Amycolatopsis sulphurea’dan Elde Edilen AsAlaDh’ın 3D Modellemesi ve Biyoinformatiği
Küçük Resim Yok
Tarih
2021
Yazarlar
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Osman SAĞDIÇ
Erişim Hakkı
info:eu-repo/semantics/openAccess
Özet
Alanin dehidrogenaz (AlaDH) (E.C.1.4.1.1), piruvat ve alaninin birbirine dönüşümünü katalize eden bir enzimdir. Bu enzim, mikroorganizmanın sporlanması ve mikroorganizmalardaki birçok amino asit, protein ve peptidoglikan tabakasının sentezi için anahtar katalitik role sahiptir. Amycolatopsis sulphurea, Pseudonocardiaceae familyası içindeki Amycolatopsis cinsinin suşlarından biri olup, Ristosetin, Vankomisin ve Epoksiquinomisin gibi farklı antibiyotikler üretmenin yanı sıra biyoplastik (poli-laktik asit (PLA) filmlerini biyolojik olarak parçalama yeteneğine sahiptir). Amycolatopsis sulphurea'dan Alanin dehidrogenazın 3D homoloji modeli I-TASSER aracılığıyla gerçekleştirildi. L-alanin ile enzimin aktif bölge amino asitlerinin etkileşimi, AutoDock Vina programı ile in silico kenetlenerek belirlendi. Protein ikincil yapıları EMBOSS tool garnier ile tahmin edildi. AsAlaDH'nin yapısal ve fonksiyonel analizleri ve fiziko-kimyasal özelliklerinin belirlenmesi farklı biyoinformatik araçlar kullanılarak gerçekleştirilmiştir. Alanin dehidrogenazın ikincil yapısı ve çoklu hizalama analizi, AlaDH'lerin farklı mikroorganizmalardan korunmuş amino asit kalıntıları olduğunu göstermiştir.
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.
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.
Açıklama
Anahtar Kelimeler
Engineering, Mühendislik
Kaynak
European Journal of Science and Technology
WoS Q Değeri
Scopus Q Değeri
Cilt
Sayı
25
