Reconstruction of Mycobacterial Dehalogenase Rv2579 by Cumulative Mutagenesis of Haloalkane Dehalogenase LinB

Author:

Nagata Yuji1,Prokop Zbyněk2,Marvanová Soňa2,Sýkorová Jana2,Monincová Marta2,Tsuda Masataka1,Damborský Jiří2

Affiliation:

1. Department of Life Sciences, Graduate School of Life Sciences, Tohoku University, Sendai 980-8577, Japan

2. National Centre for Biomolecular Research, Masaryk University, 611 37 Brno, Czech Republic

Abstract

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.

Publisher

American Society for Microbiology

Subject

Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology

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