1.1.1.365: D-galacturonate reductase
This is an abbreviated version!
For detailed information about D-galacturonate reductase, go to the full flat file.
Word Map on EC 1.1.1.365
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1.1.1.365
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l-ascorbic
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pectin
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ascorbate
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asa
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galurs
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dehydratase
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niger
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hypocrea
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ripening
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strawberry
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jecorina
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ripe
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l-galactono-1,4-lactone
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l-galactose
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trichoderma
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solanum
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reesei
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l-gulono-1,4-lactone
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pectin-rich
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gdp-d-mannose
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d-glucuronic
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dehydroascorbate
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synthesis
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nutrition
- 1.1.1.365
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l-ascorbic
- pectin
- ascorbate
- asa
- galurs
- dehydratase
- niger
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hypocrea
-
ripening
- strawberry
- jecorina
-
ripe
- l-galactono-1,4-lactone
- l-galactose
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trichoderma
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solanum
- reesei
- l-gulono-1,4-lactone
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pectin-rich
- gdp-d-mannose
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d-glucuronic
- dehydroascorbate
- synthesis
- nutrition
Reaction
Synonyms
AKR2, AnGaaA, AnGar1, Cd-GAR, D-galacturonate reductase, D-galacturonic acid reductase, D-galacturonic acid reductases, FaGalUR, gaaA, GalA reductase, galacturonate reductase, GalUR, gar1, GAR2, NADPH-dependent D-galacturonate reductase, PcGOR
ECTree
1.1.1.365 D-galacturonate reductaseAdvanced search results
results (
results (Engineering
Engineering on EC 1.1.1.365 - D-galacturonate reductase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
K261M
K261M/R267L
R267L
K261M
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the mutation confers AnGar1 the ability to accept NADH in addition to NADPH. Mutation partly abolishes the AnGar1 activity with NADPH as the cofactor
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K261M/R267L
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mutation confers NADH specificity to the enzyme. Mutation almost fully abolishes the AnGar1 activity with NADPH as the cofactor
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R267L
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the mutation confers AnGar1 the ability to accept NADH in addition to NADPH. Mutation partly abolishes the AnGar1 activity with NADPH as the cofactor
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additional information
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
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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
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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
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