| Title : Expression and characterization of the carboxyl esterase Rv3487c from Mycobacterium tuberculosis - Zhang_2005_Protein.Expr.Purif_42_59 |
| Author(s) : Zhang M , Wang JD , Li ZF , Xie J , Yang YP , Zhong Y , Wang HH |
| Ref : Protein Expr Purif , 42 :59 , 2005 |
|
Abstract :
Rv3487c (lipF), a member of the lipase family of Mycobacterium tuberculosis, is related to virulence of this pathogen. Real-time RT-PCR analysis indicated that Rv3487c was induced at low pH in M. tuberculosis cultured in vitro. The gene of Rv3487c was cloned and expressed as fusion protein in Escherichia coli. After removal of the N-terminal domain of the fusion partner by enterokinase treatment, the effect of pH, temperature, and detergents on the purified enzyme activity and stability was characterized. Rv3487c could efficiently hydrolyze short chain esters. The catalytic triad of Rv3487c consists of residues Ser90, Glu189, and His219 as demonstrated by amino acid sequence alignment, three-dimensional modeling, and site-directed mutagenesis. |
| PubMedSearch : Zhang_2005_Protein.Expr.Purif_42_59 |
| PubMedID: 15939293 |
| Gene_locus related to this paper: myctu-Rv3487c |
| Gene_locus | myctu-Rv3487c |
Zhang M, Wang JD, Li ZF, Xie J, Yang YP, Zhong Y, Wang HH (2005)
Expression and characterization of the carboxyl esterase Rv3487c from Mycobacterium tuberculosis
Protein Expr Purif
42 :59
Zhang M, Wang JD, Li ZF, Xie J, Yang YP, Zhong Y, Wang HH (2005)
Protein Expr Purif
42 :59