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Enzyme Nomenclature
Information on EC 1.1.1.316 - L-galactose 1-dehydrogenase
Word Map on EC 1.1.1.316
- 1.1.1.316
- ascorbate
- l-galactono-1,4-lactone
- apple
-
l-ascorbic
- gdp-l-galactose
-
l-galactose-1-phosphate
- malus
- domestica
- lettuce
- gpp
-
re-exposed
- dehydroascorbate
- monodehydroascorbate
- gamma-tocopherol
-
lactuca
- gamma-tmt
- gdp-d-mannose
-
borkh
- d-arabinose
-
peel
-
ammonia-lyase
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.1.1.316
-
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RECOMMENDED NAME
GeneOntology No.
L-galactose 1-dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-galactose + NAD+ = L-galactono-1,4-lactone + NADH + H+
; a key enzyme in the biosynthetic pathway of L-ascorbate in plants (Smirnoff-Wheeler pathway)
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
L-galactose:NAD+ 1-oxidoreductase
The enzyme catalyses a step in the ascorbate biosynthesis in higher plants (Smirnoff-Wheeler pathway). The activity with NADP+ is less than 10% of the activity with NAD+.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
key enzyme in the biosynthetic pathway of L-ascorbate in plants
metabolism
the enzyme is involved in the ascorbate bioosynthesis in fruits
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
NAD+ preferred cofactor, lower activity with L-sorbosone, no activity with D-arabinose, D-galactose, D-glucose and D-mannose
-
-
?
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
-
a step in the Smirnoff-Wheeler pathway, ascorbate biosynthesis in higher plants
-
-
?
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
a step in the Smirnoff-Wheeler pathway, ascorbate biosynthesis in higher plants
-
-
ir
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
-
activity with 0.1 mM NADP+ is 6% of that with NAD+, lower activity with L-sorbosone, no activity with D-arabinose and L-fucose
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-
ir
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
-
a step in the Smirnoff-Wheeler pathway, ascorbate biosynthesis in higher plants
-
-
?
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
-
a step in the Smirnoff-Wheeler pathway, ascorbate biosynthesis in higher plants
-
-
ir
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
activity with 1 mM NADP+ was 4.7% of that with 1 mM NAD+, no activity with L-fructose, L-mannose, L-Xylose, L-arabinose, D-galactose, D-glucose, L-fucose, D-mannose and D-arabinose
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-
ir
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
a step in the Smirnoff-Wheeler pathway, ascorbate biosynthesis in higher plants
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-
ir
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
high specificity for L-galactose. The activity with 1 mM NADP+ is 4.7% of that with 1 mM NAD+
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-
ir
additional information
?
-
-
no activity is detectable with D-arabinose, D-galactose, D-glucose and D-mannose
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-
-
additional information
?
-
no activity is detectable with D-arabinose, D-galactose, D-glucose and D-mannose
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-
-
additional information
?
-
-
no activity with D-galactose, D-glucose, D-mannose, L-fucose and D-arabinose. The enzyme oxidizes L-sorbosone with very low affinity
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-
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additional information
?
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no activity with L-fructose, L-mannose, L-xylose, L-arabinose, D-galactose, D-glucose, L-fucose, D-mannose and D-arabinose
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-
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additional information
?
-
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no activity with L-fructose, L-mannose, L-xylose, L-arabinose, D-galactose, D-glucose, L-fucose, D-mannose and D-arabinose
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-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
-
a step in the Smirnoff-Wheeler pathway, ascorbate biosynthesis in higher plants
-
-
?
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
O81884
a step in the Smirnoff-Wheeler pathway, ascorbate biosynthesis in higher plants
-
-
ir
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
-
a step in the Smirnoff-Wheeler pathway, ascorbate biosynthesis in higher plants
-
-
?
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
-
a step in the Smirnoff-Wheeler pathway, ascorbate biosynthesis in higher plants
-
-
ir
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
Q6BDJ2
a step in the Smirnoff-Wheeler pathway, ascorbate biosynthesis in higher plants
-
-
ir
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
L-ascorbate
1 mM, 41% inhibition, linear-competitive inhibition, inhibition is reversible, equilibrium-type of feedback regulation for L-ascorbate synthesis; reversible inhibition by the end-product of the biosynthetic pathway
N-ethylmaleimide
5 mM: 67% inhibition; 5 mM, 67% inhibition. Inhibition is restored to 71% by incubation with 5 mM GSH
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
56.3
L-fucose
pH 7.5, temperature not specified in the publication
0.085
L-galactose
pH 7.5, temperature not specified in the publication
0.43
L-galactose
-
pH 7.5, 22°C; pH 7.5, temperature not specified in the publication
3.7
L-gulose
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pH 7.5, 22°C; pH 7.5, temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
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comparison of enzyme activity and ascorbate pool size in fruit pulp of orange and Satsuma mandarins, i.e. Citrus sinensis and Citrus unshiu, overview
comparison of enzyme activity and ascorbate pool size in fruit pulp of orange and Satsuma mandarins, i.e. Citrus sinensis and Citrus unshiu, overview
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the enzyme shows an expression pattern similar to the ascorbate levels and changes in fruits during development, overview
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the enzyme shows an expression pattern similar to the ascorbate levels and changes in fruits during development, overview
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additional information
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quantitative real-time PCR expression analysis in peel pulp and source leaf
additional information
quantitative real-time PCR expression analysis in peel pulp and source leaf
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36000
2 * 36000, SDS-PAGE; 2 * 36000, SDS-PAGE, gel filtration, 35261 Da calculated
40000
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4 * 40000, gel filtration and SDS-PAGE, N-terminal sequencing; 4 * 40000, SDS-PAGE
42200
2 * 42200, SDS-PAGE; 2 * 42200, SDS-PAGE and gel filtration
87500
gel filtration; gel filtration, two peaks of activity at 42400 Da and 87500 Da
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
homotetramer
-
4 * 40000, gel filtration and SDS-PAGE, N-terminal sequencing; 4 * 40000, SDS-PAGE
homodimer
2 * 42200, SDS-PAGE; 2 * 42200, SDS-PAGE and gel filtration
homodimer
2 * 35261, calculated from sequence; 2 * 36000, SDS-PAGE; 2 * 36000, SDS-PAGE, gel filtration, 35261 Da calculated
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; ammonium sulfate precipitation, anion exchange chromatography, hydrophobic interaction chromatography and gel filtration, recombinant fusion protein by GST-affinity chromatography
; ammonium sulfate precipitation, hydrophobic interaction chromatography, anion exchange chromatography, Blue Sepharose affinity chromatography and gel filtration
-
; immobilized metal ion affinity chromatography (Ni2+) and gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli; fusion construct with glutathione S-transferase expressed in Escherichia coli BL21(DE3)pLysS
expression in Escherichia coli; His-tagged version expressed in Escherichia coli BL21(DE3)lysS, expressed in Nicotiana tabacum SRI
quantitative real-time PCR expression analysis
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is rapidly activated by chilling stress, heat shock and high light
-
the enzyme expression increases until day 7, with maximal level at day 5-7, of copper treatment of the alga
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.316)
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