A single amino acid substitution in soybean VSPalpha increases its acid phosphatase activity nearly 20-fold.

@article{Leelapon2004ASA,
  title={A single amino acid substitution in soybean VSPalpha increases its acid phosphatase activity nearly 20-fold.},
  author={Oranuch Leelapon and Gautam Sarath and Paul Staswick},
  journal={Planta},
  year={2004},
  volume={219 6},
  pages={1071-9}
}
Soybean [Glycine max (L.) Merr.] contains two proteins called vegetative storage proteins (VSPs) that function as temporary storage reserves, but are also closely related to plant acid phosphatases of the haloacid dehalogenase (HAD) superfamily. This study examined the biochemical basis for the relatively low catalytic activity previously reported for these VSPs. The specific activity of purified recombinant VSPalpha on GMP was about 40-fold lower than for a related soybean root nodule acid… CONTINUE READING