Revisiting histidine-dependent acid phosphatases: a distinct group of tyrosine phosphatases

Suresh Veeramani, Ming Shyue Lee, Ming-Fong Lin

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

Although classical protein tyrosine phosphatase (PTP) superfamily members are cysteine-dependent, emerging evidence shows that many acid phosphatases (AcPs) function as histidine-dependent PTPs in vivo. These AcPs dephosphorylate phospho-tyrosine substrates intracellularly and could have roles in development and disease. In contrast to cysteine-dependent PTPs, they utilize histidine, rather than cysteine, for substrate dephosphorylation. Structural analyses reveal that active site histidine, but not cysteine, faces towards the substrate and functions as the phosphate acceptor. Nonetheless, during dephosphorylation, both histidine-dependent and cysteine-dependent PTPs use their active site arginine and aspartate for substrate binding and proton donation, respectively. Thus, we propose that they should be referred to as a distinct group of 'histidine-dependent PTPs' within the PTP superfamily.

Original languageEnglish (US)
Pages (from-to)273-278
Number of pages6
JournalTrends in Biochemical Sciences
Volume34
Issue number6
DOIs
StatePublished - Jun 1 2009

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Acid Phosphatase
Phosphoric Monoester Hydrolases
Histidine
Cysteine
Tyrosine
Protein Tyrosine Phosphatases
Substrates
Catalytic Domain
Protons
Phosphates

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Cite this

Revisiting histidine-dependent acid phosphatases : a distinct group of tyrosine phosphatases. / Veeramani, Suresh; Lee, Ming Shyue; Lin, Ming-Fong.

In: Trends in Biochemical Sciences, Vol. 34, No. 6, 01.06.2009, p. 273-278.

Research output: Contribution to journalArticle

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