Molecular mechanisms underlying catalytic activity of delta 6 desaturase from Glossomastix chrysoplasta and Thalassiosira pseudonana

摘要: Delta 6 desaturase (FADS2) is a critical bifunctional enzyme required for PUFA biosynthesis. In some organisms, FADS2s have high substrate specificity, whereas in others, they catalytic activity. Previously, we analyzed the molecular mechanisms underlying FADS2 specificity; this study, assessed those activity of from Glossomastix chrysoplasta and Thalassiosira pseudonana To understand structural basis activity, GcFADS2 TpFADS2 sequences were divided into nine sections, domain-swapping approach was applied to examine role each section facilitating overall protein. The results revealed two regions essential process: one that extends end fourth beginning fifth cytoplasmic transmembrane domain, another includes C-terminal region occurs after sixth domain. Based on analyses, amino acid residues at ten sites identified differ between sequences, therefore further by site-directed mutagenesis. T302V, S322A, Y375F, M384S/M385 substitutions significantly affected efficiency. This study offers solid in-depth understanding efficiency FADS2.