Protozoan protein tyrosine phosphatases.
The aim of this review is to provide a synthesis of the published experimental data on protein tyrosine phosphatases from parasitic protozoa, in silico analysis based on the availability of completed genomes and to place available data for individual phosphatases from different unicellular parasites into the comparative and evolutionary context. We analysed the complement of protein tyrosine phosphatases (PTP) in several species of unicellular parasites that belong to Apicomplexa (Plasmodium; Cryptosporidium, Babesia, Theileria, and Toxoplasma), kinetoplastids (Leishmania and Trypanosoma spp.), as well as Entamoeba histolytica, Giardia lamblia, Trichomonas vaginalis and a microsporidium Encephalitozoon cuniculi. The analysis shows distinct distribution of the known families of tyrosine phosphatases in different species. Protozoan tyrosine phosphatases show considerable levels of divergence compared with their mammalian homologues, both in terms of sequence similarity between the catalytic domains and the structure of their flanking domains. This potentially makes them suitable targets for development of specific inhibitors with minimal effects on physiology of mammalian hosts.
Department of Pharmacology (MC 868), University of Illinois at Chicago, Chicago, IL 60612, USA. aandrev@uic.edu
Alexandra V
AV
Andreeva
Mikhail A
MA
Kutuzov
D000818:Animals; D016782:Apicomplexa / Q000201:enzymology; D056890:Eukaryota / Q000201:enzymology*; D016830:Kinetoplastida / Q000201:enzymology; D021861:Microsporidia, Unclassified / Q000276:immunology; D010766:Phosphorylation; D017027:Protein Tyrosine Phosphatases / Q000145:classification / Q000378:metabolism; D016053:RNA, Protozoan / Q000378:metabolism
D016053:RNA, Protozoan; D017027:Protein Tyrosine Phosphatases