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EC Number
Protein Variants
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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
715482
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