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Information on EC 1.1.1.316 - L-galactose 1-dehydrogenase
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1.1.1.316 L-galactose 1-dehydrogenaseIUBMB 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+.
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Word Map
- 1.1.1.316
- ascorbate
- l-galactono-1,4-lactone
- asa
- gdp-l-galactose
- dehydroascorbate
-
l-galactose-1-phosphate
-
l-ascorbic
-
pyrophosphorylase
- gpp
- monodehydroascorbate
- gdp-d-mannose
- d-galacturonate
-
ammonia-lyase
- kiwifruit
-
benth
- compressa
- gamma-tocopherol
- d-arabinose
- galldh
- gamma-tmt
-
actinidia
-
lactuca
-
copper-induced
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
l-galactose dehydrogenase, l-galdh, l-galactose 1-dehydrogenase, 
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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+
-
-
-
-
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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PATHWAY SOURCE
PATHWAYS
BRENDA
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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
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
-
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
-
ir
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+
high specificity for L-galactose. The activity with 1 mM NADP+ is 4.7% of that with 1 mM NAD+
-
ir
additional information
?
-
no activity is detectable with D-arabinose, D-galactose, D-glucose and D-mannose
-
?
additional information
?
-
-
no activity is detectable with D-arabinose, D-galactose, D-glucose and D-mannose
-
?
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
-
?
additional information
?
-
no activity with L-fructose, L-mannose, L-xylose, L-arabinose, D-galactose, D-glucose, L-fucose, D-mannose and D-arabinose
-
?
additional information
?
-
-
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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NATURAL SUBSTRATE
NATURAL 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+
-
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+
-
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+
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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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; 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
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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
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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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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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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). GALDH_ARATH
319
0
34532
Swiss-Prot
other Location (Reliability: 4)
A0A5B7C4C5_DAVIN
321
0
35725
TrEMBL
other Location (Reliability: 4)
A0A5B7A4E8_DAVIN
319
0
34535
TrEMBL
other Location (Reliability: 3)
A0A1Y0Y9K6_ACEPA
178
0
19318
TrEMBL
-
A0A5B7A2G6_DAVIN
348
0
37751
TrEMBL
other Location (Reliability: 5)
A0A5B7B7L8_DAVIN
270
0
30245
TrEMBL
Mitochondrion (Reliability: 4)
A0A5B7AVW9_DAVIN
195
0
21360
TrEMBL
Mitochondrion (Reliability: 5)
A0A5B6ZZ63_DAVIN
224
0
24559
TrEMBL
other Location (Reliability: 3)
A0A2P6PJG1_ROSCH
108
0
12092
TrEMBL
other Location (Reliability: 1)
A0A2P6PJG2_ROSCH
368
0
40060
TrEMBL
other Location (Reliability: 4)
A0A5B7B871_DAVIN
251
0
28208
TrEMBL
Mitochondrion (Reliability: 4)
A0A2G9GGV5_9LAMI
322
0
34889
TrEMBL
other Location (Reliability: 4)
A0A5B7BUD5_DAVIN
345
0
38171
TrEMBL
Mitochondrion (Reliability: 5)
A0A5B7BYR3_DAVIN
196
0
21865
TrEMBL
Mitochondrion (Reliability: 5)
A0A5B7BPS4_DAVIN
321
0
35680
TrEMBL
other Location (Reliability: 2)
A0A0E4CYF5_9BACL
319
0
35285
TrEMBL
-
G7JTZ5_MEDTR
316
0
34289
TrEMBL
other Location (Reliability: 5)
A0A5B7B6W4_DAVIN
388
0
42966
TrEMBL
Chloroplast (Reliability: 4)
A0A5B6Z7G6_DAVIN
348
0
38732
TrEMBL
other Location (Reliability: 4)
A0A1R3SZ67_9BACT
300
0
33756
TrEMBL
-
A0A5B7CE76_DAVIN
226
2
25532
TrEMBL
other Location (Reliability: 5)
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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
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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 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
Pisum sativum, Arabidopsis thaliana (O81884), Arabidopsis thaliana
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, Pisum sativum
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
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