Article ; Online: Construing recombinant ZFP160 from Aspergillus terreus as pterin deaminase enzyme.
Biotechnology and applied biochemistry
2023 Volume 70, Issue 6, Page(s) 2150–2162
Abstract: Pterin deaminase stands as a metalloenzyme and exhibits both antitumor and anticancer activities. Therefore, this study aimed to explore the molecular function of zinc finger protein-160 (zfp160) from Aspergillus terreus with its enzyme mechanism in ... ...
Abstract | Pterin deaminase stands as a metalloenzyme and exhibits both antitumor and anticancer activities. Therefore, this study aimed to explore the molecular function of zinc finger protein-160 (zfp160) from Aspergillus terreus with its enzyme mechanism in detail. Subsequently, preliminary molecular docking studies on zfp160 from A. terreus were done. Next, the cloning and expression of zfp160 protein were carried out. Following, protein expression was induced and purified through nickel NTA column with imidazole gradient elution. Through the Mascot search engine tool, the expressed protein of MALDI-TOF was confirmed by 32 kDa bands of SDS-PAGE. Furthermore, its enzymatic characterization and biochemical categorization were also explored. The optimum conditions for enzyme were determined to be pH 8, temperature 35°C, km 50 μm with folic acid as substrate, and V |
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MeSH term(s) | Molecular Docking Simulation ; Aspergillus ; Aminohydrolases/chemistry ; Aminohydrolases/metabolism ; Hydrogen-Ion Concentration ; Temperature |
Chemical Substances | pterin deaminase (EC 3.5.4.11) ; Aminohydrolases (EC 3.5.4.-) |
Language | English |
Publishing date | 2023-09-27 |
Publishing country | United States |
Document type | Journal Article |
ZDB-ID | 883433-7 |
ISSN | 1470-8744 ; 0885-4513 |
ISSN (online) | 1470-8744 |
ISSN | 0885-4513 |
DOI | 10.1002/bab.2515 |
Database | MEDical Literature Analysis and Retrieval System OnLINE |
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