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Shelphs

Shewanella-like phosphatases, abbreviated as Shelphs, are a group of enzymes structurally related to protein serine/threonine phosphatases (PPP family).[1] Unlike the canonical subfamilies found in eukaryotes (PP1, PP2A, calcineurin, PP5 and PPEF/PP7),[1][2][3] Shelphs span the eukaryote-prokaryote boundary and are found in several genera of Pseudomonadota (formerly proteobacteria), in plants, red algae, fungi and some unicellular parasites, including a causative agent of malaria Plasmodium, Cryptosporidium and kinetoplastids (Trypanosoma and Leishmania species).[4]

The prototypic member of the group, a phosphatase from a psychrophilic bacterium Shewanella, has been studied as a model to understand the mechanisms that contribute to the high catalytic efficiency of enzymes from organisms adapted to low temperatures.[5][6] Although PPP phosphatases in general are serine/threonine specific,[1] Shewanella phosphatase is tyrosine specific.[5] One of the two Shelph isoforms in plants is predicted to be located in the chloroplast.[4]

Due to the absence of Shelphs in humans, these phosphatases have recently attracted attention as potential targets for new antiparasitic drug discovery.[7][8][9]

References

  1. ^ a b c Cohen PT (July 1997). "Novel protein serine/threonine phosphatases: variety is the spice of life". Trends in Biochemical Sciences. 22 (7): 245–51. doi:10.1016/S0968-0004(97)01060-8. PMID 9255065.
  2. ^ Andreeva AV, Kutuzov MA (1 March 2001). "PPP family of protein Ser/Thr phosphatases: two distinct branches?". Molecular Biology and Evolution. 18 (3): 448–52. doi:10.1093/oxfordjournals.molbev.a003823. PMID 11230548.
  3. ^ Farkas I, Dombrádi V, Miskei M, Szabados L, Koncz C (April 2007). "Arabidopsis PPP family of serine/threonine phosphatases". Trends in Plant Science. 12 (4): 169–76. Bibcode:2007TPS....12..169F. doi:10.1016/j.tplants.2007.03.003. hdl:11858/00-001M-0000-0012-388C-7. PMID 17368080.
  4. ^ a b Andreeva AV, Kutuzov MA (November 2004). "Widespread presence of "bacterial-like" PPP phosphatases in eukaryotes". BMC Evolutionary Biology. 4 47. doi:10.1186/1471-2148-4-47. PMC 535813. PMID 15555063.
  5. ^ a b Tsuruta H, Aizono Y (January 2000). "Cloning of phosphatase I gene from a psychrophile, Shewanella sp., and some properties of the recombinant enzyme". Journal of Biochemistry. 127 (1): 143–9. doi:10.1093/oxfordjournals.jbchem.a022576. PMID 10731677.
  6. ^ Tsuruta H, Mikami B, Yamamoto C, Yamagata H (September 2008). "The role of group bulkiness in the catalytic activity of psychrophile cold-active protein tyrosine phosphatase". The FEBS Journal. 275 (17): 4317–28. doi:10.1111/j.1742-4658.2008.06575.x. PMID 18647345.
  7. ^ Kutuzov MA, Andreeva AV (October 2008). "Protein Ser/Thr phosphatases of parasitic protozoa". Molecular and Biochemical Parasitology. 161 (2): 81–90. doi:10.1016/j.molbiopara.2008.06.008. PMID 18619495.
  8. ^ Wilkes JM, Doerig C (2008). "The protein-phosphatome of the human malaria parasite Plasmodium falciparum". BMC Genomics. 9: 412. doi:10.1186/1471-2164-9-412. PMC 2559854. PMID 18793411.
  9. ^ Bajsa J, Duke SO, Tekwani BL (November 2008). "Plasmodium falciparum serine/threonine phoshoprotein phosphatases (PPP): from housekeeper to the 'holy grail'". Current Drug Targets. 9 (11): 997–1012. doi:10.2174/138945008786786055. PMID 18991611.

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