European Journal of Biotechnology and Bioscience

Authors
Yogesh N Joshi, Prathusha S Chegu, Nitin N Bolabattin, Chetan Godale

Abstract
Pectin methylesterase (PME) is a ubiquitous cellwall- associated enzyme present in plants & certain micro-organisms. PME is a hydrolytic enzyme that catalyzes demethylesterification of the pectin homogalacturonan which present in the plant cell wall producing pectate and methanol. It has been proved that PME enzyme plays important role in seed germination of Arabidopsis thaliana allowing water uptake. The present in-silico study includes retrieval of sequence of PME of A. thaliana & its analysis followed by prediction of its domain, secondary structure & 3D structure which is further validated by PROCHECK analysis using various Insilco tools & servers. The results showed that the PME is alkaline, cationic enzyme having two domains PMEI & pectin esterase. In the secondary structure, it contains more % of random coils than helices & sheets & the most favorable region of predicted 3D structure is 86.1%. These findings will put insight into its functional role in seed germination which will be helpful to find the natural inhibitor & also to design the novel inhibitor to stop the seed germination process.