Information on EC 1.1.1.316 - L-galactose 1-dehydrogenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.316
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RECOMMENDED NAME
GeneOntology No.
L-galactose 1-dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-galactose + NAD+ = L-galactono-1,4-lactone + NADH + H+
show the reaction diagram
; a key enzyme in the biosynthetic pathway of L-ascorbate in plants (Smirnoff-Wheeler pathway)
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-ascorbate biosynthesis I (L-galactose pathway)
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ascorbate metabolism
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Ascorbate and aldarate metabolism
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Metabolic pathways
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Biosynthesis of secondary metabolites
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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+.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cvs. Newhall Dream, navel oranges
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Manually annotated by BRENDA team
cvs.Egan No.2 and Guoqing No.1, Satsuma mandarins
UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
specific activity depends on leaf age
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-fucose + NAD+
?
show the reaction diagram
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?
L-fucose + NAD+
? + NADH + H+
show the reaction diagram
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?
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
show the reaction diagram
L-galactose + NADP+
L-galactono-1,4-lactone + NADPH + H+
show the reaction diagram
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?
L-glucose + NAD+
?
show the reaction diagram
11.9% of the activity with L-galactose
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?
L-gulose + NAD+
?
show the reaction diagram
L-gulose + NAD+
? + NADH + H+
show the reaction diagram
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?
L-sorbosone + NAD+
?
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-chloromercuribenzoate
0.2 mM: 92% inhibition
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
L-galactono-1,4-lactone
uncompetitive; uncompetitive
lycorine
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N-ethylmaleimide
oxidized glutathione
5 mM, 65% inhibition; 65% inhibition with 5 mM
p-chloromercuribenzoate
0.2 mM, 92% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
1 mM, 17% stimulation
DTT
1 mM: 17% stimulation
glutathione
1 mM, 28% stimulation; 1 mM: 28% stimulation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
56.3
L-fucose
pH 7.5, temperature not specified in the publication
0.085 - 0.43
L-galactose
1.5 - 3.7
L-gulose
0.0179 - 0.0203
NAD+
0.59
NADP+
pH 7.5, temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.133 - 0.1332
L-ascorbate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.25
purified protein from spinach, pH 7.5, 37C
2.17
pH 7.5, 37C; purified recombinant protein, pH 7.5, 37C
16.4
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control alga, pH 7.5, 37C
25.5
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copper treated alga, pH 7.5, 37C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
75000
gel filtration
87500
gel filtration; gel filtration, two peaks of activity at 42400 Da and 87500 Da
156000
gel filtration; gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
homotetramer
4 * 40000, gel filtration and SDS-PAGE, N-terminal sequencing; 4 * 40000, SDS-PAGE
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
partial
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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
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is rapidly activated by chilling stress, heat shock and high light
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the enzyme expression increases until day 7, with maximal level at day 5-7, of copper treatment of the alga
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