γ-Aminobutyric acid (GABA) is a very important metabolite which plays a crucial role in signal transmission, stress metabolism and some other activities are also reported. Although the actual role of GABA shunt is not clearly understood. Three key enzymes, gamma aminobutaric acid transaminase (GABA-T), succinic semialdehyde dehydrogenase and succinic semialdehyde reductase are involved in GABA shunt mechanism en route from glutamate to the tricaboxylic acid cycle (TCA) which can pave the way of GABA shunt action. The enzyme gamma aminobutaric acid transaminase (GABA-T) plays a key role in GABA shunt action by converting of GABA to succinic semialdehyde (SSA). In this study the protein sequence of γ-Aminobutyric acid transaminase of Brassica napus (Rape) is retrieved from UniProt protein database and analyzed GABA-T enzyme using different bioinformatics tools and servers to analyze the physiochemical properties, amino acid composition, conformational states and 3D structure. We found that our experimental protein sequence is very unstable and the graph of Local Quality Estimate shows that the sequence is porn to mutation and value of Z score is above two in comparison with non-redundant set of PDB structure. In addition, the phylogenetic tree reveals that GABA-T of Malus domestica Solanum lycopersicum , Oryza sativa , Arabidopsis thaliana and Brassica napus were evolved from a common ancestor gene.
Key words: GABA-T, TCA cycle, UniPort, bioinformatics, metabolism, transmission, stress
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