Identification and structural prediction of the unrevealed amidohydrolase enzyme: Pterin deaminase from Agrobacterium tumefaciens LBA4404.
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| Title: | Identification and structural prediction of the unrevealed amidohydrolase enzyme: Pterin deaminase from Agrobacterium tumefaciens LBA4404. |
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| Authors: | Dhanapal, Anand Raj1 (AUTHOR) rajanandvk88d@gmail.com, Thandeeswaran, Murugesan2 (AUTHOR) thandeesm@gmail.com, Muthusamy, Palaniswamy3 (AUTHOR) m.palaniswamy@gmail.com, Jayaraman, Angayarkanni2 (AUTHOR) angaibiotech@buc.edu.in |
| Source: | Biotechnology & Applied Biochemistry. Feb2023, Vol. 70 Issue 1, p193-200. 8p. |
| Subjects: | Agrobacterium tumefaciens, Enzyme stability, Enzyme specificity, Endoenzymes, Bacterial enzymes, Microbial enzymes, Polyacrylamide gel electrophoresis |
| Abstract: | Microbes make a remarkable contribution to the health and well‐being of living beings all over the world. Interestingly, pterin deaminase is an amidohydrolase enzyme that exhibits antitumor, anticancer activities and antioxidant properties. With the existing evidence of the presence of pterin deaminase from microbial sources, an attempt was made to reveal the existence of this enzyme in the unexplored bacterium Agrobacterium tumefaciens LBA4404. After, the cells were harvested and characterized as intracellular enzymes and then partially purified through acetone precipitation. Subsequently, further purification step was carried out with an ion‐exchange chromatogram (HiTrap Q FF) using the Fast‐Protein Liquid Chromatography technique (FPLC). Henceforward, the approximate molecular weight of the purified pterin deaminase was determined through SDS–PAGE. Furthermore, the purified protein was identified accurately by MALDI‐TOF, and the sequence was explored through a Mascot search engine. Additionally, the three‐dimensional structure was predicted and then validated, as well as ligand‐binding sites, and the stability of this enzyme was confirmed for the first time. Thus, the present study revealed the selected parameters showing a considerable impact on the identification and purification of pterin deaminase from A. tumefaciens LBA4404 for the first time. The enzyme specificity makes it a favorable choice as a potent anticancer agent. [ABSTRACT FROM AUTHOR] |
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| Database: | Engineering Source |
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| Abstract: | Microbes make a remarkable contribution to the health and well‐being of living beings all over the world. Interestingly, pterin deaminase is an amidohydrolase enzyme that exhibits antitumor, anticancer activities and antioxidant properties. With the existing evidence of the presence of pterin deaminase from microbial sources, an attempt was made to reveal the existence of this enzyme in the unexplored bacterium Agrobacterium tumefaciens LBA4404. After, the cells were harvested and characterized as intracellular enzymes and then partially purified through acetone precipitation. Subsequently, further purification step was carried out with an ion‐exchange chromatogram (HiTrap Q FF) using the Fast‐Protein Liquid Chromatography technique (FPLC). Henceforward, the approximate molecular weight of the purified pterin deaminase was determined through SDS–PAGE. Furthermore, the purified protein was identified accurately by MALDI‐TOF, and the sequence was explored through a Mascot search engine. Additionally, the three‐dimensional structure was predicted and then validated, as well as ligand‐binding sites, and the stability of this enzyme was confirmed for the first time. Thus, the present study revealed the selected parameters showing a considerable impact on the identification and purification of pterin deaminase from A. tumefaciens LBA4404 for the first time. The enzyme specificity makes it a favorable choice as a potent anticancer agent. [ABSTRACT FROM AUTHOR] |
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| ISSN: | 08854513 |
| DOI: | 10.1002/bab.2342 |
