Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • 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 (2006), J. Biol. Chem., 281, 15662-15670.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.1.3.93 P92L 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 Arabidopsis thaliana

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.3.B9 L-galactose 1-phosphate + H2O Arabidopsis thaliana 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 L-galactose + phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.B9 Arabidopsis thaliana Q9M8S8
-
-
3.1.3.93 Arabidopsis thaliana Q9M8S8
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.3.B9 leaf
-
 Arabidopsis thaliana
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.B9 L-galactose 1-phosphate + H2O
-
 Arabidopsis thaliana L-galactose + phosphate
-
 ?
3.1.3.B9 L-galactose 1-phosphate + H2O 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 Arabidopsis thaliana L-galactose + phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.3.B9 At3g02870
-
 Arabidopsis thaliana
3.1.3.B9 L-galactose-1-P phosphatase
-
 Arabidopsis thaliana
3.1.3.B9 L-galactose-1-phosphate phosphatase
-
 Arabidopsis thaliana
3.1.3.B9 VTC4
-
 Arabidopsis thaliana
3.1.3.93 At3g02870 locus name Arabidopsis thaliana
3.1.3.93 VTC4
-
 Arabidopsis thaliana

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.3.B9 20
-
 assay at Arabidopsis thaliana

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.3.B9 7.5
-
 assay at Arabidopsis thaliana

General Information

EC Number General Information Comment Organism
3.1.3.B9 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 Arabidopsis thaliana
3.1.3.93 physiological function 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 Arabidopsis thaliana