orthophosphoric-monoester phosphohydrolase (acid optimum)
6-phytase (name based on 1L-numbering system and not 1D-numbering)
myo-inositol-hexakisphosphate 6-phosphohydrolase (name based on1L-numbering system and not 1D-numbering)
1D-myo-inositol 1,2,3,4,5-pentakisphosphate
ARG 16;ARG 20;ARG 92;HIS 303(Stabilizers);HIS 17;ASP 304
ARG 16;ARG 20;ARG 92;HIS 303(Stabilizers); ;ASP 304
Three-dimensional structure of rat acid phosphatase in complex with L(+)-tartrate.
Crystal structures of rat acid phosphatase complexed with the transition-state analogs vanadate and molybdate. Implications for the reaction mechanism.
Heterologous expression of human prostatic acid phosphatase and site-directed mutagenesis of the enzyme active site.
Structural origins of L(+)-tartrate inhibition of human prostatic acid phosphatase.
Improvement of catalytic efficiency by site-directed mutagenesis
Site-directed mutagenesis improves catalytic efficiency and thermostability of Escherichia coli pH 2.5 acid phosphatase/phytase expressed in Pichia pastoris.
Crystal structures of Escherichia coli phytase and its complex with phytate.
Crystal structure of human prostatic acid phosphatase .
According to the literature [2] and [3], His12 (of 1rpa/1rpt) acts as nucleophile, which attacks the phosphorous atom of the phosphate ester, whilst Asp258 protonates the leaving group. At the next stage, the deprotonated Asp258 abstracts proton from the water, which hydrolyzes the phosphorylated imidazole ring of His12 [2]. Moreover, the three positively charged arginine residues (Arg11, Arg15, Arg79) near His12 play an important role in the catalysis, as follows [2]; (1) The positive charged groups lower the pKa of the nucelophilic histidine (His12), so that the acidic phosphatase can function below pH 7. (2) These groups will orient the phosphate group in a proper position so that the nucleophilic attack at the phosphorous atom can take place while the phosphorous-oxygen bond is cleaved.