Stimulation of Staphylococcus aureus Ligase Enzyme by Magnesium Ion

Autor:	Ibrahim Faris Ali, Aseel A. H. Al-Layla, Arqam Mohamad Alomari
Rok vydání:	2021
Předmět:	chemistry.chemical_classification DNA ligase biology Health Toxicology and Mutagenesis DNA Ligases Toxicology Cofactor Pathology and Forensic Medicine Enzyme chemistry Biochemistry Phosphodiester bond biology.protein Transferase NAD+ kinase Law Magnesium ion
Zdroj:	Indian Journal of Forensic Medicine & Toxicology.
ISSN:	0973-9130 0973-9122
Popis:	Ligases enzymes were discovered as a member of the nucleotidyl transferase family. Here in this paper, DNALigase is extracted from S. aureus works with the cofactor NAD+ to make a phosphodiester bond and reformbetween the 3’hydroxyl and 5’phosphate DNA end. Staphylococcus aureus-DNA Ligases Enzyme type A(SLE-A) contains two essential domains; NTase and OB- fold domain, which are the most essential domainsfor the enzyme function. The main aim of the study is to investigate the activity of SLE-A in the presenceof magnesium ion (Mg+2) by evaluating several kinetic parameters on a time course. The result showed thatSLE-A has optimal activity at 500 µM of Mg+2. Furthermore, the low number of Equilibrium AssociationConstant (Km value) explains the binding affinity between DNA ligase of Staphylococcus aureus SLE-Aenzyme and Mg+2 ion was very high and sold.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::d9c4a7c1720bc0179b3801553805f378 https://doi.org/10.37506/ijfmt.v15i1.13723 Zobrazit plný text záznamu