1.1.1.203: uronate dehydrogenase
This is an abbreviated version!
For detailed information about uronate dehydrogenase, go to the full flat file.
Word Map on EC 1.1.1.203
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1.1.1.203
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d-galacturonic
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agrobacterium
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tumefaciens
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syringae
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myo-inositol
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glucaric
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value-added
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galactaric
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pectin
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oxygenase
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d-glucuronic
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l-ascorbic
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asa
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myo-inositol-1-phosphate
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aldaric
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strawberry
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degradation
- 1.1.1.203
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d-galacturonic
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agrobacterium
- tumefaciens
- syringae
- myo-inositol
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glucaric
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value-added
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galactaric
- pectin
- oxygenase
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d-glucuronic
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l-ascorbic
- asa
- myo-inositol-1-phosphate
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aldaric
- strawberry
- degradation
Reaction
Synonyms
Atu3143, CsUDH, D-galacturonate (uronate) dehydrogenase, D-GalUA oxidoreductase, EC 1.2.1.35, galacturonate acid reductase, galacturonate oxidoreductase, GalUR, Gor, PfUDH, PmUDH, PnUDH, poly-d-galacturonase, PSPTO_1053, PsUDH, Udh, uronate dehydrogenase, uronate:NAD-oxidoreductase, uronic acid dehydrogenase
ECTree
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General Information
General Information on EC 1.1.1.203 - uronate dehydrogenase
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evolution
metabolism
physiological function
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ascorbate accumulation is affected mainly by biosynthesis rather than recycling in radish root, and the L-galactose pathway may be the major biosynthetic route of ascorbate, and moreover, the salvage pathway may also contribute to ascorbate accumulation. Ascorbate level regulation involves the D-galacturonate reductase and GDP-D-mannose diphosphorylase
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the enzyme belongs to the short-chain dehydrogenase/reductase (SDR) superfamily
evolution
the enzyme belongs to the short-chain dehydrogenase/reductase (SDR) superfamily
evolution
the enzyme belongs to the short-chain dehydrogenase/reductase (SDR) superfamily
evolution
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the enzyme belongs to the short-chain dehydrogenase/reductase (SDR) superfamily
evolution
-
the enzyme belongs to the short-chain dehydrogenase/reductase (SDR) superfamily
evolution
-
UDH is a member of the short-chain dehydrogenase/reductase(SDR) superfamily, whose members typically contain a single domain having a highly variable C-terminal substrate binding site, reflecting the diverse nature of SDR substrates and attendant substrate binding site structures, and a conserved N-terminal cofactor binding site
evolution
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UDH is a member of the short-chain dehydrogenase/reductase(SDR) superfamily, whose members typically contain a single domain having a highly variable C-terminal substrate binding site, reflecting the diverse nature of SDR substrates and attendant substrate binding site structures, and a conserved N-terminal cofactor binding site
evolution
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UDH is a member of the short-chain dehydrogenase/reductase(SDR) superfamily, whose members typically contain a single domain having a highly variable C-terminal substrate binding site, reflecting the diverse nature of SDR substrates and attendant substrate binding site structures, and a conserved N-terminal cofactor binding site
evolution
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UDH is a member of the short-chain dehydrogenase/reductase(SDR) superfamily, whose members typically contain a single domain having a highly variable C-terminal substrate binding site, reflecting the diverse nature of SDR substrates and attendant substrate binding site structures, and a conserved N-terminal cofactor binding site
evolution
UDH is a member of the short-chain dehydrogenase/reductase(SDR) superfamily, whose members typically contain a single domain having a highly variable C-terminal substrate binding site, reflecting the diverse nature of SDR substrates and attendant substrate binding site structures, and a conserved N-terminal cofactor binding site
evolution
-
the enzyme belongs to the short-chain dehydrogenase/reductase (SDR) superfamily
-
evolution
-
the enzyme belongs to the short-chain dehydrogenase/reductase (SDR) superfamily
-
evolution
-
the enzyme belongs to the short-chain dehydrogenase/reductase (SDR) superfamily
-
evolution
-
UDH is a member of the short-chain dehydrogenase/reductase(SDR) superfamily, whose members typically contain a single domain having a highly variable C-terminal substrate binding site, reflecting the diverse nature of SDR substrates and attendant substrate binding site structures, and a conserved N-terminal cofactor binding site
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evolution
Agrobacterium tumefaciens C58 / ATCC 33970
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the enzyme belongs to the short-chain dehydrogenase/reductase (SDR) superfamily
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evolution
Pseudomonas syringae pv. tomato ATCC BAA-871 / DC3000
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UDH is a member of the short-chain dehydrogenase/reductase(SDR) superfamily, whose members typically contain a single domain having a highly variable C-terminal substrate binding site, reflecting the diverse nature of SDR substrates and attendant substrate binding site structures, and a conserved N-terminal cofactor binding site
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uronate dehydrogenases catalyse the initial step in an oxidative pathway
metabolism
uronate dehydrogenases catalyse the initial step in an oxidative pathway
metabolism
uronate dehydrogenases catalyse the initial step in an oxidative pathway
metabolism
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uronate dehydrogenases catalyse the initial step in an oxidative pathway
metabolism
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uronate dehydrogenases catalyses the initial step in an oxidative pathway
metabolism
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the enzyme is proposed to be part of the salvage pathway in ascorbate production as galacturonate acid reductase, GalUR, EC 1.1.1.203, converting D-galacturonate to L-galactono-1,4-lactone, ascorbate biosynthesis and recycling pathways in plants, overview
metabolism
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uronate dehydrogenases catalyse the initial step in an oxidative pathway
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metabolism
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uronate dehydrogenases catalyse the initial step in an oxidative pathway
-
metabolism
-
uronate dehydrogenases catalyse the initial step in an oxidative pathway
-
metabolism
Agrobacterium tumefaciens C58 / ATCC 33970
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uronate dehydrogenases catalyse the initial step in an oxidative pathway
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