Molecular architecture of pterin deaminase from Saccharomyces cerevisiae NCIM 3458-Reference-Cited by-同舟云学术

Molecular architecture of pterin deaminase from Saccharomyces cerevisiae NCIM 3458

Published:2017-10-14 Issue:3-4 Volume:28 Page:141-151
ISSN:2195-4720
Container-title:Pteridines
language:en
Short-container-title:

Author:

Murugesan Thandeeswaran¹,Velliayadevar Karuppuswamy¹,Easwaran Murugesh²,KG Kiran¹,KA Ayub Nawaz¹,Ramasamy Mahendran¹,Muthusamy Palaniswamy³,Jayaraman Angayarkanni¹

Affiliation:

1. Cancer Therapeutics Lab , Department of Microbial Biotechnology , Bharathiar University , Coimbatore 641046, Tamilnadu , India

2. Department of Bioinformatics , Bharathiar University , Coimbatore 641046, Tamilnadu , India

3. Department of Microbiology , Karpagam University , Coimbatore 641021, Tamilnadu , India

Abstract

Abstract As early as 1974, reports have confirmed the anticancer activity of pterin deaminase isolated from fungi. The enzyme has also been reported in bacteria, fungi and slime mold genera, but the enzyme characterization was effetely done. The present study attempted to purify and characterize pterin deaminase enzyme from Saccharomyces cerevisiae NCIM 3458. The protein was extracted from the extracellular extract by using the ethanol precipitation method. Partial purification of pterin deaminase enzyme was achieved by ion exchange chromatography (Hi-Trap QFF) by fast protein liquid chromatography (AKTA purifier). The molecular weight of the protein was apparently determined by SDS-PAGE, and the presence of pterin deaminase was confirmed by activity staining. The purified enzyme was further biochemically characterized. Molecular docking studies showed higher binding affinity towards folic acid interaction. The structural characterization of this protein may open the windows for new drug targets for cancer therapy.

Publisher

Walter de Gruyter GmbH

Subject

Clinical Biochemistry,Molecular Medicine,Biochemistry

Link

https://www.degruyter.com/document/doi/10.1515/pterid-2017-0011/pdf

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