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Information on EC 1.1.1.316 - L-galactose 1-dehydrogenase
for references in articles please use BRENDA:EC1.1.1.316
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.316 L-galactose 1-dehydrogenase
IUBMB Comments
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+.
The enzyme appears in viruses and cellular organisms
- 1.1.1.316
- ascorbate
- l-galactono-1,4-lactone
- asa
- gdp-l-galactose
- dehydroascorbate
-
l-ascorbic
-
pyrophosphorylase
- gdp-d-mannose
- gpp
-
l-galactose-1-phosphate
- monodehydroascorbate
- kiwifruit
- d-galacturonate
showSynonyms
l-galactose dehydrogenase, l-galdh, l-galactose 1-dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
GDH
L-galactose dehydrogenase
L-GalDH
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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)
-
-
-
L-galactose + NAD+ = L-galactono-1,4-lactone + NADH + H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
L-ascorbate biosynthesis I (plants, L-galactose pathway)
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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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-galactose + NADP+
L-galactono-1,4-lactone + NADPH + H+
Substrates: -
Products: -
Products: -
?
L-glucose + NAD+
?
Substrates: 11.9% of the activity with L-galactose
Products: -
Products: -
?
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
Substrates: -
Products: -
Products: -
r
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
Substrates: NAD+ preferred cofactor, lower activity with L-sorbosone, no activity with D-arabinose, D-galactose, D-glucose and D-mannose
Products: -
Products: -
?
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
Substrates: a step in the Smirnoff-Wheeler pathway, ascorbate biosynthesis in higher plants
Products: -
Products: -
ir
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
-
Substrates: a step in the Smirnoff-Wheeler pathway, ascorbate biosynthesis in higher plants
Products: -
Products: -
?
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
Substrates: -
Products: -
Products: -
ir
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
Substrates: -
Products: -
Products: -
?
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
-
Substrates: 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
Products: -
Products: -
ir
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
-
Substrates: a step in the Smirnoff-Wheeler pathway, ascorbate biosynthesis in higher plants
Products: -
Products: -
ir
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
-
Substrates: a step in the Smirnoff-Wheeler pathway, ascorbate biosynthesis in higher plants
Products: -
Products: -
?
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
ir
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
Substrates: -
Products: -
Products: -
?
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
Substrates: 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
Products: -
Products: -
ir
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
Substrates: a step in the Smirnoff-Wheeler pathway, ascorbate biosynthesis in higher plants
Products: -
Products: -
ir
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
Substrates: high specificity for L-galactose. The activity with 1 mM NADP+ is 4.7% of that with 1 mM NAD+
Products: -
Products: -
ir
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
L-gulose + NAD+
?
Substrates: 71.4% of the activity with L-galactose
Products: -
Products: -
?
additional information
?
-
Substrates: no activity is detectable with D-arabinose, D-galactose, D-glucose and D-mannose
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity is detectable with D-arabinose, D-galactose, D-glucose and D-mannose
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with D-galactose, D-glucose, D-mannose, L-fucose and D-arabinose. The enzyme oxidizes L-sorbosone with very low affinity
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with L-fructose, L-mannose, L-xylose, L-arabinose, D-galactose, D-glucose, L-fucose, D-mannose and D-arabinose
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with L-fructose, L-mannose, L-xylose, L-arabinose, D-galactose, D-glucose, L-fucose, D-mannose and D-arabinose
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
Substrates: -
Products: -
Products: -
r
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
Substrates: a step in the Smirnoff-Wheeler pathway, ascorbate biosynthesis in higher plants
Products: -
Products: -
ir
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
-
Substrates: a step in the Smirnoff-Wheeler pathway, ascorbate biosynthesis in higher plants
Products: -
Products: -
?
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
Substrates: -
Products: -
Products: -
?
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
-
Substrates: a step in the Smirnoff-Wheeler pathway, ascorbate biosynthesis in higher plants
Products: -
Products: -
ir
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
-
Substrates: a step in the Smirnoff-Wheeler pathway, ascorbate biosynthesis in higher plants
Products: -
Products: -
?
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
Substrates: a step in the Smirnoff-Wheeler pathway, ascorbate biosynthesis in higher plants
Products: -
Products: -
ir
L-galactose + NAD+
L-galactono-1,4-lactone + NADH + H+
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
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. Inhibition is restored to 71% by incubation with 5 mM GSH; 5 mM: 67% inhibition
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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
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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
2.17
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
comparison of enzyme activity and ascorbate pool size in fruit pulp of orange and Satsuma mandarins, i.e. Citrus sinensis and Citrus unshiu, overview
brenda
comparison of enzyme activity and ascorbate pool size in fruit pulp of orange and Satsuma mandarins, i.e. Citrus sinensis and Citrus unshiu, overview
brenda
-
the enzyme shows an expression pattern similar to the ascorbate levels and changes in fruits during development, overview
brenda
-
the enzyme shows an expression pattern similar to the ascorbate levels and changes in fruits during development, overview
-
brenda
additional information
-
quantitative real-time PCR expression analysis
brenda
additional information
quantitative real-time PCR expression analysis in peel pulp and source leaf
brenda
additional information
-
quantitative real-time PCR expression analysis in peel pulp and source leaf
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
metabolism
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 genes including GMP, GME, GGP, GPP, GalDH, and GalLDH involve in L-galactose pathway. 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. GalDH activity is positively correlated with AsA content. GalLDH activity maintains a relatively steady level for the first 17 days of fruit storage, and then decreases a lowest level at 21 days of storage. The expression of GalDH increases sharply during the first 9 days, and then gradually increases to about 4times higher level compared to the initial level whereas, GalLDH is stably expressed with a slight fluctuation during storage
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). E9M5S4_CITUN
317
0
34414
TrEMBL
Secretory Pathway (Reliability: 1)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36000
40000
42200
87500
87500
gel filtration, two peaks of activity at 42400 Da and 87500 Da
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
homotetramer
homotetramer
-
4 * 40000, gel filtration and SDS-PAGE, N-terminal sequencing
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 0.1 M bis-Tris pH 6.5, 0.2 M MgCl2, 25% (w/v) polyethylene glycol 3350
-
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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
His-tagged version expressed in Escherichia coli BL21(DE3)lysS, expressed in Nicotiana tabacum SRI
quantitative real-time PCR enzyme expression analysis in Actinidia eriantha cv. White
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Oh, M.M.; Carey, E.E.; Rajashekar, C.B.
Environmental stresses induce health-promoting phytochemicals in lettuce
Plant Physiol. Biochem.
47
578-583
2009
Lactuca sativa
brenda
Mieda, T.; Yabuta, Y.; Rapolu, M.; Motoki, T.; Takeda, T.; Yoshimura, K.; Ishikawa, T.; Shigeoka, S.
Feedback inhibition of spinach L-galactose dehydrogenase by L-ascorbate
Plant Cell Physiol.
45
1271-1279
2004
Spinacia oleracea (Q6BDJ2), Spinacia oleracea
brenda
Gatzek, S.; Wheeler, G.L.; Smirnoff, N.
Antisense suppression of L-galactose dehydrogenase in Arabidopsis thaliana provides evidence for its role in ascorbate synthesis and reveals light modulated L-galactose synthesis
Plant J.
30
541-553
2002
Arabidopsis thaliana (O81884), Arabidopsis thaliana, Lathyrus oleraceus
brenda
Li, M.; Ma, F.; Guo, C.; Liu, J.
Ascorbic acid formation and profiling of genes expressed in its synthesis and recycling in apple leaves of different ages
Plant Physiol. Biochem.
48
216-224
2010
Malus domestica (Q84L20), Malus domestica
brenda
Wheeler, G.L.; Jones, M.A.; Smirnoff, N.
The biosynthetic pathway of vitamin C in higher plants
Nature
393
365-369
1998
Arabidopsis thaliana, Lathyrus oleraceus
brenda
Li, M.; Chen, X.; Wang, P.; Ma, F.
Ascorbic acid accumulation and expression of genes involved in its biosynthesis and recycling in developing apple fruit
J. Am. Soc. Hort. Sci.
136
231-238
2011
Malus domestica, Malus domestica Gala
-
brenda
Yang, X.Y.; Xie, J.X.; Wang, F.F.; Zhong, J.; Liu, Y.Z.; Li, G.H.; Peng, S.A.
Comparison of ascorbate metabolism in fruits of two citrus species with obvious difference in ascorbate content in pulp
J. Plant Physiol.
168
2196-2205
2011
Citrus sinensis, Citrus unshiu (E9M5S4), Citrus unshiu
brenda
Mellado, M.; Contreras, R.A.; Gonzalez, A.; Dennett, G.; Moenne, A.
Copper-induced synthesis of ascorbate, glutathione and phytochelatins in the marine alga Ulva compressa (Chlorophyta)
Plant Physiol. Biochem.
51
102-108
2012
Ulva compressa
brenda
Momma, M.; Fujimoto, Z.
Expression, crystallization and preliminary X-ray analysis of rice L-galactose dehydrogenase
Acta Crystallogr. Sect. F
69
809-811
2013
Oryza sativa
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 (C0LVA5)
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.316)
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