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Information on EC 3.1.3.B9 - L-galactose 1-phosphate phosphatase
for references in articles please use BRENDA:EC3.1.3.B9
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preliminary BRENDA-supplied EC number
EC Tree 3 Hydrolases
3.1 Acting on ester bonds
3.1.3 Phosphoric-monoester hydrolases
3.1.3.B9 L-galactose 1-phosphate phosphatase
The enzyme appears in viruses and cellular organisms
- 3.1.3.B9
- asa
-
l-ascorbic
- l-galactono-1,4-lactone
- gdp-l-galactose
- phosphorylase
-
pyrophosphorylase
- myo-inositol
- gmp
- gdp-d-mannose
-
actinidia
- d-galacturonate
- kiwifruit
-
monophosphatase
-
pathway-related
-
ripening
- deliciosa
- monodehydroascorbate
-
guanylyltransferase
- peach
- galur
-
reductase1
- galldh
- dehydroascorbate
-
bloom
- ozone
- myo-inositol-1-phosphate
-
protoplasts
- l-gulono-1,4-lactone
showSynonyms
l-galactose-1-phosphate phosphatase, ntgppase, at3g02870, l-galactose-1-p phosphatase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
GPP
L-Gal-1-Pase
L-galactose-1-phosphate phosphatase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-galactose 1-phosphate + H2O = L-galactose + phosphate
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
L-galactose 1-phosphate phosphohydrolase
-
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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 1-phosphate + H2O
L-galactose + phosphate
Substrates: -
Products: -
Products: -
?
L-galactose 1-phosphate + H2O
L-galactose + phosphate
Substrates: the enzyme is very specific for L-galactose 1-phosphate
Products: -
Products: -
?
L-galactose 1-phosphate + H2O
L-galactose + phosphate
Substrates: -
Products: -
Products: -
?
L-galactose 1-phosphate + H2O
L-galactose + phosphate
Substrates: the enzyme is very specific for L-galactose 1-phosphate
Products: -
Products: -
?
L-galactose 1-phosphate + H2O
L-galactose + phosphate
Substrates: the enzyme is involved in biosynthesis of asorbate
Products: -
Products: -
?
L-galactose 1-phosphate + H2O
L-galactose + phosphate
Substrates: the enzyme plays a role in plant ascorbate biosynthesis. The presence of ascorbate in the T-DNA insertion mutant suggests there is a bypass to this enzyme or that other pathways also contribute to ascorbate biosynthesis
Products: -
Products: -
?
L-galactose 1-phosphate + H2O
L-galactose + phosphate
Substrates: -
Products: -
Products: -
?
L-galactose 1-phosphate + H2O
L-galactose + phosphate
Substrates: the enzyme is very specific for L-galactose 1-phosphate
Products: -
Products: -
?
L-galactose 1-phosphate + H2O
L-galactose + phosphate
Substrates: -
Products: -
Products: -
?
L-galactose 1-phosphate + H2O
L-galactose + phosphate
Substrates: the bifunctional enzyme VTC4 also acts on myo-inositol phosphate (cf. EC 3.1.3.25)
Products: -
Products: -
?
L-galactose 1-phosphate + H2O
L-galactose + phosphate
-
Substrates: the enzyme is involved in biosynthesis of asorbate
Products: -
Products: -
?
L-galactose 1-phosphate + H2O
L-galactose + phosphate
-
Substrates: the enzyme is very specific for L-galactose 1-phosphate
Products: -
Products: -
?
L-galactose 1-phosphate + H2O
L-galactose + phosphate
Substrates: -
Products: -
Products: -
?
L-galactose 1-phosphate + H2O
L-galactose + phosphate
-
Substrates: -
Products: -
Products: -
?
L-galactose 1-phosphate + H2O
L-galactose + phosphate
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: the protein shows some myo-inositol-1-Pase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: the protein shows some myo-inositol-1-Pase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: the protein shows some myo-inositol-1-Pase activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme also dephosphorylates myo-inositol 1-phosphate
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 1-phosphate + H2O
L-galactose + phosphate
Substrates: -
Products: -
Products: -
?
L-galactose 1-phosphate + H2O
L-galactose + phosphate
Substrates: -
Products: -
Products: -
?
L-galactose 1-phosphate + H2O
L-galactose + phosphate
Substrates: the enzyme is involved in biosynthesis of asorbate
Products: -
Products: -
?
L-galactose 1-phosphate + H2O
L-galactose + phosphate
Substrates: the enzyme plays a role in plant ascorbate biosynthesis. The presence of ascorbate in the T-DNA insertion mutant suggests there is a bypass to this enzyme or that other pathways also contribute to ascorbate biosynthesis
Products: -
Products: -
?
L-galactose 1-phosphate + H2O
L-galactose + phosphate
Substrates: -
Products: -
Products: -
?
L-galactose 1-phosphate + H2O
L-galactose + phosphate
-
Substrates: the enzyme is involved in biosynthesis of asorbate
Products: -
Products: -
?
L-galactose 1-phosphate + H2O
L-galactose + phosphate
Substrates: -
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
the enzyme is completely dependent on Mg2+ for activity. Ka(Mg2+): 0.2 mM
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.107
L-galactose 1-phosphate
pH and 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
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.2 - 7.5
pH 6.2: about 20% of maximal activity, pH 7.5: about 35% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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pI VALUE
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
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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
malfunction
physiological function
malfunction
L-Gal-1-phosphate phosphatase activity in low ascorbate mutant vtc4-1 is 50% of wild-type plants. In addition, vtc4-1 plants incorporate significantly more radiolabel from [2-3H]Man into L-galactosyl residues suggesting that the mutation increases the availability of GDP-L-Gal for polysaccharide synthesis
malfunction
knockout lines of VTC4 exhibit small perturbations in abscisic acid, salt, and cold responses. Analysis of metabolite levels in vtc4 mutants show that less myo-inositol and ascorbate accumulate in these mutants
malfunction
-
tobacco BY-2 cells over-expressing NtGPPase have a higher content of L-ascorbic acid 13 days after subculture compared to control cells
physiological function
VTC4 is a bifunctional enzyme that impacts both myo-inositol and ascorbate synthesis pathways
physiological function
L-galactose-1-phosphate phosphatase could play an important role in regulating ascorbic acid biosynthesis via the L-galactose pathway
physiological function
-
L-galactose-1-phosphate phosphatase could play an important role in regulating ascorbic acid accumulation during tomato fruit development and ripening
physiological function
-
GPP plays an important role in ascorbic acid accumulation under varying light conditions or when plants are exposed to abscisic acid, salicylic acid, wounding, or hypoxic conditions
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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). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned into a plasmid construct containing the T7 viral promoter, an N-terminal polyhistidine peptide, an Xpress epitope, and an EK cleavage site (pAtIMPH). Overexpression of soluble VTC4 protein in Escherichia coli strain pREP4/BL21(DE3)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
accumulation of GPP mRNA experienced an important increment at latter stages of fruit maturation
expression of L-galactose-1-phosphate phosphatase shows good correlation with the rate of ascorbic acid synthesis
expression of L-galactose-1-phosphate phosphatase shows good correlation with the rate of ascorbic acid synthesis. The relative expression of L-galactose-1-phosphate phosphatase peaks in 15 days after anthesis fruits, and then clearly declined to a steady level after 60 days after anthesis. From day 30 to 45, expression decreases by about 65%. This is similar to the pattern of change observed for the rate of ascorbic acid accumulation during fruit development. L-Galactose-1-phosphate phosphatase expression is highest at 30 days after anthesis, then decreases greatly at 45 days after anthesis before remaining largely unchanged through fruit maturation
ozone treatment increasea the expression of L-galactose-1-phosphate phosphatase gene
-
accumulation of GPP mRNA experienced an important increment at latter stages of fruit maturation
-
accumulation of GPP mRNA experienced an important increment at latter stages of fruit maturation
-
expression of L-galactose-1-phosphate phosphatase shows good correlation with the rate of ascorbic acid synthesis
-
expression of L-galactose-1-phosphate phosphatase shows good correlation with the rate of ascorbic acid synthesis
-
-
expression of L-galactose-1-phosphate phosphatase shows good correlation with the rate of ascorbic acid synthesis. The relative expression of L-galactose-1-phosphate phosphatase peaks in 15 days after anthesis fruits, and then clearly declined to a steady level after 60 days after anthesis. From day 30 to 45, expression decreases by about 65%. This is similar to the pattern of change observed for the rate of ascorbic acid accumulation during fruit development. L-Galactose-1-phosphate phosphatase expression is highest at 30 days after anthesis, then decreases greatly at 45 days after anthesis before remaining largely unchanged through fruit maturation
-
expression of L-galactose-1-phosphate phosphatase shows good correlation with the rate of ascorbic acid synthesis. The relative expression of L-galactose-1-phosphate phosphatase peaks in 15 days after anthesis fruits, and then clearly declined to a steady level after 60 days after anthesis. From day 30 to 45, expression decreases by about 65%. This is similar to the pattern of change observed for the rate of ascorbic acid accumulation during fruit development. L-Galactose-1-phosphate phosphatase expression is highest at 30 days after anthesis, then decreases greatly at 45 days after anthesis before remaining largely unchanged through fruit maturation
-
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 (Q5U788), Malus domestica
brenda
Conklin, P.L.; Gatzek, S.; Wheeler, G.L.; Dowdle, J.; Raymond, M.J.; Rolinski, S.; Isupov, M.; Littlechild, J.A.; Smirnoff, N.
Arabidopsis thaliana VTC4 encodes L-galactose-1-P phosphatase, a plant ascorbic acid biosynthetic enzyme
J. Biol. Chem.
281
15662-15670
2006
Arabidopsis thaliana (Q9M8S8), Arabidopsis thaliana
brenda
Ioannidi, E.; Kalamaki, M.S.; Engineer, C.; Pateraki, I.; Alexandrou, D.; Mellidou, I.; Giovannonni, J.; Kanellis, A.K.
Expression profiling of ascorbic acid-related genes during tomato fruit development and ripening and in response to stress conditions
J. Exp. Bot.
60
663-678
2009
Solanum lycopersicum
brenda
Cruz-Rus, E.; Amaya, I.; Sanchez-Sevilla, J.F.; Botella, M.A.; Valpuesta, V.
Regulation of L-ascorbic acid content in strawberry fruits
J. Exp. Bot.
62
4191-4201
2011
Fragaria x ananassa
brenda
Torabinejad, J.; Donahue, J.L.; Gunesekera, B.N.; Allen-Daniels, M.J.; Gillaspy, G.E.
VTC4 is a bifunctional enzyme that affects myoinositol and ascorbate biosynthesis in plants
Plant Physiol.
150
951-961
2009
Arabidopsis thaliana (Q9M8S8)
brenda
Li, M.; Ma, F.; Liang, D.; Li, J.; Wang, Y.
Ascorbate biosynthesis during early fruit development is the main reason for its accumulation in kiwi
PLoS One
5
e14281
2010
Actinidia deliciosa, Actinidia deliciosa cv. Qinmei
brenda
Laing, W.A.; Bulley, S.; Wright, M.; Cooney, J.; Jensen, D.; Barraclough, D.; MacRae, E.
A highly specific L-galactose-1-phosphate phosphatase on the path to ascorbate biosynthesis
Proc. Natl. Acad. Sci. USA
101
16976-16981
2004
Actinidia deliciosa (Q5U789), Actinidia deliciosa, Actinidia deliciosa A. Chev. (Q5U789), Arabidopsis thaliana (Q9M8S8), Arabidopsis thaliana
brenda
Sakamoto, S.; Fujikawa, Y.; Tanaka, N.; Esaka, M.
Molecular cloning and characterization of L-galactose-1-phosphate phosphatase from tobacco (Nicotiana tabacum)
Biosci. Biotechnol. Biochem.
76
1155-1162
2012
Nicotiana tabacum
brenda
Li, J.; Li, M.; Liang, D.; Cui, M.; Ma, F.
Expression patterns and promoter characteristics of the gene encoding Actinidia deliciosa L-galactose-1-phosphate phosphatase involved in the response to light and abiotic stresses
Mol. Biol. Rep.
40
1473-1485
2013
Actinidia deliciosa
brenda
Alos, E.; Rodrigo, M.J.; Zacarias, L.
Differential transcriptional regulation of L-ascorbic acid content in peel and pulp of citrus fruits during development and maturation
Planta
239
1113-1128
2014
Citrus sinensis, Citrus unshiu
brenda
EXTERNAL LINKS (specific for EC-Number 3.1.3.B9)
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