Bioinformatics and 3D homology modelling of AsAlaDH fromAmycolatopsis sulphurea

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2021

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info:eu-repo/semantics/openAccess

Özet

Alanine dehydrogenase (AlaDH) (E.C.1.4.1.1) is an enzyme that catalyzes the interconversion of pyruvate and alanine. This enzymehas the key catalytic role for the sporulation of microorganisms and synthesis of the many amino acids, proteins, and peptidoglycanlayers in the microorganisms. Amycolatopsis sulphurea one of the strains of Amycolatopsis genus within the familyPseudonocardiaceae has capable to produce different antibiotics such as Ristocetin, Vancomycin, and Epoxyquinomicin as well as tobiodegrade the bioplastic (poly-lactic acid (PLA) films). The 3D homology model of Alanine dehydrogenase from Amycolatopsissulphurea was carried out through I-TASSER. The interaction of L-alanine and active site amino acids of the enzyme was determinedby docking in silico via AutoDock Vina program. Protein secondary structures were predicted with EMBOSS tool garnier. Structuraland functional analysis and determination of Physico-chemical properties of AsAlaDH were performed by using differentbioinformatics tools. The secondary structure and multiple alignment analysis of alanine dehydrogenase displayed that there areconserved amino acid residues of AlaDH's from different microorganisms.

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Avrupa Bilim ve Teknoloji Dergisi

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0

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25

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