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adonitol + NAD+
? + NADH
-
-
-
-
?
adonitol + NAD+
? + NADH + H+
-
-
-
?
D-adonitol + NAD+
?
-
-
-
-
?
D-allitol + NAD+
D-psicose + NADH
-
-
-
-
r
D-arabino-3-hexulose + NADH
D-talitol + NAD+
-
-
-
-
r
D-fructose + NADH + H+
D-sorbitol + NAD+
-
-
-
-
r
D-psicose + NADH
D-allitol + NAD+
-
-
-
-
?
D-sorbitol + NAD+
? + NADH + H+
wild-type shows no activity on D-sorbitol, whereas mutant Y318F does
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
D-sorbose + NADH
D-gulitol + NAD+
-
-
-
-
?
galactitol + NAD+
L-xylo-3-hexulose + NADH
-
-
-
-
r
L-arabinitol + NAD+
? + NADH
-
-
-
-
?
L-arabinitol + NAD+
L-xylulose + NADH
L-arabinitol + NAD+
L-xylulose + NADH + H+
L-arabinitol + NADP+
L-xylulose + NADPH + H+
no activity with cofactor NADP+ for wild-type
-
-
?
L-arabitol + NAD+
L-xylulose + NADH + H+
L-iditol + NAD+
L-sorbose + NADH
-
-
-
-
r
L-mannitol + NAD+
L-fructose + NADH
-
-
-
-
r
L-sorbitol + NAD+
? + NADH
-
-
-
-
?
L-tagatose + NADH
L-talitol + NAD+
-
-
-
-
?
L-talitol + NAD+
D-arabino-3-hexulose + NADH
-
-
-
-
r
L-xylo-3-hexulose + NADH
galactitol + NAD+
-
-
-
-
r
ribitol + NAD+
?
93% of the activity with L-arabinitol
-
-
?
ribitol + NAD+
D-ribulose + NADH + H+
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
xylitol + NADP+
D-xylulose + NADPH + H+
very low activity with NADP+
-
-
r
additional information
?
-
D-sorbitol + NAD+
D-fructose + NADH + H+
-
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
-
-
r
D-sorbitol + NAD+
D-fructose + NADH + H+
-
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
-
-
-
-
r
L-arabinitol + NAD+
L-xylulose + NADH
-
-
-
?
L-arabinitol + NAD+
L-xylulose + NADH
-
-
-
?
L-arabinitol + NAD+
L-xylulose + NADH + H+
-
-
-
r
L-arabinitol + NAD+
L-xylulose + NADH + H+
-
-
-
-
?
L-arabinitol + NAD+
L-xylulose + NADH + H+
-
-
-
-
r
L-arabinitol + NAD+
L-xylulose + NADH + H+
-
-
-
?
L-arabinitol + NAD+
L-xylulose + NADH + H+
-
enzyme of the L-arabinose catabolic pathway
-
-
r
L-arabinitol + NAD+
L-xylulose + NADH + H+
-
-
-
?
L-arabinitol + NAD+
L-xylulose + NADH + H+
-
-
-
-
?
L-arabinitol + NAD+
L-xylulose + NADH + H+
-
-
-
?
L-arabinitol + NAD+
L-xylulose + NADH + H+
-
-
-
?
L-arabinitol + NAD+
L-xylulose + NADH + H+
-
-
-
?
L-arabinitol + NAD+
L-xylulose + NADH + H+
-
-
-
?
L-arabinitol + NAD+
L-xylulose + NADH + H+
-
-
-
?
L-arabinitol + NAD+
L-xylulose + NADH + H+
-
-
-
?
L-arabinitol + NAD+
L-xylulose + NADH + H+
-
-
-
-
?
L-arabinitol + NAD+
L-xylulose + NADH + H+
-
L-arabitol consumption rate by resting cells is of the same order of magnitude as the LAD activity determined for crude cell extracts. The strong accumulation of L-arabitol (intracellular concentration of up to 0.4 M) during aerobic L-arabinose metabolism indicates the existence of a bottleneck at the level of LAD
-
-
?
L-arabinitol + NAD+
L-xylulose + NADH + H+
-
L-arabitol consumption rate by resting cells is of the same order of magnitude as the LAD activity determined for crude cell extracts. The strong accumulation of L-arabitol (intracellular concentration of up to 0.4 M) during aerobic L-arabinose metabolism indicates the existence of a bottleneck at the level of LAD
-
-
?
L-arabinitol + NAD+
L-xylulose + NADH + H+
-
-
-
-
?
L-arabinitol + NAD+
L-xylulose + NADH + H+
-
-
-
-
?
L-arabinitol + NAD+
L-xylulose + NADH + H+
-
-
-
?
L-arabinitol + NAD+
L-xylulose + NADH + H+
-
-
-
?
L-arabinitol + NAD+
L-xylulose + NADH + H+
-
-
-
r
L-arabinitol + NAD+
L-xylulose + NADH + H+
-
-
-
?
L-arabinitol + NAD+
L-xylulose + NADH + H+
-
-
-
?
L-arabinitol + NAD+
L-xylulose + NADH + H+
-
-
-
-
?
L-arabinitol + NAD+
L-xylulose + NADH + H+
-
-
-
?
L-arabinitol + NAD+
L-xylulose + NADH + H+
-
-
-
r
L-arabinitol + NAD+
L-xylulose + NADH + H+
-
-
-
?
L-arabinitol + NAD+
L-xylulose + NADH + H+
-
-
-
-
?
L-arabinitol + NAD+
L-xylulose + NADH + H+
-
-
-
-
?
L-arabinitol + NAD+
L-xylulose + NADH + H+
-
-
-
-
?
L-arabitol + NAD+
L-xylulose + NADH + H+
-
-
-
?
L-arabitol + NAD+
L-xylulose + NADH + H+
about 20% activity compared to xylitol
-
-
r
L-arabitol + NAD+
L-xylulose + NADH + H+
-
-
-
-
r
L-arabitol + NAD+
L-xylulose + NADH + H+
-
-
-
-
r
Xylitol + NAD+
?
17% of the activity with L-arabinitol
-
-
?
Xylitol + NAD+
?
-
-
-
-
?
Xylitol + NAD+
?
-
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
preferred substrates, reaction of EC 1.1.1.9
-
-
r
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
-
-
-
-
?
additional information
?
-
Y318 of LadA contributes significantly to the substrate specificity difference between LAD and xylitol dehydrogenase/D-sorbitol dehydrogenase
-
-
?
additional information
?
-
-
Y318 of LadA contributes significantly to the substrate specificity difference between LAD and xylitol dehydrogenase/D-sorbitol dehydrogenase
-
-
?
additional information
?
-
the enzyme exhibits broad specificity to polyols, such as xylitol, D-sorbitol, ribitol (cf. EC 1.1.1.56), and L-arabitol. Xylitol is the preferred substrate, but native and recombinant enzyme McXDH exhibits relative activities toward L-arabinitol of approximately 20% that toward xylitol
-
-
?
additional information
?
-
-
the enzyme exhibits broad specificity to polyols, such as xylitol, D-sorbitol, ribitol (cf. EC 1.1.1.56), and L-arabitol. Xylitol is the preferred substrate, but native and recombinant enzyme McXDH exhibits relative activities toward L-arabinitol of approximately 20% that toward xylitol
-
-
?
additional information
?
-
the enzyme has L-arabitol dehydrogenase (LAD) activity and also exhibits broad specificity to polyols, such as xylitol, D-sorbitol, and ribitol. Xylitol is the preferred substrate (EC 1.1.1.9)
-
-
-
additional information
?
-
-
the enzyme has L-arabitol dehydrogenase (LAD) activity and also exhibits broad specificity to polyols, such as xylitol, D-sorbitol, and ribitol. Xylitol is the preferred substrate (EC 1.1.1.9)
-
-
-
additional information
?
-
the enzyme exhibits broad specificity to polyols, such as xylitol, D-sorbitol, ribitol (cf. EC 1.1.1.56), and L-arabitol. Xylitol is the preferred substrate, but native and recombinant enzyme McXDH exhibits relative activities toward L-arabinitol of approximately 20% that toward xylitol
-
-
?
additional information
?
-
-
the enzyme exhibits broad specificity to polyols, such as xylitol, D-sorbitol, ribitol (cf. EC 1.1.1.56), and L-arabitol. Xylitol is the preferred substrate, but native and recombinant enzyme McXDH exhibits relative activities toward L-arabinitol of approximately 20% that toward xylitol
-
-
?
additional information
?
-
-
no substrate: D-mannitol, D-arabinitol, D-sorbitol
-
-
?
additional information
?
-
no substrate: D-arabinitol. The promiscuity of LAD towards different substrates is restricted to five-carbon sugars, and no activity is observed towards either D-sorbitol or D-mannitol
-
-
?
additional information
?
-
-
no substrate: D-arabinitol. The promiscuity of LAD towards different substrates is restricted to five-carbon sugars, and no activity is observed towards either D-sorbitol or D-mannitol
-
-
?
additional information
?
-
-
enzyme contributes to 30% of total xylitol dehydrogenase activity, enzyme can partially compensate for loss of xylitol dehydrogenase function
-
-
?
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Zn2+
zinc metalloenzyme
Zn2+
required, the zinc ADH signature and conserved coenzyme binding motif are observed in the amino acid sequence of McXDH at positions 65-76 and 183-188 and are completely conserved among McXDH and XDHs from other yeasts and filamentous fungi
Zn2+
-
two ions per subunit
Zn2+
a structural zinc ion is situated at a loop region located adjacent to the catalytic domain, where it is ligated by enzyme residues Cys108, Cys111, Cys114, and Cys122. The catalytically requisite zinc ion constitutes the second metal found in each monomer of LAD. This metal is coordinated by residues Cys53, His78, and Glu79, with a water molecule completing a near-tetrahedral coordination sphere
Zn2+
structure analysis indicates that enzyme belongs to the family of Zn2+-containing, medium-chain alcohol dehydrogenases. Residues involved in Zn2+ binding are C55, H80, and E165. Thereis a second zinc-binding site C110, C113, C116, and C124
Zn2+
catalytic Zn2+ binding domain involving residues Cys66, His91, Glu92 and Glu176, molecular docking studies
Zn2+
the Cys66, His91, Glu92, and Glu176 residues are involved in coordination of catalytic Zn2+ along with a water molecule
additional information
after incubation with ZnSO4, ZnCl2, FeCl2, and CuCl2, 40, 37, 30, and 25%, respectively, of the activity of the metal-free enzyme is restored. Poorer effects by Fe3+, Cd2+, and Ca2+, while Ni2+, Mn2+, Co2+, Mg2+, K+, and Na+ do not exert restorative effects
additional information
-
after incubation with ZnSO4, ZnCl2, FeCl2, and CuCl2, 40, 37, 30, and 25%, respectively, of the activity of the metal-free enzyme is restored. Poorer effects by Fe3+, Cd2+, and Ca2+, while Ni2+, Mn2+, Co2+, Mg2+, K+, and Na+ do not exert restorative effects
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35
adonitol
-
pH 8.0, 25°C
11.3
D-allitol
-
pH 8.6, 25°C
580
D-arabino-3-hexulose
-
pH 8.6, 25°C
96
D-fructose
-
pH 8.6, 25°C
81
D-psicose
-
pH 8.6, 25°C
115
D-sorbose
-
pH 8.6, 25°C
25
D-talitol
-
pH 8.6, 25°C
60
galactitol
-
pH 8.6, 25°C
191
L-Iditol
-
pH 8.6, 25°C
37
L-mannitol
-
pH 8.6, 25°C
19
L-sorbitol
-
pH 8.6, 25°C
28
L-tagatose
-
pH 8.6, 25°C
81
L-xylo-3-hexulose
-
pH 8.6, 25°C
5
L-xylulose
-
30°C, pH 9.6
0.008
NADH
-
30°C, pH 9.6
15.8
ribitol
pH 7.0, 30°C, native enzyme
0.868
D-sorbitol
mutant Y318F, pH 9.6, 20°C
4.12
D-sorbitol
wild-type, pH 9.6, 20°C
4.122
D-sorbitol
wild-type
4.868
D-sorbitol
mutant Y318F
21.2
D-sorbitol
pH 7.0, 30°C, native enzyme
46
D-sorbitol
-
pH 8.6, 25°C
483.5
D-sorbitol
pH 9, 30°C
0.056
L-arabinitol
wild-type, pH 9.6, 20°C
0.078
L-arabinitol
mutant Y318F, pH 9.6, 20°C
4.5
L-arabinitol
-
pH 8.6, 25°C
8 - 9
L-arabinitol
-
30°C, pH 9.6
13.4
L-arabinitol
pH 9, 30°C
14.5
L-arabinitol
pH 9.5, 25°C
17.2
L-arabinitol
pH 8.0, 25°C
18
L-arabinitol
-
pH 8.0, 25°C
18
L-arabinitol
pH 7.0, 22°C
18
L-arabinitol
pH 8.0, 25°C, free recombinant enzyme
18.2
L-arabinitol
pH 7.0, 25°C
21.3
L-arabinitol
pH 8.0, 25°C, immobilzed recombinant enzyme in nanoflowers
25
L-arabinitol
pH 7.0, 22°C
31.1
L-arabinitol
recombinant enzyme, pH 7.0, 30°C
37
L-arabinitol
pH 7.0, 22°C
0.056
L-arabitol
wild-type
0.078
L-arabitol
mutant Y318F
31.1
L-arabitol
pH 7.0, 30°C, native enzyme
132
L-arabitol
pH 7.0, 30°C, recombinant enzyme
0.05
NAD+
-
30°C, pH 9.6
0.1
NAD+
pH 7.0, 30°C, recombinant enzyme, with xylitol
0.11
NAD+
pH 7.0, 30°C, native enzyme, with xylitol
0.14
NAD+
wild-type, pH 8.0, 25°C
2.9
NAD+
mutant D211S, pH 8.0, 25°C
3.6
NAD+
mutant D211S/I212R, pH 8.0, 25°C
5
NAD+
or above, mutant D211S/I212R/D213N, pH 8.0, 25°C
5
NAD+
or above, mutant D211S/I212R/S348T, pH 8.0, 25°C
0.48
NADP+
mutant D211S/I212R, pH 8.0, 25°C
0.55
NADP+
mutant D211S/I212R/S348T, pH 8.0, 25°C
1.45
NADP+
mutant D211S/I212R/D213N, pH 8.0, 25°C
5
NADP+
or above, mutant D211S, pH 8.0, 25°C
7.28
NADP+
pH 7.0, 30°C, native enzyme, with xylitol
8
NADP+
or above, wild-type, pH 8.0, 25°C
0.218
xylitol
mutant Y318F
0.218
xylitol
mutant Y318F, pH 9.6, 20°C
0.25
xylitol
wild-type, pH 9.6, 20°C
16
xylitol
pH 7.0, 30°C, recombinant enzyme
16.1
xylitol
pH 7.0, 30°C, native enzyme
290
xylitol
-
pH 8.0, 25°C
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evolution
the enzyme belongs to a medium-chain dehydrogenase/reductase (MDR) superfamily and a subfamily of polyol dehydrogenase, PDH
evolution
the enzyme belongs to the medium-chain dehydrogenase/reductase (MDR) superfamily and polyol dehydrogenase (PDH) subfamily. The enzyme contains the typical NAD+-binding motif GxGxxG of MDR family enzymes
evolution
-
the enzyme belongs to a medium-chain dehydrogenase/reductase (MDR) superfamily and a subfamily of polyol dehydrogenase, PDH
-
evolution
-
the enzyme belongs to the medium-chain dehydrogenase/reductase (MDR) superfamily and polyol dehydrogenase (PDH) subfamily. The enzyme contains the typical NAD+-binding motif GxGxxG of MDR family enzymes
-
malfunction
disruption of the L-arabitol dehydrogenase encoding gene in Aspergillus tubingensis results in increased xylanase production. The xylanase overproducing phenotype is mainly caused by loss of ladA function, while improved xylanase production is mediated by XlnR
malfunction
disruption of the L-arabitol dehydrogenase encoding gene in Aspergillus tubingensis results in increased xylanase production. The xylanase overproducing phenotype is mainly caused by loss of ladA function, while improved xylanase production is mediated by XlnR. The ladA locus is the direct cause of the increased xylanase activity of 3M-43, a pyrA mutant of 3M-43
malfunction
-
disruption of the L-arabitol dehydrogenase encoding gene in Aspergillus tubingensis results in increased xylanase production. The xylanase overproducing phenotype is mainly caused by loss of ladA function, while improved xylanase production is mediated by XlnR
-
metabolism
the enzyme is involved in the L-arabinose catabolic pathway
metabolism
-
Yarrowia lipolytica strain ATCC MYA-2613 has endogenous enzymes for D-xylose assimilation, but inefficient xylitol dehydrogenase causes Yarrowia lipolytica to assimilate xylose poorly. L-Arabitol dehydrogenase is the rate-limiting step responsible for poor arabinose utilization in Yarrowia lipolytica. Functional roles of native sugar-specific transporters for activating the dormant pentose metabolism in Yarrowia lipolytica, cryptic pentose metabolism and native L-arabinose assimilation pathway, overview. TRP6Yli and TRP22Yli are xylose-specific transporters in Yarrowia lipolytica. L-Arabinose is first reduced into L-arabitol by NAD(P)H-dependent arabinose reductase (ARD), which is then converted into L-xylulose by NAD(P)+-dependent arabitol dehydrogenase (ADH). L-Xylulose is then converted to D-xylitol by NAD(P)H-dependent xylulose reductase (XLR), which is further assimilated to D-xylulose-5-phosphate, a precursor for the pentose-phosphate pathway (PPP)
metabolism
-
Yarrowia lipolytica strain ATCC MYA-2613 has endogenous enzymes for D-xylose assimilation, but inefficient xylitol dehydrogenase causes Yarrowia lipolytica to assimilate xylose poorly. L-Arabitol dehydrogenase is the rate-limiting step responsible for poor arabinose utilization in Yarrowia lipolytica. Functional roles of native sugar-specific transporters for activating the dormant pentose metabolism in Yarrowia lipolytica, cryptic pentose metabolism and native L-arabinose assimilation pathway, overview. TRP6Yli and TRP22Yli are xylose-specific transporters in Yarrowia lipolytica. L-Arabinose is first reduced into L-arabitol by NAD(P)H-dependent arabinose reductase (ARD), which is then converted into L-xylulose by NAD(P)+-dependent arabitol dehydrogenase (ADH). L-Xylulose is then converted to D-xylitol by NAD(P)H-dependent xylulose reductase (XLR), which is further assimilated to D-xylulose-5-phosphate, a precursor for the pentose-phosphate pathway (PPP)
-
metabolism
-
the enzyme is involved in the L-arabinose catabolic pathway
-
physiological function
induction of gene expression of the alpha-L-arabinofuranosidase encoding genes abf1, abf2, and abf3 and also bxl1, which encodes a beta-xylosidase with a separate alpha-L-arabinofuranosidase domain and activity, by L-arabinitol is strongly enhanced in a DELTAlad1 strain lacking L-arabinitol dehydrogenase activity and severely impaired in an aldose reductase DELTAxyl1 strain, suggesting a cross talk between L-arabinitol and the aldose reductase XYL1 in alpha-L-arabinofuranosidase gene expression
physiological function
the organism catabolizes L-arabinose as well as D-glucose and D-xylose. The highest production amounts of ethanol from D-glucose, xylitol from D-xylose, and L-arabitol from L-arabinose were 0.45 g/g D-glucose, 0.60 g/g D-xylose, and 0.61 g/g L-arabinose with 21.7 g/l ethanol, 20.2 g/l xylitol, and 30.3 g/l L-arabitol, respectively. The enzyme has L-arabitol dehydrogenase (LAD) activity and also exhibits broad specificity to polyols, such as xylitol, D-sorbitol, ribitol, and L-arabitol. Xylitol is the preferred substrate
physiological function
-
the organism catabolizes L-arabinose as well as D-glucose and D-xylose. The highest production amounts of ethanol from D-glucose, xylitol from D-xylose, and L-arabitol from L-arabinose were 0.45 g/g D-glucose, 0.60 g/g D-xylose, and 0.61 g/g L-arabinose with 21.7 g/l ethanol, 20.2 g/l xylitol, and 30.3 g/l L-arabitol, respectively. The enzyme has L-arabitol dehydrogenase (LAD) activity and also exhibits broad specificity to polyols, such as xylitol, D-sorbitol, ribitol, and L-arabitol. Xylitol is the preferred substrate
-
additional information
homology modeling and docking of L-arabinitol in the substrate-binding pocket of HjLAD suggesting routes of hydride transfer, where the key amino acid residues comprise the core region, molecular dynamics, overview
additional information
-
homology modeling and docking of L-arabinitol in the substrate-binding pocket of HjLAD suggesting routes of hydride transfer, where the key amino acid residues comprise the core region, molecular dynamics, overview
additional information
three-dimensional structure homology modelling, overview
additional information
-
three-dimensional structure homology modelling, overview
additional information
xylitol production of wild-type and mutant strains, overview
additional information
-
xylitol production of wild-type and mutant strains, overview
additional information
xylitol production of wild-type and mutant strains, overview
additional information
-
xylitol production of wild-type and mutant strains, overview
-
additional information
-
xylitol production of wild-type and mutant strains, overview
-
additional information
-
three-dimensional structure homology modelling, overview
-
additional information
-
homology modeling and docking of L-arabinitol in the substrate-binding pocket of HjLAD suggesting routes of hydride transfer, where the key amino acid residues comprise the core region, molecular dynamics, overview
-
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D213S/I214R
significantly higher preference for NADP+ over NAD+
D211S
strong decrease in activity
D211S/I212R
strong decrease in activity, increase in activity with cofactor NADP+
D211S/I212R/D213N
strong decrease in activity, increase in activity with cofactor NADP+
D211S/I212R/S348T
strong decrease in activity, increase in activity with cofactor NADP+
D224S/I225R
significantly altered cofactor specificity from NAD+ to NADP+
M70F
almost complete loss of activity
M70F
results in a nearly complete enzyme inactivation
Y318F
results in a significant increase in affinity for D-sorbitol, xylitol and L-arabitol
Y318F
increased activity for L-arabinitol and xylitol, increased affinity for D-sorbitol
D212S/I213R
no activity with NAD+, slight activity with NADP+
D212S/I213R
-
no activity with NAD+, slight activity with NADP+
-
H91A
site-directed mutagenesis, catalytically inactive mutant
H91A
-
site-directed mutagenesis, catalytically inactive mutant
-
additional information
construction of deletion mutants of ladA and ladA-xdhA, to generate mutants with decreased dehydrogenase activities and increased xylitol production. Genomic DNA from Aspergillus oryzae strain KBN616 is used as the template for amplification of the three xdhA and ladA inserts. Activities of xylitol dehydrogenase and xylose reductase in the mutant strains, phenotype, overview
additional information
-
construction of deletion mutants of ladA and ladA-xdhA, to generate mutants with decreased dehydrogenase activities and increased xylitol production. Genomic DNA from Aspergillus oryzae strain KBN616 is used as the template for amplification of the three xdhA and ladA inserts. Activities of xylitol dehydrogenase and xylose reductase in the mutant strains, phenotype, overview
additional information
construction of deletion mutants of ladA by homologous transformation, to generate mutants with decreased dehydrogenase activities and increased xylitol production. Gene pyrG is used as a selectable marker. Consumption of D-xylose for xdhA2-1 and ladA2-1 is similar to that of KBN616. Mutant ladA2-1 displays the reduced xylitol productivity
additional information
-
construction of deletion mutants of ladA and ladA-xdhA, to generate mutants with decreased dehydrogenase activities and increased xylitol production. Genomic DNA from Aspergillus oryzae strain KBN616 is used as the template for amplification of the three xdhA and ladA inserts. Activities of xylitol dehydrogenase and xylose reductase in the mutant strains, phenotype, overview
-
additional information
-
construction of deletion mutants of ladA by homologous transformation, to generate mutants with decreased dehydrogenase activities and increased xylitol production. Gene pyrG is used as a selectable marker. Consumption of D-xylose for xdhA2-1 and ladA2-1 is similar to that of KBN616. Mutant ladA2-1 displays the reduced xylitol productivity
-
additional information
gene disruption of the L-arabitol dehydrogenase encoding gene resulting in increased xylanase production. Complementation with constitutively expressed ladA confirms that the xylanase overproducing phenotype is mainly caused by loss of ladA function, while a knockout of xlnR in the UV mutant demonstrates that improved xylanase production is mediated by XlnR
additional information
JQ079782
gene disruption of the L-arabitol dehydrogenase encoding gene resulting in increased xylanase production. Complementation with constitutively expressed ladA confirms that the xylanase overproducing phenotype is mainly caused by loss of ladA function, while a knockout of xlnR in the UV mutant demonstrates that improved xylanase production is mediated by XlnR
additional information
-
gene disruption of the L-arabitol dehydrogenase encoding gene resulting in increased xylanase production. Complementation with constitutively expressed ladA confirms that the xylanase overproducing phenotype is mainly caused by loss of ladA function, while a knockout of xlnR in the UV mutant demonstrates that improved xylanase production is mediated by XlnR
additional information
-
gene disruption of the L-arabitol dehydrogenase encoding gene resulting in increased xylanase production. Complementation with constitutively expressed ladA confirms that the xylanase overproducing phenotype is mainly caused by loss of ladA function, while a knockout of xlnR in the UV mutant demonstrates that improved xylanase production is mediated by XlnR
-
additional information
-
gene disruption mutant, almost unable to grow on L-arabinose, extremely weak growth on L-arabinitol, D-talitol, galactitol
additional information
all tested wild-type and mutant enzymes have a similar secondary structure and the global folding of mutant and wild-type HjLAD is similar
additional information
-
all tested wild-type and mutant enzymes have a similar secondary structure and the global folding of mutant and wild-type HjLAD is similar
additional information
preparation of a metal-protein hybrid nanoflower system for efficient immobilization of the recombinant enzyme L-arabinitol 4-dehydrogenase from Hypocrea jecorina (HjLAD). Synthesis of enzyme-Cu(PO4)2 x 3H2O hybrid nanoflowers and encapsulation of His-tagged enzyme, FESEM images, overview. Compared with the free enzyme, the synthesized hybrid nanoflower exhibit enhanced enzymatic activity of 246% for HjLAD. The immobilized enzyme retains high catalytic activity and shows improved he tolerance towards pH and temperature changes. Synthesized nanoflowers also retain high storage stability and reusability. In addition, the immobilized enzyme exhibits significantly enhanced L-xylulose production under cofactor regeneration conditions compared to the free enzyme combination
additional information
-
all tested wild-type and mutant enzymes have a similar secondary structure and the global folding of mutant and wild-type HjLAD is similar
-
additional information
-
overexpression of native pentose-specific transporters together with the rate-limiting D-xylitol and L-arabitol dehydrogenases, the dormant pentose metabolism of Yarrowia lipolytica is activated, overview. Recombinant overexpression of a heterologous L-arabitol dehydrogenase of Aspergillus oryzae (ADHAoz), in Yarrowia lipolytica strain YlSR157 using the constitutive TEF promoter, ADHAoz is chosen because it exhibits higher activity toward L-arabitol (39.2 mU/mg protein) than D-xylitol (6.54 mU/mg protein). Unlike strain YlSR102, strain YlSR157 grows faster and consumes more sugars when growing on both single arabinose and mixed pentose sugars
additional information
-
overexpression of native pentose-specific transporters together with the rate-limiting D-xylitol and L-arabitol dehydrogenases, the dormant pentose metabolism of Yarrowia lipolytica is activated, overview. Recombinant overexpression of a heterologous L-arabitol dehydrogenase of Aspergillus oryzae (ADHAoz), in Yarrowia lipolytica strain YlSR157 using the constitutive TEF promoter, ADHAoz is chosen because it exhibits higher activity toward L-arabitol (39.2 mU/mg protein) than D-xylitol (6.54 mU/mg protein). Unlike strain YlSR102, strain YlSR157 grows faster and consumes more sugars when growing on both single arabinose and mixed pentose sugars
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Fernandes, S.; Tuohy, M.G.; Murray, P.G.
Cloning, heterologous expression, and characterization of the xylitol and L-arabitol dehydrogenase genes, Texdh and Telad, from the thermophilic fungus Talaromyces emersonii
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Immobilization of L-arabinitol dehydrogenase on aldehyde-functionalized silicon oxide nanoparticles for L-xylulose production
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Disruption of the L-arabitol dehydrogenase encoding gene in Aspergillus tubingensis results in increased xylanase production
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Understanding functional roles of native pentose-specific transporters for activating dormant pentose metabolism in Yarrowia lipolytica
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Sukpipat, W.; Komeda, H.; Prasertsan, P.; Asano, Y.
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