabolic pathways
-
Pentose and glucuronate interconversions
-
xylitol degradation
-
SYSTEMATIC NAME
IUBMB Comments
xylitol:NAD+ 2-oxidoreductase (D-xylulose-forming)
Also acts as an L-erythrulose reductase.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
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
Q86ZV0
-
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
SEQUENCE CODE
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
strain Y-1632
-
-
Manually annotated by BRENDA team
Candida shehatae Y-1632
strain Y-1632
-
-
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
expressed in Saccharomyces cerevisiae
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
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
Q2K0Q7, -
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
-, Q6KAV2
-
-
-
?
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
-, Q6KAV2
-
-
-
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
Q2K0Q7, -
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 shehatae Y-1632, Candida tropicalis Y-456, Scheffersomyces stipitis Y-2160
-
-
-
-
?
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
Q2K0Q7, -
0.77% of the activity with xylitol
-
-
?
galactitol + NAD+
? + NADH + H+
show the reaction diagram
Q2K0Q7, -
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
Q2K0Q7, -
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
-, Q6KAV2
-
-
-
?
L-threitol + NAD+
? + NADH + H+
show the reaction diagram
Q2K0Q7, -
0.05% of the activity with xylitol
-
-
?
L-threitol + NAD+
? + NADH + H+
show the reaction diagram
Q2K0Q7, -
75% of the activity with xylitol
-
-
?
L-xylulose + NADH
L-xylitol + NAD+
show the reaction diagram
-
-
-
-
?
ribitol + NAD+
?
show the reaction diagram
-, Q6KAV2
-
-
-
?
ribitol + NAD+
? + NADH + H+
show the reaction diagram
Q2K0Q7, -
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
P22144
-
-
-
?
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
Q8GR61
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-, Q6KAV2
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
Q2K0Q7, -
-
-
-
?
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
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 + NADH + H+
show the reaction diagram
Q8GR61
wild-type enzyme shows no activity with NADP+, mutant enzyme D38S/M39R is able to exclusively use NADP+, with no loss of activity
-
-
?
xylitol + NADP+
D-xylulose + NADPH + H+
show the reaction diagram
P22144
-
-
-
-
xylitol + NADP+
D-xylulose + NADPH + H+
show the reaction diagram
-
-
-
-
?
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 shehatae Y-1632, 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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
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
-
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
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 ACCESSION NO.
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+
-, Q6KAV2
no activity with NADP+
NAD+
P22144
kcat/Km for wild-type enzyme is 2760/min*mM
NAD+
Q8GR61
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+
Q2K0Q7
the deduced XDH gene product possesses an NAD-binding glycine-rich Rossmann fold domain [GXGXXG] present in MDR superfamily
NADH
-, Q6KAV2
no activity with NADPH
NADP+
-
xylitol oxidation favors NAD+ over NADP+, but xylulose reduction favores NADPH over NADH
NADP+
P22144
kcat/Km for wild-type enzyme is 0.65/min*mM
NADP+
Q8GR61
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
Q2K0Q7
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 ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
Q2K0Q7
1 mM, 18% of the activity with Mg2+
Co2+
Q2K0Q7
1 mM, 38% of the activity with Mg2+
Cu2+
Q2K0Q7
1 mM, 51% of the activity with Mg2+
KCl
-
slight activation
Mg2+
-
activation at high concentration
Mg2+
Q2K0Q7
or Mn2+, required
Mn2+
-
requirement
Mn2+
Q2K0Q7
or Mg2+, required. At 1 mM, 108% of the activity with Mg2+
NaCl
-
activation
NH4Cl
-
activation
Zn2+
-
0.9 molecules per subunit
Zn2+
Q2K0Q7
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
Q2K0Q7
activity is not significantly stimulated by Ba2+, Ca2+, Fe2+, Hg2+, or K+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
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
EDTA
-
dialysis overnight, 80% residual activity
EDTA
Q2K0Q7
1-10 mM, strong inhibition
HgCl2
-
complete inhibition
iodoacetate
-
complete inhibition
MgCl2
-
10 mM, 4% inhibition
NiCl2
-
1 mM, complete inhibition
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 ACCESSION NO.
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
L-arabinose
-
induces activity
Sodium acetate
-
1 g/l in reaction medium, about 15% increase of activity
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.7
-
D-ribulose
-, Q6KAV2
35C, pH 7.5, native enzyme
4
-
D-Sorbitol
-, Q6KAV2
35C, pH 7.5, native enzyme
30
-
D-Sorbitol
-
-
12
-
D-xylitol
-
pH 8.2, 22C
94
-
D-xylitol
-
-
0.66
-
D-xylulose
-
-
2
-
D-xylulose
-, Q6KAV2
35C, pH 7.5, native enzyme
10
-
D-xylulose
-
25C, pH 9.0
0.152
-
NAD+
P22144
pH 9.0, 35C, mutant enzyme D207A/I208R/F209Y
0.162
-
NAD+
P22144
pH 9.0, 35C, mutant enzyme D207A/F209S
0.25
-
NAD+
Q2K0Q7
pH 9.5, 25C
0.265
-
NAD+
P22144
pH 9.0, 35C, mutant enzyme D207A/I208R/F209T
0.348
-
NAD+
Q8GR61
pH 7.0, wild-type enzyme
0.381
-
NAD+
P22144
pH 9.0, 35, wild-type enzyme
0.403
-
NAD+
P22144
pH 9.0, 35C, mutant enzyme D207A
0.498
-
NAD+
P22144
pH 9.0, 35C, mutant enzyme I208R
0.538
-
NAD+
P22144
pH 9.0, 35C, mutant enzyme N211R
0.568
-
NAD+
P22144
pH 9.0, 35C, mutant enzyme D207A/I208R
0.665
-
NAD+
P22144
pH 9.0, 35C, mutant enzyme I208R/F209S
0.739
-
NAD+
P22144
pH 9.0, 35C, mutant enzyme S96C/S99CY102C
0.848
-
NAD+
P22144
pH 9.0, 35C, mutant enzyme F209S
1.3
-
NAD+
P22144
pH 9.0, 35C, mutant enzyme D207A/I208R/F209S
7.6
-
NAD+
P22144
pH 9.0, 35C, mutant enzym S96C/S99C/Y102C/D207A/I208R/F209S/N211R
17.3
-
NAD+
P22144
pH 9.0, 35C, mutant enzyme D207A/I208R/F209S/N211R
23.5
-
NAD+
P22144
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
0.037
-
NADH
-
-
0.0205
-
NADP+
Q8GR61
pH 7.0, mutant enzyme D38S/M39R
0.638
-
NADP+
P22144
pH 9.0, 35C, mutant enzyme D207A/I208R/F209T
0.731
-
NADP+
P22144
pH 9.0, 35C, mutant enzyme D207A/I208R/F209Y
0.897
-
NADP+
P22144
pH 9.0, 35C, mutant enzyme D207A/I208R/F209S
1.04
-
NADP+
P22144
pH 9.0, 35C, mutant enzym S96C/S99C/Y102C/D207A/I208R/F209S/N211R
1.18
-
NADP+
P22144
pH 9.0, 35C, mutant enzyme S96C/S99C/Y102C/D207A/I208R/F209S
1.38
-
NADP+
P22144
pH 9.0, 35C, mutant enzyme D207A/I208R/F209S/N211R
9.19
-
NADP+
P22144
pH 9.0, 35C, mutant enzyme I208R/F209S
9.56
-
NADP+
P22144
pH 9.0, 35C, mutant enzyme S96C/S99CY102C
9.96
-
NADP+
P22144
pH 9.0, 35C, mutant enzyme D207A/F209S
11.3
-
NADP+
P22144
pH 9.0, 35C, mutant enzyme D207A/I208R
21.1
-
NADP+
P22144
pH 9.0, 35C, mutant enzyme I208R
28.9
-
NADP+
P22144
pH 9.0, 35C, mutant enzyme F209S
56.5
-
NADP+
P22144
pH 9.0, 35C, mutant enzyme N211R
120
-
NADP+
P22144
pH 9.0, 35C, mutant enzyme D207A
170
-
NADP+
P22144
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
P22144
pH 9.0, 35C, cofactor: NADP+, mutant enzyme D207A/I208R/F209T
0.731
-
xylitol
P22144
pH 9.0, 35C, cofactor: NADP+, mutant enzyme D207A/I208R/F209Y
0.897
-
xylitol
P22144
pH 9.0, 35C, cofactor: NADP+, mutant enzyme D207A/I208R/F209S
1.04
-
xylitol
P22144
pH 9.0, 35C, cofactor: NADP+, mutant enzyme S96C/S99C/Y102C/D207A/I208R/F209S/N211R
1.18
-
xylitol
P22144
pH 9.0, 35C, cofactor: NADP+, mutant enzyme S96C/S99C/Y102C/D207A/I208R/F209S
1.38
-
xylitol
P22144
pH 9.0, 35C, cofactor: NADP+, mutant enzyme D207A/I208R/F209S/N211R
4
5.4
xylitol
P22144
pH 9.0, 35C, cofactor: NAD+, mutant enzyme I208R/F209S
4
-
xylitol
-, Q6KAV2
35C, pH 7.5, native enzyme
5.2
-
xylitol
-, Q6KAV2
35C, pH 7.5, recombinant enzyme
7.1
-
xylitol
-
-
9.56
-
xylitol
P22144
pH 9.0, 35C, cofactor: NADP+, mutant enzyme S96C/S99CY102C
9.96
-
xylitol
P22144
pH 9.0, 35C, cofactor: NADP+, mutant enzyme D207A/F209S
12.1
-
xylitol
Q2K0Q7
pH 9.5, 25C
12.6
-
xylitol
-
-
13.7
-
xylitol
Q8GR61
pH 7.0, cofactor: NAD+, wild-type enzyme
16.4
-
xylitol
-
-
18.5
-
xylitol
-
-
21.7
-
xylitol
P22144
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
P22144
pH 9.0, 35C, cofactor: NAD+, mutant enzyme D207A
24.2
-
xylitol
P22144
pH 9.0, 35C, cofactor: NAD+, mutant enzyme D207A/I208R
27.4
-
xylitol
P22144
pH 9.0, 35C, cofactor: NAD+, mutant enzyme N211R
29.5
-
xylitol
P22144
pH 9.0, 35C, cofactor: NAD+, mutant enzyme I208R
30.3
-
xylitol
P22144
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
P22144
pH 9.0, 35C, cofactor: NAD+, mutant enzyme F209S
45.2
-
xylitol
P22144
pH 9.0, 35C, cofactor: NAD+, mutant enzyme D207A/F209S
49.8
-
xylitol
-
-
50.1
-
xylitol
P22144
pH 9.0, 35C, cofactor: NAD+, mutant enzyme D207A/I208R/F209Y
55.7
-
xylitol
P22144
pH 9.0, 35C, cofactor: NAD+, mutant enzyme D207A/I208R/F209S
97.8
-
xylitol
P22144
pH 9.0, 35C, cofactor: NAD+, mutant enzyme D207A/I208R/F209T
100
-
xylitol
Q8GR61
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
-, Q6KAV2
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]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
920
-
D-fructose
-
25C, pH 7.5, Tris-HCl
74
-
D-ribulose
-, Q6KAV2
35C, pH 7.5, native enzyme
114
-
D-Sorbitol
-
25C, pH 7.5, Tris-HCl
528
-
D-Sorbitol
-, Q6KAV2
35C, pH 7.5, native enzyme
302.9
-
D-xylulose
-, Q6KAV2
35C, pH 7.5, native enzyme
1500
-
D-xylulose
-
25C, pH 7.5, Tris-HCl
1800
-
D-xylulose
-
25C, pH 7.5, potassium phosphate
216
-
L-sorbose
-, Q6KAV2
35C, pH 7.5, native enzyme
0.052
2.1
NAD+
P22144
pH 9.0, 35C, mutant enzyme D207A/I208R
0.5
-
NAD+
P22144
pH 9.0, 35C, mutant enzym S96C/S99C/Y102C/D207A/I208R/F209S/N211R
1
-
NAD+
P22144
pH 9.0, 35C, mutant enzyme D207A/I208R/F209Y; pH 9.0, 35C, mutant enzyme I208R/F209S
3.33
-
NAD+
P22144
pH 9.0, 35C, mutant enzyme D207A/F209S
4
-
NAD+
P22144
pH 9.0, 35C, mutant enzyme D207A/I208R/F209S
5.17
-
NAD+
P22144
pH 9.0, 35C, mutant enzyme D207A; pH 9.0, 35C, mutant enzyme D207A/I208R/F209T
10.33
-
NAD+
P22144
pH 9.0, 35C, mutant enzyme D207A/I208R
13.17
-
NAD+
P22144
pH 9.0, 35C, mutant enzym S96C/S99C/Y102C/D207A/I208R/F209S/N211R
16.9
-
NAD+
P22144
pH 9.0, 35C, mutant enzyme N211R
17.5
-
NAD+
P22144
pH 9.0, 35, wild-type enzyme
18
-
NAD+
P22144
pH 9.0, 35C, mutant enzyme D207A/I208R/F209S/N211R
20.33
-
NAD+
P22144
pH 9.0, 35C, mutant enzyme F209S
22.83
-
NAD+
P22144
pH 9.0, 35C, mutant enzyme N211R
23.8
-
NAD+
P22144
pH 9.0, 35C, mutant enzyme I208R
23.83
-
NAD+
P22144
pH 9.0, 35C, mutant enzyme D207A/I208R/F209S/N211R
27.2
-
NAD+
Q8GR61
pH 7.0, wild-type enzyme
29.5
-
NAD+
P22144
pH 9.0, 35C, mutant enzyme S96C/S99C/Y102C/D207A/I208R/F209S
30.33
-
NAD+
P22144
pH 9.0, 35C, mutant enzyme S96C/S99CY102C
0.017
-
NADP+
P22144
pH 9.0, 35C, mutant enzyme D207A/I208R/F209T
0.145
-
NADP+
P22144
pH 9.0, 35C, mutant enzyme I208R/F209S
0.206
-
NADP+
Q8GR61
pH 7.0, mutant enzyme D38S/M39R
0.91
-
NADP+
P22144
pH 9.0, 35C, mutant enzyme S96C/S99CY102C
1.83
-
NADP+
P22144
pH 9.0, 35, wild-type enzyme
2
8
NADP+
P22144
pH 9.0, 35C, mutant enzyme D207A/I208R
4.67
-
NADP+
P22144
pH 9.0, 35C, mutant enzyme N211R
5.7
-
NADP+
P22144
pH 9.0, 35C, mutant enzyme D207A
6.17
-
NADP+
P22144
pH 9.0, 35C, mutant enzyme D207A/I208R/F209Y
8
-
NADP+
P22144
pH 9.0, 35C, mutant enzyme D207A/F209S
9.83
-
NADP+
P22144
pH 9.0, 35C, mutant enzyme F209S
10
-
NADP+
P22144
pH 9.0, 35C, mutant enzyme I208R
32.83
-
NADP+
P22144
pH 9.0, 35C, mutant enzyme D207A/I208R/F209T
41.7
-
NADP+
P22144
pH 9.0, 35C, mutant enzyme D207A/I208R/F209S
64
-
NADP+
P22144
pH 9.0, 35C, mutant enzyme D207A/I208R/F209S/N211R
183.3
-
NADP+
P22144
pH 9.0, 35C, mutant enzym S96C/S99C/Y102C/D207A/I208R/F209S/N211R
210
-
NADP+
P22144
pH 9.0, 35C, mutant enzyme S96C/S99C/Y102C/D207A/I208R/F209S
1.19
-
Sorbitol
-
mutant E154C
2
8
Sorbitol
-
-
161
-
Sorbitol
-
-
17.9
-
xylitol
Q8GR61
pH 7.0, cofactor: NADP+mutant enzyme D38S/M39R
24.6
-
xylitol
Q8GR61
pH 7.0, cofactor: NAD+, wild-type enzyme
143
-
xylitol
-
25C, pH 7.5, Tris-HCl
170
-
xylitol
-
25C, pH 7.5, potassium phosphate
2115
-
xylitol
-, Q6KAV2
35C, pH 7.5, recombinant enzyme
2644
-
xylitol
-, Q6KAV2
35C, pH 7.5, native enzyme
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
10
-
D-xylulose
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.005
-
ZnSO4
-
value identical for wildtype and for mutant E154C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
15.95
-
-
-
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
-
P22144
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
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
-
-, Q6KAV2
native and recombinant enzyme
8.6
-
-
oxidation of erythritol
8.6
-
-
D-xylulose formation
9.1
10
-
substrate oxidation, plateau
9.5
-
Q2K0Q7
-
10.5
11
-
oxidation reaction
11
-
-
oxidation of xylitol
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
assay at
30
-
-
reduction reaction
35
-
-, Q6KAV2
native and recombinant enzyme
35
-
-
oxidation reaction
70
-
Q2K0Q7
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
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
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
72000
-
-, Q6KAV2
native enzyme, gel filtration, non-denaturing PAGE
80000
-
-, Q6KAV2
recombinant enzyme, gel filtration, non-denaturing PAGE
82000
-
-
gel filtration
94000
-
-
PAGE
120000
-
-
gel filtration
130000
-
-
PAGE
135000
-
Q2K0Q7
gel filtration
142000
-
-
PAGE
155000
-
-
PAGE
160000
-
-
gel filtration
160000
-
-
gel filtration, protein is a homotetramer
172000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 27800, deduced from genen sequence, x * 27000, SDS-PAGE
?
-, Q86ZV0
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
-, Q6KAV2
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
Q2K0Q7
4 * 35858, calculated, 4 * 34000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hanging drop vapor diffusion method, crystal structure of the holoenzyme to 1.9 A resolution
Q8GR61
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
Q2K0Q7
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
7
-
24 h, fully stable
6.8
7.4
-
90% of maximal activity retained at pH 6.8 and 7.4 at 2C
7
-
-
24 h stable at 2C
7.2
7.9
-, Q6KAV2
stable
8
10
-
4C, 60 min, stable
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0
40
-
10 min, 2.5 mM NAD+, stable
20
-
-
at room temperature, the enzyme is inactivated within 2 days
25
-
-
and below stable
30
-
-
1 h, completely stable
40
-
Q2K0Q7
half-life 120 min
50
-
-
1 h, no residual activity
50
-
-
10 min, 2.5 mM NAD+, about 50% loss of activity
53.1
-
Q2K0Q7
half denaturation temperature
60
-
-
complete inactivation within 5 min
60
-
-
10 min, 2.5 mM NAD+, about 80% loss of activity
additional information
-
-
wild-type: half denaturation temperature T1/2 (C): 35.2, thermal transition temperature Tcd (C): 43.0
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
LITERATURE
Acetone
-
stable to precipitation with 50% v/v
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, stable with 50% v/v glycerol
-
-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
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
Q2K0Q7
recombinant enzyme
P22144
using Ni-NTA chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-, Q6KAV2
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
Q2K0Q7
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
P22144
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 ACCESSION NO.
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
P22144
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
P22144
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
P22144
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
P22144
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
P22144
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
P22144
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
P22144
kcat/Km for NAD+ is 6.9fold lowerthan wild-type value, kcat/Km for NADP+ is 788fold higher than wild-type value
F209S
P22144
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
P22144
kcat/Km for NAD+ is nearly identical to wild-type value, kcat/Km for NADP+ is 44fold higher than wild-type value
N211R
P22144
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
P22144
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
P22144
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
P22144
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
Q8GR61
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
P22144
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 ACCESSION NO.
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