Literature summary for 3.1.3.93 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.

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Protein Variants

Protein Variants	Comment	Organism
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

Organism

Organism	UniProt	Comment	Textmining
Arabidopsis thaliana	Q9M8S8	-	-

Synonyms

Synonyms	Comment	Organism
At3g02870	locus name	Arabidopsis thaliana
VTC4	-	Arabidopsis thaliana

General Information

General Information	Comment	Organism
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

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Release 2023.1 (January 2023)