Characterization of pterin deaminase from Mucor indicus MTCC 3513

International Conference on Green Agro-industry and Bioeconomy 2017

农业科学;生物科学;经济学

Thandeeswaran, M.^1 ; Karthika, P.^1 ; Mahendran, R.^1 ; Palaniswamy, M.^2 ; Angayarkanni, J.^1

Cancer Therapeutics Lab, Department of Microbial Biotechnology, Bharathiar University, Tamil Nadu Coimbatore, India^1

Department of Microbiology, School of Life Sciences, Karpagam University, Tamil Nadu Coimbatore, India^2

关键词: Amidohydrolase;    Binding affinities;    Cancer therapy;    Ethanol precipitation;    Fast protein liquid chromatography;    Ion-exchange columns;    Molecular docking;    Purified enzyme;   

Others  :  https://iopscience.iop.org/article/10.1088/1755-1315/131/1/012044/pdf
DOI  :  10.1088/1755-1315/131/1/012044

来源: IOP

【 摘 要 】

Pterin deaminase is an amidohydrolase enzyme which hydrolyses pteridines to produce lumazine derivatives and ammonia. Even though the enzyme was shown as early as 1959 for its anticancer efficacy there was a long gap in the communique after that which was in 2013. In our study we have chosen Mucor indicus MTCC 3513 which was a promising strain for production of different industrial products.The pterin deaminase enzyme was harvested and extracellular from M. indicus. The extracellular sample was partially purified by using ethanol precipitation and ion exchange column (Hi-Trap QFF) in Fast Protein Liquid Chromatography. The molecular weight of the purified pterin deaminase enzyme was apparently determined by SDS-PAGE. The purified enzyme was further biochemically characterized. Molecular docking studies with the predicted sequence showed higher binding affinity towards folic acid interaction. The structure of this protein may open the windows for new drug targets for cancer therapy.