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