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

BRENDA support

Literature summary for 3.1.3.B9 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
Search for more literature for 3.1.3.B9

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Arabidopsis thaliana Q9M8S8
-
-

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
 Arabidopsis thaliana
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
At3g02870
-
 Arabidopsis thaliana
L-galactose-1-P phosphatase
-
 Arabidopsis thaliana
L-galactose-1-phosphate phosphatase
-
 Arabidopsis thaliana
VTC4
-
 Arabidopsis thaliana

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
20
-
 assay at Arabidopsis thaliana

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Arabidopsis thaliana

General Information

General Information Comment Organism
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