Record number :
1256085
Title of article :
A Novel Phosphatase Family, Structurally Related to Dual-specificity Phosphatases, that Displays Unique Amino Acid Sequence and Substrate Specificity
Author/Authors :
Carlos Rom?-Mateo، نويسنده , , Pablo R?os، نويسنده , , Lydia Tabernero، نويسنده , , Teresa K. Attwood، نويسنده , , Rafael Pulido، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2007
Pages :
11
From page :
899
To page :
909
Abstract :
Members of the superfamily of protein tyrosine phosphatases (PTPs) share the presence of an evolutionarily conserved PTP catalytic domain. Among them, the dual-specificity phosphatases (DSPs) constitute a diverse group of enzymes in terms of substrate specificity, including nonprotein substrates. In recent years, an increasing number of novel DSPs, whose functions and biological substrates are not well defined, have been discovered in a variety of organisms. In this study, we define the structural and functional properties of evolutionarily related atypical DSPs from different phyla. Sets of conserved motifs were defined that (i) uniquely segregated mammalian atypical DSPs from closely related enzymes and (ii) exclusively characterised a novel family of atypical DSPs present in plants, fungi, and kinetoplastids [plant and fungi atypical (PFA)-DSPs]; despite having different sequence “fingerprints,” the PTP tertiary structure of PFA-DSPs is conserved. Analysis of the catalytic properties of PFA-DSPs suggests the existence of a unique substrate specificity for these enzymes. Our findings predict characteristic functional motifs for the diverse members of the DSP families of PTPs and provide insights into the functional properties of DSPs of unknown function.
Keywords :
fingerprint analysis , dephosphorylation , protein tyrosine phosphatases , dual-specificity phosphatases , plant phosphatases
Journal title :
Journal of Molecular Biology
Serial Year :
2007
Link To Document :
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