Title |
Isolation, purification and characterization of Cardiolipin synthase from Mycobacterium phlei {PRIVATE}
|
Authors |
Potukuchi Venkata Gurunadha Krishna Sarma1*, Lokanathan Srikanth1, Katari Venkatesh1, P Suryanarayana Murthy1 & Puranam Usha Sarma2
|
Affiliation |
1Department of Biotechnology, Sri Venkateswara Institute of Medical Sciences, Tirupati 517507; 2Department of Virology, Indian Agricultural Research Institute, Pusa Road, New Delhi 110012 |
|
pvgksarma@gmail.com; *Corresponding author |
Article Type |
Hypothesis |
Date |
Received July 08, 2013; Accepted July 08, 2013; Published July 17, 2013
|
Abstract |
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. |
Keywords |
Cardiolipin, Cardiolipin synthase, CDP-diacylglycerol and phosphatidyl glycerol
|
Citation |
Sarma et al.
Bioinformation 9(13): 690-695 (2013) |
Edited by |
P Kangueane
|
ISSN |
0973-2063
|
Publisher |
|
License |
This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License. |