TY - JOUR
T1 - Reconstruction of mycobacterial dehalogenase Rv2579 by cumulative mutagenesis of haloalkane dehalogenase LinB
AU - Nagata, Yuji
AU - Prokop, Zbyněk
AU - Marvanová, Soňa
AU - Sýkorova, Jana
AU - Monincová, Marta
AU - Tsuda, Masataka
AU - Damborský, Jiří
PY - 2003/4/1
Y1 - 2003/4/1
N2 - 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.
AB - 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.
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U2 - 10.1128/AEM.69.4.2349-2355.2003
DO - 10.1128/AEM.69.4.2349-2355.2003
M3 - Article
C2 - 12676719
AN - SCOPUS:0242432320
SN - 0099-2240
VL - 69
SP - 2349
EP - 2355
JO - Applied and Environmental Microbiology
JF - Applied and Environmental Microbiology
IS - 4
ER -
