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] |
| Copyright of Biotechnology & Applied Biochemistry is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Database: | Engineering Source |
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| Header | DbId: egs DbLabel: Engineering Source An: 161968638 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: Identification and structural prediction of the unrevealed amidohydrolase enzyme: Pterin deaminase from Agrobacterium tumefaciens LBA4404. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Dhanapal%2C+Anand+Raj%22">Dhanapal, Anand Raj</searchLink><relatesTo>1</relatesTo> (AUTHOR)<i> rajanandvk88d@gmail.com</i><br /><searchLink fieldCode="AR" term="%22Thandeeswaran%2C+Murugesan%22">Thandeeswaran, Murugesan</searchLink><relatesTo>2</relatesTo> (AUTHOR)<i> thandeesm@gmail.com</i><br /><searchLink fieldCode="AR" term="%22Muthusamy%2C+Palaniswamy%22">Muthusamy, Palaniswamy</searchLink><relatesTo>3</relatesTo> (AUTHOR)<i> m.palaniswamy@gmail.com</i><br /><searchLink fieldCode="AR" term="%22Jayaraman%2C+Angayarkanni%22">Jayaraman, Angayarkanni</searchLink><relatesTo>2</relatesTo> (AUTHOR)<i> angaibiotech@buc.edu.in</i> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Biotechnology+%26+Applied+Biochemistry%22">Biotechnology & Applied Biochemistry</searchLink>. Feb2023, Vol. 70 Issue 1, p193-200. 8p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Agrobacterium+tumefaciens%22">Agrobacterium tumefaciens</searchLink><br /><searchLink fieldCode="DE" term="%22Enzyme+stability%22">Enzyme stability</searchLink><br /><searchLink fieldCode="DE" term="%22Enzyme+specificity%22">Enzyme specificity</searchLink><br /><searchLink fieldCode="DE" term="%22Endoenzymes%22">Endoenzymes</searchLink><br /><searchLink fieldCode="DE" term="%22Bacterial+enzymes%22">Bacterial enzymes</searchLink><br /><searchLink fieldCode="DE" term="%22Microbial+enzymes%22">Microbial enzymes</searchLink><br /><searchLink fieldCode="DE" term="%22Polyacrylamide+gel+electrophoresis%22">Polyacrylamide gel electrophoresis</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: 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] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Biotechnology & Applied Biochemistry is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1002/bab.2342 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 8 StartPage: 193 Subjects: – SubjectFull: Agrobacterium tumefaciens Type: general – SubjectFull: Enzyme stability Type: general – SubjectFull: Enzyme specificity Type: general – SubjectFull: Endoenzymes Type: general – SubjectFull: Bacterial enzymes Type: general – SubjectFull: Microbial enzymes Type: general – SubjectFull: Polyacrylamide gel electrophoresis Type: general Titles: – TitleFull: Identification and structural prediction of the unrevealed amidohydrolase enzyme: Pterin deaminase from Agrobacterium tumefaciens LBA4404. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Dhanapal, Anand Raj – PersonEntity: Name: NameFull: Thandeeswaran, Murugesan – PersonEntity: Name: NameFull: Muthusamy, Palaniswamy – PersonEntity: Name: NameFull: Jayaraman, Angayarkanni IsPartOfRelationships: – BibEntity: Dates: – D: 01 M: 02 Text: Feb2023 Type: published Y: 2023 Identifiers: – Type: issn-print Value: 08854513 Numbering: – Type: volume Value: 70 – Type: issue Value: 1 Titles: – TitleFull: Biotechnology & Applied Biochemistry Type: main |
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