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

Suresh Veeramani, Ming Shyue Lee, Ming Fong Lin

Research output: Contribution to journalArticle

15 Scopus citations

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 2009

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Fingerprint Dive into the research topics of 'Revisiting histidine-dependent acid phosphatases: a distinct group of tyrosine phosphatases'. Together they form a unique fingerprint.

  • Cite this