Homology modeling and in silico characterization of an alliinase protein from Allium tuberosum Rottler ex Spreng

Information of the three dimensional structure of any protein is essential for further study of its function and evolution. In this study, physocochemical characterization of an alliinase protein from Allium tuberosum Rottler ex Spreng. has been performed by some bioinformatic tools and three dimensional structure of this protein has been predicted in silico by homology modeling approach. The study showed that this protein is basic in nature and it is a stable protein. It showed two domains namely EGF_alliinase and Alliinase_C. Secondary structure prediction revealed the predominance of random coils which indicates the structural flexibility and stability of this protein. The three-dimensional structure is composed of several alpha helices and beta sheets. The surface electrostatic potentials showed large positive and negative potential patches over its entire surface. This study provides insight into the structural properties of alliinase which are important for further depiction of the roles of this enzyme class in the genus Allium.