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Information on EC 3.1.3.93 - L-galactose 1-phosphate phosphatase for references in articles please use BRENDA:EC3.1.3.93
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EC Tree
IUBMB Comments The enzyme from plants also has the activity of EC 3.1.3.25, inositol-phosphate phosphatase. The enzymes have very low activity with D-galactose 1-phosphate (cf. EC 3.1.3.94, D-galactose 1-phosphate phosphatase).
The enzyme appears in viruses and cellular organisms
Synonyms
impl2, l-gal-1-p phosphatase,
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At3g02870
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IMPL2
gene name, ambiguous
IMPL2
gene name, ambiguous
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L-Gal-1-P phosphatase
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L-Gal-1-P phosphatase
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L-Gal-1-P phosphatase
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L-Gal-1-Pase
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VTC4
gene name, ambiguous
VTC4
gene name, ambiguous
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VTC4
gene name, ambiguous
VTC4
gene name, ambiguous
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beta-L-galactose 1-phosphate + H2O = L-galactose + phosphate
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-
-
-
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beta-L-galactose-1-phosphate phosphohydrolase
The enzyme from plants also has the activity of EC 3.1.3.25, inositol-phosphate phosphatase. The enzymes have very low activity with D-galactose 1-phosphate (cf. EC 3.1.3.94, D-galactose 1-phosphate phosphatase).
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alpha-D-glucose 1-phosphate + H2O
alpha-D-glucose + phosphate
19% of the activity with myo-inositol
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-
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beta-L-galactose 1-phosphate + H2O
L-galactose + phosphate
D-galactose 1-phosphate + H2O
D-galactose + phosphate
16.6% of the activity with myo-inositol
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-
?
D-inositol 3-phosphate + H2O
D-inositol + phosphate
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
52% of the activity with myo-inositol
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-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
additional information
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Fru 1-phosphate, Fru 1,6-bisphosphate, Glc 6-phosphate, D-alpha-glycerophosphate, sorbitol 6-phosphate, and myo-inositol 2-V show little to no hydrolysis in assays
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-
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beta-L-galactose 1-phosphate + H2O
L-galactose + phosphate
highly specific for beta-L-galactose 1-phosphate
-
-
?
beta-L-galactose 1-phosphate + H2O
L-galactose + phosphate
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highly specific for beta-L-galactose 1-phosphate
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-
?
beta-L-galactose 1-phosphate + H2O
L-galactose + phosphate
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highly specific for beta-L-galactose 1-phosphate
-
-
?
beta-L-galactose 1-phosphate + H2O
L-galactose + phosphate
166-240% of the activity with myo-inositol
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-
?
beta-L-galactose 1-phosphate + H2O
L-galactose + phosphate
highly specific for beta-L-galactose 1-phosphate
-
-
?
beta-L-galactose 1-phosphate + H2O
L-galactose + phosphate
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
9% of the activity with beta-L-galactose
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-
?
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Mg2+
completely dependent on Mg2+ for activity, Ka-value: 0.2 mM
Mg2+
about 3fold activation, optimum concentration 3-4 mM
Mg2+
-
absolutely dependent on Mg2+. K1 value: 0.016 mM
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D-inositol 3-phosphate
substrate inhibition above 0.7 mM
EDTA
no activity is found in the presence of 0.2 mM EDTA without added Mg2+, native enzyme
LiCl
inhibition of recombinant enzyme
Mg2+
above 2 mM, native enzyme
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0.01 - 0.15
beta-L-galactose 1-phosphate
0.191
D-inositol 3-phosphate
pH 7.5, 22°C
0.01
beta-L-galactose 1-phosphate
pH 7.0, 30°C, 1.8 mM Mg2+, native enzyme
0.022
beta-L-galactose 1-phosphate
pH 7.0, 30°C, 4.8 mM Mg2+
0.044
beta-L-galactose 1-phosphate
-
pH 7.0, 30°C, 2 mM Mg2+
0.107
beta-L-galactose 1-phosphate
pH 7.5, 22°C
0.15
beta-L-galactose 1-phosphate
pH 7.0, 30°C, recombinant enzyme
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3.7
LiCl
pH 7.0, 30°C, inhibition of recombinant enzyme
0.6
Mg2+
pH 7.0, 30°C, inhibition of native enzyme
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6.8 - 7
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at 2 mM MgCl2 and 0.5 mM L-galactose 1-phosphate
7.5
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6.5 - 7.8
pH 6.5: about 70% of maximal activity, pH 7.8: about 0% of maximal activity
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5.01
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calculated from sequence
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UniProt
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UniProt
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UniProt
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UniProt
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bifunctional L-galactose 1-phosphate phosphatase/myo-inositol monophosphatase
UniProt
brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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physiological function
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a homozygous T-DNA insertion line, which lacks a functional At3g02870 gene product, is ascorbate-deficient and deficient in L-Gal-1-phosphate phosphatase activity. The significantly lower ascorbate and perturbed L-Gal metabolism in the mutant indicate that L-Gal-1-phosphate phosphatase plays a role in plant ascorbate biosynthesis
physiological function
knockout lines of isoform VTC4 exhibit small perturbations in abscisic acid, salt, and cold responses. Less myo-inositol and ascorbate accumulate in these mutants
physiological function
the ascorbic acid contents of enzyme overexpression lines are higher than those of controls
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VTC4_ARATH
271
0
29121
Swiss-Prot
HIS7_ARATH
346
0
38235
Swiss-Prot
A0A1C7FEH2_9VIBR
288
0
32959
TrEMBL
A0A1Y0XU51_ACEPA
265
0
28769
TrEMBL
A0A1Y0UTE0_9PROT
265
0
28808
TrEMBL
A0A1A0DEG7_ACEPA
265
0
28795
TrEMBL
A0A1Y0XEU2_BACAM
294
0
34126
TrEMBL
B3GK03_TOBAC
270
0
29166
TrEMBL
Q5U789_ACTDE
270
0
29226
TrEMBL
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29121
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x * 29121, calculated from sequence
29226
2 * 29226, calculated from sequence
33100
x * 39700, SDS-PAGE, x * 33100, calculated
39700
x * 39700, SDS-PAGE, x * 33100, calculated
58000
x * 58000, SDS-PAGE, fusion proein with glutathione S-transferase
65000
gel filtration, native enzyme
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?
x * 39700, SDS-PAGE, x * 33100, calculated
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x * 29121, calculated from sequence
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x * 29121, calculated from sequence
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?
x * 58000, SDS-PAGE, fusion proein with glutathione S-transferase
dimer
2 * 29226, calculated from sequence
dimer
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2 * 29226, calculated from sequence
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P92L
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mutant shows decreased ascorbate synthesis. The mutation is predicted to disrupt the positioning of catalytic amino acid residues within the active site. Accordingly, L-Gal-1-phoshate phosphatase activity in the mutant is about 50% of wild-type plants. In addition, mutant plants incorporate significantly more radiolabelfrom [2-3H]Man into L-galactosyl residues suggesting that the mutation increases the availability of GDP-L-Gal for polysaccharide synthesis
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expression in Escherichia coli
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mRNA and protein expression are clearly correlated with L-ascorbic acid contents of cells during culture
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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, Arabidopsis thaliana (Q9M8S8)
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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)
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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), Arabidopsis thaliana (Q9M8S8), Arabidopsis thaliana Columbia-1 (Q9M8S8)
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 (B3GK03)
brenda
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