Mycobacterium tuberculosis PE1 and PE2 proteins carrying conserved α/β-serine hydrolase domain are esterases hydrolyzing short to medium chain p-nitrophenyl esters

Progress in Biophysics and Molecular Biology
Bala Divya MLalitha Guruprasad

Abstract

The distinctive PE and PPE families of proteins in Mycobacterium tuberculosis (M.tb), the tuberculosis (TB) causing bacteria, have been associated primarily with antigenicity, immune-modulation and virulence. Earlier, using structure-based sequence annotation, we identified a 225 amino acid conserved PE-PPE domain (Pfam: PF08237) commonly present in some PE and PPE proteins which was observed to comprise α/β-serine hydrolase fold. The prediction was supported by experimental validations of PE16 that was shown to exhibit esterase activity. In this study, we undertook the characterization of the probable operonic ORFs Rv0151c (pe1) and Rv0152c (pe2). Here we demonstrated that pe1 and pe2 are operonic in organization and are co-transcribed. Both PE1 and PE2 proteins possess esterase activity and hydrolyze short to medium chain p-nitrophenyl esters with more specific activity for p-nitrophenyl caproate (C6) with the optimal catalytic conditions of 37-38 °C and pH 7.0-8.0. The thermal denaturation temperature of PE1 and PE2 proteins were found to be 50 °C. The esterase activity of full length PE1, PE2 and their PE-PPE (α/β-serine hydrolase) domains are similar indicating that the function of PE-PPE domain is independent of the rest ...Continue Reading

Citations

Jun 25, 2021·Biochemical and Biophysical Research Communications·Shruti Srivastava, Sangita Mukhopadhyay

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