Castor bean biochemistry has long been thoroughly analysed in the context of lipids as they are industrially potent metabolites but profiling of other bio-molecules and their control over co-ordinated metabolism are not comprehensive.

Biochemists have made research on castor bean derived enzyme,phosphoenolpyruvate carboxylase(PEPC) which is an ubiquitous enzyme,implicated to carbon metabolism.The level and functional activity of this enzyme is  variable in castor seed and subjected to different molecular mechanisms for a regulation in functional activity during the course of seed development  .Recently, people have identified a modification called mono-ubiquitination in PEPC but its relevance to enzyme’s activity is not well understood and hence to identify its significance, biochemists have purified the enzyme and subjected for in vitro activity,inhibitor sensitivity and other physiochemical parameters.The results indicated a striking difference in enzyme behaviour between modified and unmodified versions with monoubiquitinated forms had a increased functional activity and enabled the researchers to detect the importance of this mechanism in developing castor seeds.Immunoelectroblotting and advanced mass spectrometry were the major analytical tools of this study.

The research is unique as it is often proved that ubiquitination will normally direct the labeled targets for proteolytic degradation for turn over.However in this case it is contrary and proves that this post translational modification in proteins is not completely favouring protein catabolism.

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