Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D-galactose + NADPH + H+
?
D-galacturonate + NADH + H+
L-galactonate + NAD+
D-galacturonate + NADPH + H+
L-galactonate + NADP+
D-glucuronate + NADH + H+
?
D-glucuronate + NADPH + H+
?
D-glucuronic acid + NADPH + H+
?
D-glucurono-3,6-lactone + NADPH + H+
L-gulono-1,4-lactone
-
-
-
-
r
D-xylose + NADPH + H+
?
-
29.9% activity compared to D-glucuronate
-
-
?
DL-glyceraldehyde + NADPH + H+
?
L-arabinose + NADPH + H+
?
-
14.2% activity compared to D-glucuronate
-
-
ir
L-galactonate + NAD+
D-galacturonate + NADH + H+
L-galactonate + NADP+
D-galacturonate + NADPH + H+
L-galactose + NADPH + H+
?
-
18.8% activity compared to D-glucuronate
-
-
ir
L-gluconate + NADP+
D-glucuronate + NADPH + H+
-
-
-
-
r
additional information
?
-
D-galactose + NADPH + H+
?
-
14.9% activity compared to D-glucuronate
-
-
ir
D-galactose + NADPH + H+
?
-
14.9% activity compared to D-glucuronate
-
-
ir
D-galacturonate + NADH + H+
L-galactonate + NAD+
-
-
-
-
r
D-galacturonate + NADH + H+
L-galactonate + NAD+
-
-
-
-
r
D-galacturonate + NADH + H+
L-galactonate + NAD+
-
17.7% activity compared to NADPH
-
-
ir
D-galacturonate + NADPH + H+
L-galactonate + NADP+
-
-
-
-
?
D-galacturonate + NADPH + H+
L-galactonate + NADP+
-
-
-
-
r
D-galacturonate + NADPH + H+
L-galactonate + NADP+
-
-
-
r
D-galacturonate + NADPH + H+
L-galactonate + NADP+
-
-
-
?
D-galacturonate + NADPH + H+
L-galactonate + NADP+
-
-
-
-
?
D-galacturonate + NADPH + H+
L-galactonate + NADP+
-
-
-
-
?, r
D-galacturonate + NADPH + H+
L-galactonate + NADP+
-
-
-
r
D-galacturonate + NADPH + H+
L-galactonate + NADP+
-
-
-
?
D-galacturonate + NADPH + H+
L-galactonate + NADP+
-
-
-
-
r
D-galacturonate + NADPH + H+
L-galactonate + NADP+
-
-
-
-
r
D-galacturonate + NADPH + H+
L-galactonate + NADP+
-
-
-
-
ir
D-galacturonate + NADPH + H+
L-galactonate + NADP+
-
100% activity
-
-
ir
D-galacturonate + NADPH + H+
L-galactonate + NADP+
-
-
-
-
ir
D-galacturonate + NADPH + H+
L-galactonate + NADP+
-
-
-
-
?
D-galacturonate + NADPH + H+
L-galactonate + NADP+
-
-
-
r
D-galacturonate + NADPH + H+
L-galactonate + NADP+
HV538330
-
-
-
r
D-galacturonate + NADPH + H+
L-galactonate + NADP+
HV538330
-
-
-
r
D-galacturonate + NADPH + H+
L-galactonate + NADP+
-
-
-
r
D-galacturonate + NADPH + H+
L-galactonate + NADP+
-
-
-
-
?
D-galacturonate + NADPH + H+
L-galactonate + NADP+
-
-
-
-
r
D-galacturonate + NADPH + H+
L-galactonate + NADP+
-
-
-
-
?
D-galacturonate + NADPH + H+
L-galactonate + NADP+
-
-
-
-
r
D-glucose + NADPH + H+
?
-
14.6% activity compared to D-glucuronate
-
-
ir
D-glucose + NADPH + H+
?
-
14.6% activity compared to D-glucuronate
-
-
ir
D-glucuronate + NADH + H+
?
-
-
-
-
?
D-glucuronate + NADH + H+
?
-
-
-
-
?
D-glucuronate + NADPH + H+
?
-
-
-
-
?
D-glucuronate + NADPH + H+
?
-
-
-
-
?
D-glucuronate + NADPH + H+
?
-
-
-
-
r
D-glucuronate + NADPH + H+
?
-
-
-
-
r
D-glucuronate + NADPH + H+
?
-
82.4% activity compared to D-glucuronate
-
-
?
D-glucuronate + NADPH + H+
?
-
82.4% activity compared to D-glucuronate
-
-
?
D-glucuronate + NADPH + H+
?
-
-
-
-
?
D-glucuronic acid + NADPH + H+
?
-
-
-
-
?
D-glucuronic acid + NADPH + H+
?
-
-
-
-
?
DL-glyceraldehyde + NADPH + H+
?
-
14.2% activity compared to D-glucuronate
-
-
ir
DL-glyceraldehyde + NADPH + H+
?
-
-
-
-
?
DL-glyceraldehyde + NADPH + H+
?
-
-
-
-
?
L-galactonate + NAD+
D-galacturonate + NADH + H+
-
-
-
-
r
L-galactonate + NAD+
D-galacturonate + NADH + H+
-
-
-
r
L-galactonate + NADP+
D-galacturonate + NADPH + H+
-
-
-
-
r
L-galactonate + NADP+
D-galacturonate + NADPH + H+
-
-
-
r
L-galactonate + NADP+
D-galacturonate + NADPH + H+
-
-
-
-
r
L-galactonate + NADP+
D-galacturonate + NADPH + H+
-
-
-
-
r
L-galactonate + NADP+
D-galacturonate + NADPH + H+
-
-
-
-
r
additional information
?
-
-
the enzyme does not catalyze the reverse reaction with L-galactonate and NADP+ and does not utilize 4-nitrobenzaldehyde or menadione
-
-
?
additional information
?
-
-
the enzyme does not catalyze the reverse reaction with L-galactonate and NADP+ and does not utilize 4-nitrobenzaldehyde or menadione
-
-
?
additional information
?
-
HV538330
optimization of conversion of D-galacturonic acid to L-galactonic acid by recombinant enzyme in Saccharomyces cerevisiae, overview
-
-
?
additional information
?
-
-
optimization of conversion of D-galacturonic acid to L-galactonic acid by recombinant enzyme in Saccharomyces cerevisiae, overview
-
-
?
additional information
?
-
HV538330
optimization of conversion of D-galacturonic acid to L-galactonic acid by recombinant enzyme in Saccharomyces cerevisiae, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes the reduction of the C-1 carbon of D-glucuronate and C-4 epimer D-galacturonate to their corresponding aldonic acids. It is active on both glucuronic acid and galacturonic acid, with similar substrate specificities using the preferred cosubstrate NADPH. Substrate acceptance extends to lactone congeners, and D-glucurono-3,6-lactone is converted to L-gulono-1,4-lactone
-
-
-
additional information
?
-
-
no activity with NADH and D-glucose, D-fructose, D-xylose, D-galactose, L-arabinose, or D-mannose. No backward reaction with L-gulonic acid, glycerol, D-arabitol, L-arabitol, xylitol, galactitol, or ribitol
-
-
?
additional information
?
-
-
no activity with NADH and D-glucose, D-fructose, D-xylose, D-galactose, L-arabinose, or D-mannose. No backward reaction with L-gulonic acid, glycerol, D-arabitol, L-arabitol, xylitol, galactitol, or ribitol
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.175 - 7.11
D-galacturonate
0.12 - 4.67
D-glucuronate
11
D-glucuronic acid
-
in 100 mM sodium phosphate (pH 7.0), at 22°C
8.48
D-xylose
-
in 50 mM Tris-HCl (pH 7.2), at 25°C
6
DL-glyceraldehyde
-
in 100 mM sodium phosphate (pH 7.0), at 22°C
4
L-galactonate
-
in 100 mM sodium phosphate (pH 7.0), at 22°C
0.326
NADH
-
with D-galacturonate as cosubstrate, in 10 mM sodium phosphate, at pH 7.2 and 22°C
0.001
NADP+
-
in 100 mM sodium phosphate (pH 7.0), at 22°C
0.175
D-galacturonate
-
with NADPH as cosubstrate, in 10 mM sodium phosphate, at pH 7.2 and 22°C
1.4
D-galacturonate
-
isoform GAR2, 10 mM sodium phosphate, pH 7.0, at 22°C
2.5
D-galacturonate
-
isoform GAR1, 10 mM sodium phosphate, pH 7.0, at 22°C
3.79
D-galacturonate
-
in 50 mM Tris-HCl (pH 7.2), at 25°C
6
D-galacturonate
-
in 100 mM sodium phosphate (pH 7.0), at 22°C
7.11
D-galacturonate
-
with NADH as cosubstrate, in 10 mM sodium phosphate, at pH 7.2 and 22°C
0.12
D-glucuronate
-
isoform GAR1, 10 mM sodium phosphate, pH 7.0, at 22°C
1
D-glucuronate
-
isoform GAR2, 10 mM sodium phosphate, pH 7.0, at 22°C
4.67
D-glucuronate
-
in 50 mM Tris-HCl (pH 7.2), at 25°C
0.03
NADPH
-
in 100 mM sodium phosphate (pH 7.0), at 22°C
0.036
NADPH
-
with D-galacturonate as cosubstrate, in 10 mM sodium phosphate, at pH 7.2 and 22°C
0.0625
NADPH
-
in 50 mM Tris-HCl (pH 7.2), at 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
HV538330
the enzyme belongs to the NAD(P)+-binding Rossmann fold oxidoreductase family of proteins
evolution
AnGaaA is identified as the bona fide GalA reductase in Aspergillus niger. AnGaaA is not related to Gar1 proteins
evolution
-
the enzyme belongs to the NAD(P)+-binding Rossmann fold oxidoreductase family of proteins
-
malfunction
-
deletion of the NADPH-dependent D-galacturonate reductase gene results in strains unable to grow on D-galacturonate
malfunction
-
deletion of the NADPH-dependent D-galacturonate reductase gene results in strains unable to grow on D-galacturonate
malfunction
-
deletion of the NADPH-dependent D-galacturonate reductase gene results in strains unable to grow on D-galacturonate
-
malfunction
-
deletion of the NADPH-dependent D-galacturonate reductase gene results in strains unable to grow on D-galacturonate
-
metabolism
-
D-galacturonic acid reductase is a key enzyme of the ascorbate biosynthesis pathway
metabolism
after import via the D-galacturonic acid transporter encoded by An14g04280, D-galacturonic acid is catabolized by three key enzymes: D-galacturonic acid reductase, L-galactonate dehydratase, and 2-keto-3-deoxy-galactonate aldolase, in Aspegillus niger. The first step in the D-galacturonic acid metabolism is the enzymatic conversion of D-galacturonic acid to L-galactonic acid by D-galacturonic acid reductase. Overexpression of the Aspergillus niger GatA transporter leads to preferential uptake of D-galacturonic acid over D-xylose of mutant strain JS013 and enanced use of D-galacturonic acid compared to D-xylose. Increased activity of the D-galacturonic acid metabolic pathway is observed for strain JS013 transformant strain in comparison to the control
metabolism
D-galacturonate reductase (GalUR) is important in the ascorbic acid biosynthetic pathway
metabolism
enzyme D-galacturonic acid reductase, GalUR, is involved in the D-galacturonic acid pathway for ascorbic acid biosynthesis
metabolism
-
D-galacturonate reductase (GalUR) is a key enzyme involved in D-galacturonate pathway of AsA biosynthesis. L-Ascorbic acid (AsA) biosynthesis through the L-galactose pathway supplemented by D-galacturonic acid pathway and AsA recycling collectively contributes to accumulating and remaining higher AsA level in kiwifruit cv. White during postharvest. L-Galactose dehydrogenase (GalDH) activity and relative expressions of the genes encoding GDP-D-mannose diphosphorylase (GMP), L-galactose-1-P phosphatase (GPP), GDP-L-galactose phosphorylase (GGP), GalDH and GalUR are important for regulation of AsA biosynthesis. The activity and expression of dehydroascorbate reductase (DHAR) are primarily responsible for regulation of AsA recycling in kiwifruit cv. White during postharvest. Changes in activities of enzymes involved in AsA metabolism in the fruit during storage, quantitative real-time PCR expression analysis. A minor change is observed in GalUR activity. The relative expression of GalUR increases sharply to a peak at day 13, and then decreases gradually and continuously
metabolism
-
after import via the D-galacturonic acid transporter encoded by An14g04280, D-galacturonic acid is catabolized by three key enzymes: D-galacturonic acid reductase, L-galactonate dehydratase, and 2-keto-3-deoxy-galactonate aldolase, in Aspegillus niger. The first step in the D-galacturonic acid metabolism is the enzymatic conversion of D-galacturonic acid to L-galactonic acid by D-galacturonic acid reductase. Overexpression of the Aspergillus niger GatA transporter leads to preferential uptake of D-galacturonic acid over D-xylose of mutant strain JS013 and enanced use of D-galacturonic acid compared to D-xylose. Increased activity of the D-galacturonic acid metabolic pathway is observed for strain JS013 transformant strain in comparison to the control
-
metabolism
-
D-galacturonic acid reductase is a key enzyme of the ascorbate biosynthesis pathway
-
physiological function
-
enzyme expression correlates with changing ascorbic acid content in strawberry fruit during ripening. Overexpression of the enzyme in Arabidopsis thaliana enhances vitamin C content 2-3fold
physiological function
-
overexpression of strawberry D-galacturonic acid reductase in potato leads to accumulation of vitamin C with enhanced abiotic stress tolerance induced by methyl viologen, NaCl or mannitol
physiological function
all of transgenic Solanum lycopersicum lines overexpressing the Fragaria ananassa D-galacturonic acid reductase gene are morphologically indistinguishable over different generations from control lines both in vegetative traits, such as leaf size or plant height, and fruit traits such as color or size. The majority of transgenic plants display a slight increase in fruit yield, up to 1.4fold, which is a consequence of an increase in the number of fruits rather than an increase in fruit weight. The plants show no significant changes in soluble solids of transgenic plants, but a reduction in acidity. Transgenic lines show a moderate increase on AsA content, and complex changes in metabolites are found in transgenic fruits. Phenotypes, overview
physiological function
D-galacturonate reductase (GalUR) plays a prominent role in the regulation of the ascorbate biosynthetic pathway. The overexpression of gene GalUR gene enhances the level of ascorbate and Fe(II) of transgenic tomato plants which show better growth than wild-type plants under iron stresses. Ascorbate is a cofactor for many enzymes and affects the expression of genes involved in defense signaling pathways. It plays an important role as an antioxidant and protects the plant during oxidative damage by scavenging free radicals and reactive oxygen species that are generated during photosynthesis, oxidative metabolism and various abiotic stresses including excess light, soil water stress, UV-B radiation, and ozone
physiological function
L-ascorbic acid and L-ascorbic acid pool size accumulation in the leaves of Rosa roxburghii are regulated by both biosynthesis and recycling, and enzyme D-galacturonic acid reductase, GalUR, in the D-galacturonic acid pathway and monodehydroascorbate reductase, MDHAR, in the recycling pathway play important roles in this process
physiological function
the D-galacturonic acid reductase catalyzes the conversion of D-galacturonic acid to L-galactonic acid in plant. The D-galacturonic acid, known as an abundant component of the cell wall, is a degradation product of pectin in senescencing plant cells. The expression levels of FaGalUR are correlated with increased ascorbate content in ripe strawberry fruit. Fragaria x ananassa gene FaGalUR expression improves salt and cold tolerance in Solanum lycopersicum fruits, and improves tolerance to oxidative stress in tomato
physiological function
-
Penicillium camemberti reduces the C-1 carbon of D-glucuronate and C-4 epimer D-galacturonate to their corresponding aldonic acids, important reactions in both pectin catabolism and ascorbate biosynthesis. Enzyme PcGOR is active on both glucuronic acid and galacturonic acid, with similar substrate specificities (kcat/Km) using the preferred cosubstrate NADPH. Substrate acceptance extends to lactone congeners, and D-glucurono-3,6-lactone is converted to L-gulono-1,4-lactone, an immediate precursor of ascorbate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
K261M
-
the mutation confers AnGar1 the ability to accept NADH in addition to NADPH. Mutation partly abolishes the AnGar1 activity with NADPH as the cofactor
-
K261M/R267L
-
mutation confers NADH specificity to the enzyme. Mutation almost fully abolishes the AnGar1 activity with NADPH as the cofactor
-
R267L
-
the mutation confers AnGar1 the ability to accept NADH in addition to NADPH. Mutation partly abolishes the AnGar1 activity with NADPH as the cofactor
-
K261M
site-directed mutagenesis, the recombinant yeast strain expressing the enzyme mutant shows increased activity with NADH in L-galacturonate reduction compared to wild-type
K261M
the mutation confers AnGar1 the ability to accept NADH in addition to NADPH. Mutation partly abolishes the AnGar1 activity with NADPH as the cofactor
K261M/R267L
mutation confers NADH specificity to the enzyme. Mutation almost fully abolishes the AnGar1 activity with NADPH as the cofactor
K261M/R267L
site-directed mutagenesis, the recombinant yeast strain expressing the enzyme mutant shows increased activity with NADH in L-galacturonate reduction compared to wild-type
R267L
site-directed mutagenesis, the recombinant yeast strain expressing the enzyme mutant shows increased activity with NADH in L-galacturonate reduction compared to wild-type
R267L
the mutation confers AnGar1 the ability to accept NADH in addition to NADPH. Mutation partly abolishes the AnGar1 activity with NADPH as the cofactor
additional information
-
establishment of the production of L-galactonate (GalOA) or the full GalA catabolic pathway in Saccharomyces cerevisiae using the enzyme mutant K261M/R267L with increased NADH activity, and coupling the reduction of GalA to the oxidation of the sugar alcohol sorbitol that has a higher reduction state compared to glucose for yielding the necessary redox cofactors. By choosing a suitable sorbitol dehydrogenase, yeast strains are designed in which the sorbitol metabolism yields a surplus of either NADPH or NADH
additional information
establishment of the production of L-galactonate (GalOA) or the full GalA catabolic pathway in Saccharomyces cerevisiae using the enzyme mutant K261M/R267L with increased NADH activity, and coupling the reduction of GalA to the oxidation of the sugar alcohol sorbitol that has a higher reduction state compared to glucose for yielding the necessary redox cofactors. By choosing a suitable sorbitol dehydrogenase, yeast strains are designed in which the sorbitol metabolism yields a surplus of either NADPH or NADH
additional information
establishment of the production of L-galactonate (GalOA) or the full GalA catabolic pathway in Saccharomyces cerevisiae using the enzyme mutant K261M/R267L with increased NADH activity, and coupling the reduction of GalA to the oxidation of the sugar alcohol sorbitol that has a higher reduction state compared to glucose for yielding the necessary redox cofactors. By choosing a suitable sorbitol dehydrogenase, yeast strains are designed in which the sorbitol metabolism yields a surplus of either NADPH or NADH
additional information
gene FaGalUR-overexpressing Solanum lycopersicum plants show enhanced ascorbic acid levels, tolerance to abiotic stresses induced by oxidization (methyl viologen), salt (NaCl), and cold compared to the wild-type plants, overview. Ascorbate accumulation in tomato can be enhanced by regulating Fragaria x ananassa GalUR gene
additional information
stable overexpressing the Fragaria GalUR gene results in 2.6fold increase of ascorbate in fruits and 1.6fold increase of ascorbate in leaves compared to non-transformed wild-type tomato, the levels of ascorbate are positively correlated with increased GalUR activity. The transgenic plants show enhanced tolerance to iron deficiency compared to wild-type plants. Under Fe(II) deficiency condition the plant height of transgenic plants is 1.2-1.7times higher, the ascorbate content is 1.8-2.8times higher, and the Fe2+ content is 1.1-1.4times higher compared to wild-type
additional information
transgenic tomatoes with increased ascorbic acid contents due to overexpression of the enzyme are found to be more tolerant to abiotic stresses induced by viologen, NaCl, or mannitol than non-transformed plants. In leaf disc senescence assay, the tolerance of these transgenic plants is better than control plants because they retain higher chlorophyll contents. Under salt stress of less than 200 mM NaCl. These transgenic plants survive, while control plants are unable to survive such high salt stress. Ascorbic acid contents in the transgenic plants are inversely correlated with malondialdehyde contents, especially under salt stress conditions. Higher expression levels of antioxidant genes (APX and CAT) are also found in these transgenic plants compared to that in the control plants. No detectable difference in SOD expression is found between transgenic plants and control plants. Phenotype, detailed overview
additional information
HV538330
development of an ethanol fermentation system from D-galacturonic acid (or pectic waste) in enzyme lacking Saccharomyces cerevisiae, brewing yeast. Optimization of conversion of D-galacturonic acid to L-galactonic acid by recombinant enzyme in Saccharomyces cerevisiae, overview. High efficiency in the conversion of D-galacturonic acid to L-galactonic acid in large-scale cultures is achieved with 0.1% initial D-galacturonic acid concentration, pH 3.5, and glucose as additional sugar, aerobic condition is necessary. Subculture of this recombinant is not showing to decrease of the D-galacturonic acid conversion rate even though it is repeated in ten generations. Culturing in scale-up, the conversion rate of D-galacturonic acid to L-galactonic acid is increased. The recombinant strain, similar to its wild-type host strain IFO 10455, cannot grow in media containing D-galacturonic acid as the sole carbon source, but it can grow after the addition of Saccharomyces cerevisiae fermentative sugars like glucose and galactose
additional information
-
development of an ethanol fermentation system from D-galacturonic acid (or pectic waste) in enzyme lacking Saccharomyces cerevisiae, brewing yeast. Optimization of conversion of D-galacturonic acid to L-galactonic acid by recombinant enzyme in Saccharomyces cerevisiae, overview. High efficiency in the conversion of D-galacturonic acid to L-galactonic acid in large-scale cultures is achieved with 0.1% initial D-galacturonic acid concentration, pH 3.5, and glucose as additional sugar, aerobic condition is necessary. Subculture of this recombinant is not showing to decrease of the D-galacturonic acid conversion rate even though it is repeated in ten generations. Culturing in scale-up, the conversion rate of D-galacturonic acid to L-galactonic acid is increased. The recombinant strain, similar to its wild-type host strain IFO 10455, cannot grow in media containing D-galacturonic acid as the sole carbon source, but it can grow after the addition of Saccharomyces cerevisiae fermentative sugars like glucose and galactose
additional information
-
development of an ethanol fermentation system from D-galacturonic acid (or pectic waste) in enzyme lacking Saccharomyces cerevisiae, brewing yeast. Optimization of conversion of D-galacturonic acid to L-galactonic acid by recombinant enzyme in Saccharomyces cerevisiae, overview. High efficiency in the conversion of D-galacturonic acid to L-galactonic acid in large-scale cultures is achieved with 0.1% initial D-galacturonic acid concentration, pH 3.5, and glucose as additional sugar, aerobic condition is necessary. Subculture of this recombinant is not showing to decrease of the D-galacturonic acid conversion rate even though it is repeated in ten generations. Culturing in scale-up, the conversion rate of D-galacturonic acid to L-galactonic acid is increased. The recombinant strain, similar to its wild-type host strain IFO 10455, cannot grow in media containing D-galacturonic acid as the sole carbon source, but it can grow after the addition of Saccharomyces cerevisiae fermentative sugars like glucose and galactose
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
expressed in Arabidopsis thaliana and in Escherichia coli XL1-Blue MRF' cells
-
expressed in Escherichia coli BL21 cells
-
expressed in Escherichia coli DH5alpha cells
-
expressed in Saccharomyces cerevisiae strain CEN.PK2-1B
-
expressed in Solanum tuberosum cultivar Taedong Valley
-
expressed in Solanum tuberosum via Agrobacterium tumefaciens-mediated transformation
-
expression in Saccharomyces cerevisie
gene gaaA, expression analysis in wild-type strain and in a strain overexpressing the D-galacturonic acid-specific GatA transporter
gene gaaA, recombinant expression of wild-type enzyme in Saccharomyces cerevisiae strain SiHY001
gene GalUR, real-time quantitative PCR enzyme expression analysis
gene GalUR, recombinant overexpression in Solanum lycopersicum cv. Ailsa Craig leaves and fruits via Agrobacterium tumefaciens strain C58C1 transfection resulting in 2fold and 1.6fold increase in ascorbate level in tomato fruit and leaf, respectively, which correlates positively with FaGalUR transcriptional abundance and enzyme GalUR activity compared to wild-type plants, real-time PCR expression analysis
gene GalUR, recombinant stable overexpression in Solanum lycopersicum cv. H15 leaves and fruits using Agrobacterium tumefaciens strain EHA 105 transfection method, the pNW2300 vector, and the CaMV35S promoter. The transgenic plants show increased enzyme content and activity compared to wild-type. Semi-quantitative RT-PCR expression analysis, increased ascorbic acid content is correlated with high level of transcript expression, that is 2-3fold increased compared to wild-type
gene GalUR, recombinant stable overexpression in Solanum lycopersicum cv. Zhongshu 4 leaves and fruits via Agrobacterium tumefaciens strain C58C1 transfection method using the pCB302-3 vector and CaMV 35S promoter, reverse transcriptase-PCR expression analysis. The transgenic plants show 2.2-2.5fold increased enzyme activity compared to wild-type
gene GAR1, DNA and amino acid sequence determination and analysis, functional recombinant expression in Saccharomyces cerevisiae strain IFO 10455 from a genome integrated copy, integration of the pGK406GAR1 plasmid into the ura3 allele of the IFO 10455 genome, subcloning in Escherichia coli strain DH5alpha
HV538330
gene gar1, recombinant expression of wild-type and mutant enzymes in Saccharomyces cerevisiae strain SiHY001, real-time PCR expression analysis
ORF FaGalUR is recombinantly expressed in Solanum lycopersicum from plasmid pPGGUSI, which contains a 4.8 Kb promoter fragment of the polygalacturonase (PG) gene and its terminator, or from a plasmid containing the 35S CaMV promoter, mobilized from Escherichia coli by triparental mating, via Agrobacterium tumefaciens strain LBA4404 in tomato plants, PCR expression analysis. FaGalUR expression driven by the CaMV 35S promoter causes the expression of the gene in most parts of the plants, while in the second, FaGalU, is expressed under the control of the tomato fruit ripening-specific PG promoter. All of the transgenic lines are morphologically indistinguishable over different generations from control lines both in vegetative traits, such as leaf size or plant height, and fruit traits such as color or size. The majority of transgenic plants display a slight increase in fruit yield, up to 1.4fold, which is a consequence of an increase in the number of fruits rather than an increase in fruit weight. No significant changes in soluble solids of transgenic plants, but a reduction in acidity
quantitative real-time PCR enzyme expression analysis in Actinidia eriantha cv. White
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Zhang, L.; Thiewes, H.; van Kan, J.A.
The D-galacturonic acid catabolic pathway in Botrytis cinerea
Fungal Genet. Biol.
48
990-997
2011
Botrytis cinerea, Botrytis cinerea B05.10
brenda
Kuivanen, J.; Mojzita, D.; Wang, Y.; Hilditch, S.; Penttil, M.; Richard, P.; Wiebe, M.G.
Engineering filamentous fungi for conversion of D-galacturonic acid to L-galactonic acid
Appl. Environ. Microbiol.
78
8676-8683
2012
Aspergillus niger, Trichoderma reesei, Aspergillus niger ATCC 1015
brenda
Martens-Uzunova, E.S.; Schaap, P.J.
An evolutionary conserved D-galacturonic acid metabolic pathway operates across filamentous fungi capable of pectin degradation
Fungal Genet. Biol.
45
1449-1457
2008
Aspergillus niger, Aspergillus niger CBS 120.49
brenda
Mojzita, D.; Wiebe, M.; Hilditch, S.; Boer, H.; Penttilae, M.; Richard, P.
Metabolic engineering of fungal strains for conversion of D-galacturonate to meso-galactarate
Appl. Environ. Microbiol.
76
169-175
2010
Aspergillus niger, Trichoderma reesei, Aspergillus niger ATCC 1015, Trichoderma reesei QM6a
brenda
Kuorelahti, S.; Kalkkinen, N.; Penttil, M.; Londesborough, J.; Richard, P.
Identification in the mold Hypocrea jecorina of the first fungal D-galacturonic acid reductase
Biochemistry
44
11234-11240
2005
Trichoderma reesei, Trichoderma reesei RUT C-30
brenda
Ishikawa, T.; Masumoto, I.; Iwasa, N.; Nishikawa, H.; Sawa, Y.; Shibata, H.; Nakamura, A.; Yabuta, Y.; Shigeoka, S.
Functional characterization of D-galacturonic acid reductase, a key enzyme of the ascorbate biosynthesis pathway, from Euglena gracilis
Biosci. Biotechnol. Biochem.
70
2720-2726
2006
Euglena gracilis, Euglena gracilis Z
brenda
Venkatesh, J.; Upadhyaya, C.; Yu, J.; Hemavathi, A.; Kim, D.; Strasser, R.; Park, S.
Chlorophyll a fluorescence transient analysis of transgenic potato overexpressing D-galacturonic acid reductase gene for salinity stress tolerance
Hortic. Environ. Biotechnol.
53
320-328
2012
Fragaria x ananassa
-
brenda
Hemavath, H.; Upadhyaya, C.; Akula, N.; Kim, H.; Jeon, J.; Ho, O.; Chun, S.; Kim, D.; Park, S.
Biochemical analysis of enhanced tolerance in transgenic potato plants overexpressing D-galacturonic acid reductase gene in response to various abiotic stresses
Mol. Breed.
28
105-115
2011
Fragaria x ananassa
-
brenda
Agius, F.; Gonzalez-Lamothe, R.; Caballero, J.L.; Munoz-Blanco, J.; Botella, M.A.; Valpuesta, V.
Engineering increased vitamin C levels in plants by overexpression of a D-galacturonic acid reductase
Nat. Biotechnol.
21
177-181
2003
Fragaria x ananassa
brenda
Hemavath, H.; Upadhyaya, C.; Young, K.; Akula, N.; Kim, H.; Heung, J.; Oh, O.; Aswath, C.; Chun, S.; Kim, D.; Park, S.
Over-expression of strawberry D-galacturonic acid reductase in potato leads to accumulation of vitamin C with enhanced abiotic stress tolerance
Plant Sci.
177
659-667
2009
Fragaria x ananassa
brenda
Li, L.; Lu, M.; An, H.
Expression profiles of the genes involved in L-ascorbic acid biosynthesis and recycling in Rosa roxburghii leaves of various ages
Acta Physiol. Plant.
39
44
2017
Rosa roxburghii (E2G4I9)
-
brenda
Yang, J.; Liu, Y.; Huang, J.; Li, J.; Shi, Y.; Liu, Y.
Accumulation of vitamin C and enhanced tolerance to iron deficiency stress in transgenic tomato with GalUR gene
Adv. Mater. Res.
749
277-282
2013
Fragaria x ananassa (O49133)
-
brenda
Sloothaak, J.; Schilders, M.; Schaap, P.J.; de Graaff, L.H.
Overexpression of the Aspergillus niger GatA transporter leads to preferential use of D-galacturonic acid over D-xylose
AMB Express
4
66
2014
Aspergillus niger (A8DRH9), Aspergillus niger, Aspergillus niger CBS 120.49 (A8DRH9)
brenda
Amaya, I.; Osorio, S.; Martinez-Ferri, E.; Lima-Silva, V.; Doblas, V.G.; Fernandez-Munoz, R.; Fernie, A.R.; Botella, M.A.; Valpuesta, V.
Increased antioxidant capacity in tomato by ectopic expression of the strawberry D-galacturonate reductase gene
Biotechnol. J.
10
490-500
2015
Fragaria x ananassa (O49133), Fragaria x ananassa
brenda
Matsubara, T.; Hamada, S.; Wakabayashi, A.; Kishida, M.
Fermentative production of L-galactonate by using recombinant Saccharomyces cerevisiae containing the endogenous galacturonate reductase gene from Cryptococcus diffluens
J. Biosci. Bioeng.
122
639-644
2016
Naganishia diffluens (HV538330), Naganishia diffluens, Naganishia diffluens OPU-FC11 (HV538330)
brenda
Lim, M.; Jeong, B.; Jung, M.; Harn, C.
Transgenic tomato plants expressing strawberry D-galacturonic acid reductase gene display enhanced tolerance to abiotic stresses
Plant Biotechnol. Rep.
10
105-116
2016
Fragaria x ananassa (O49133)
-
brenda
Cai, X.; Zhang, C.; Ye, J.; Hu, T.; Ye, Z.; Li, H.; Zhang, Y.
Ectopic expression of FaGalUR leads to ascorbate accumulation with enhanced oxidative stress, cold, and salt tolerance in tomato
Plant Growth Regul.
76
187-197
2015
Fragaria x ananassa (O49133)
-
brenda
Wagschal, K.; Jordan, D.B.; Hart-Cooper, W.M.; Chan, V.J.
Penicillium camemberti galacturonate reductase C-1 oxidation/reduction of uronic acids and substrate inhibition mitigation by aldonic acids
Int. J. Biol. Macromol.
153
1090-1098
2020
Penicillium camemberti
brenda
Jiang, Z.Y.; Zhong, Y.; Zheng, J.; Ali, M.; Liu, G.D.; Zheng, X.L.
L-ascorbic acid metabolism in an ascorbate-rich kiwifruit (Actinidia eriantha Benth.) cv. White during postharvest
Plant Physiol. Biochem.
124
20-28
2018
Actinidia eriantha
brenda
Harth, S.; Wagner, J.; Sens, T.; Choe, J.Y.; Benz, J.P.; Weuster-Botz, D.; Oreb, M.
Engineering cofactor supply and NADH-dependent D-galacturonic acid reductases for redox-balanced production of L-galactonate in Saccharomyces cerevisiae
Sci. Rep.
10
19021
2020
Aspergillus niger, Aspergillus niger (A2R7U3), Aspergillus niger (A8DRH9), Aspergillus niger CBS 513.88 (A2R7U3)
brenda