Characterization of protein acyltransferase function of recombinant purified GlnA1 from Mycobacterium tuberculosis: a moon lighting property.
作者： Anil S. Baghel , Rashmi Tandon , Garima Gupta , Ajit Kumar , Raman K. Sharma
DOI: 10.1016/J.MICRES.2011.02.001
关键词:
摘要: The protein acetyltransferase (MTAase) function of glutamine synthetase Mycobacterium smegmatis was established earlier. In this paper, studies were undertaken to examine MTAase recombinant (rGlnA1) tuberculosis, which showed >80% similarity with M. GlnA. specificity several acyl derivative coumarins examined. results clearly indicated that exhibited differential specificities acyloxycoumarins. Further, also found capable transferring propionyl and butyryl groups from propoxy butoxy derivatives 4-methylcoumarin. These observations characterized in general as a acyltransferase. catalyzed acetylation GST by 7,8-diacetoxy-4-methylcoumarin (DAMC), model acetoxy coumarin confirmed MALDI-TOF-MS well western blot analysis using acetylated lysine polyclonal antibody. order validate the active site rGlnA1 for TAase activity, effect DAMC L-methionine-S-sulfoximine (MSO) on GS activity studied. sites different. Acetyl CoA, universal biological acetyl group donor, be substrate MTAase. appropriately characterize Mtb exhibiting transacylase action moonlighting protein.
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