Revisiting histidine-dependent acid phosphatases: a distinct group of tyrosine phosphatases
Journal
Trends in Biochemical Sciences
Journal Volume
34
Journal Issue
6
Pages
273-278
Date Issued
2009
Author(s)
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. ? 2009 Elsevier Ltd. All rights reserved.
SDGs
Other Subjects
acid phosphatase; arginine; aspartic acid; cysteine; epidermal growth factor receptor 2; epidermal growth factor receptor 4; histidine; membrane enzyme; protein tyrosine phosphatase; protein Wzc; unclassified drug; amino acid metabolism; amino acid sequence; article; enzyme active site; enzyme activity; enzyme binding; enzyme structure; enzyme substrate; human; in vivo study; nerve cell; nonhuman; phytochemistry; priority journal; prostate epithelium; protein dephosphorylation; protein expression; Acid Phosphatase; Animals; Catalytic Domain; Cysteine; Histidine; Humans; Models, Biological; Neurons; Phosphates; Phylogeny; Plants; Protein Conformation; Protein Tyrosine Phosphatases; Species Specificity
Type
journal article