Human prostatic acid phosphatase has phosphotyrosyl protein phosphatase activity

M. F. Lin, G. M. Clinton

Research output: Contribution to journalArticlepeer-review

84 Scopus citations

Abstract

The major secreted isoenzyme of human prostatic acid phosphatase (PAcP) (EC 3.1.3.2), which catalyses p-nitrophenyl phosphatase (PNPP) hydrolysis at acid pH values, was found to have phosphotyrosyl protein phosphatase activity since it dephosphorylated three different phosphotyrosine-containing protein substrates. Several lines of evidence are presented to show that the phosphotyrosyl phosphatase and PAcP are the same enzyme. (1) A highly purified PAcP enzyme preparation which contains a single N-terminal peptide sequence was used to test for the phosphotyrosyl phosphatase activity. (2) Both activities comigrated during gel filtration by high performance liquid chromatography. (3) Phosphotyrosyl phosphatase activity and PNPP acid phosphatase activity exhibited similar sensitivities to different effectors. (4) Both phosphatase activities showed the same thermal stability. (5) Specific anti-PAcP antibody reacted to the same extent with both phosphatase activities. (6) PNPP acid phosphatase activity was competitively inhibited by the phosphotyrosyl phosphatase substrate. To characterize further the phosphotyrosyl phosphatase activity, the K(m) values using different phosphoprotein substrates were determined. The apparent K(m) values for phosphorylated angiotensin II, anti-pp60src immunoglobulin G and casein were in the nM range for phosphotyrosine residues, which was about 50-fold lower than the K(m) for phosphoserine residues in casein.

Original languageEnglish (US)
Pages (from-to)351-357
Number of pages7
JournalBiochemical Journal
Volume235
Issue number2
DOIs
StatePublished - 1986
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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