| Summary: | It has been observed that mycobacterial species has high content of cardiolipin (CL) in their cell membranes more so pathogenic
mycobacteria and in bacteria CL activates polymerases, gyrases by removing the bound ADP. Therefore, in the present study
cardiolipin synthase (cls) which catalyses the formation of CL was isolated purified and characterized from the cell membrane of
Mycobacterium phlei. The purified cls obtained from C-18 RP-HPLC column had a molecular weight of 58 kDa with an isoelectric
point of 4.5. The enzyme activity (11.5+0.15 µM of CL phosphorous. ml-1 minute-1 for PG as substrate and 14+0.35µM of CL
phosphorous. ml-1 minute-1 for CDP-DG as substrate) was optimal at pH 4.8 and showed KM values of 55+0.05µM and 2.56+0.04µM
for phosphatidyl glycerol and CDP-diacylglycerol, respectively, with an absolute requirement of Mg2+ and Mn2+ ions for its activity
however, Ca2+ ions inhibited the activity of the cls. The partial amino acid sequence of cls showed significant homology with pgsA3
gene of M. tuberculosis and in this organism the CL biosynthesis is very high having three genes coding for PLs biosynthesis
therefore, enzymes involved in CL biosynthesis may be an attractive drug target in the development of new antimycobacterial
drugs.
|
|---|