PJB-2023-187
STRUCTURE ANALYSIS OF REGULATORY PROTEINS IN
Hina Nayab
Abstract
Isocitrate dehydrogenase (IDH) and Oxoglutarate dehydrogenase (OGDH) are two enzymes referred to as rate-limiting enzymes of Tricarboxylic acid (TCA) cycle. Both enzymes regulate 2-Oxogluterate production, which is a branch that links carbohydrate and amino acid metabolism. The structures of these two enzymes from Arabidopsis thaliana have not been solved yet. Through template-based homology modelling using different software such as Robetta and Alphafold, the three-dimensional structure of the enzymes of Arabidopsis thaliana has been predicted. The expression analysis of enzymes was also performed using GENEVESTIGATOR and Expression Angler BAR. The protein structure prediction revealed that isocitrate dehydrogenase displayed an alternative mixed structure; and oxoglutarate dehydrogenase displayed an alpha-beta sheet structure. Structure validation by the PROCHECK and ProSA databases has shown that Robetta has provided more real structure than Alphafold. By using a STRING database based on neighborhood and co-expression parameters, the interactions of the enzymes within the TCA cycle and other metabolic pathways such as glutamate and L-leucine biosynthesis, pyruvate metabolism, and glycine decarboxylation were thoroughly observed. The study of eight developmental stages revealed that isocitrate dehydrogenase was highly expressed during the senescence time compared to oxoglutarate. In-silico modelling of the proteins IDH and OGDH studied here was successful through Robetta.
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