Reconstruction of mycobacterial dehalogenase Rv2579 by cumulative mutagenesis of haloalkane dehalogenase LinB

Yuji Nagata, Zbyněk Prokop, Soňa Marvanová, Jana Sýkorova, Marta Monincová, Masataka Tsuda, Jiří Damborský

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19 Citations (Scopus)

Abstract

The homology model of protein Rv2579 from Mycobacterium tuberculosis H37Rv was compared with the crystal structure of haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26, and this analysis revealed that 6 of 19 amino acid residues which form an active site and entrance tunnel are different in LinB and Rv2579. To characterize the effect of replacement of these six amino acid residues, mutations were introduced cumulatively into the six amino acid residues of LinB. The sixfold mutant, which was supposed to have the active site of Rv2579, exhibited haloalkane dehalogenase activity with the haloalkanes tested, confirming that Rv2579 is a member of the haloalkane dehalogenase protein family.

Original languageEnglish
Pages (from-to)2349-2355
Number of pages7
JournalApplied and environmental microbiology
Volume69
Issue number4
DOIs
Publication statusPublished - 2003 Apr 1

ASJC Scopus subject areas

  • Biotechnology
  • Food Science
  • Applied Microbiology and Biotechnology
  • Ecology

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