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Online Journal of Bioinformatics ©
Volume 13(2):184-191, 2012
Amino acid sequence analysis of glutamate dehydrogenase from different source organisms
Vivek Dhar Dwivedi1 (MSc), Sarad Kumar Mishra2 (PhD).
¹Department of Bioinformatics, UCST, Dehradun – ²Department of Biotechnology, DDU University, Gorakhpur. India
Dwivedi VD, Mishra SK., Amino acid sequence analysis of glutamate dehydrogenase from different source organisms, Onl J Bioinform., 13(2):184-191, 2012. Glutamate dehydrogenase (GLDH) is present in most microbes and mitochondria of eukaryotes to convert glutamate to α-ketoglutarate and vice versa. Thirty full-length amino acid sequences of GLDH from fungi, plants and animals were subjected to multiple sequence alignment (MSA), pattern and domain identification for individual amino acid composition and phylogenetic tree construction. MSA revealed 6 identical glycine, 2 glutamic acid and asparagine, and 1 aspartic acid, tyrosine, alanine, valine, serine and leucine residues in all species studied. Five identical glycine, 2 glutamic acid and proline, and 1 arginine and alanine residues were found in fungal and plants sources. Five identical glycine, 3 glutamic acid, 2 praline, 1 threonine, arginine, alanine, asparagine, 1 tryptophan and leucine residues occurred in plant and fungi. Five amino acid residue patterns of different length occurred in plant and animal GLDH. Two major sequence clusters were used to construct plant and animal and fungal philogenetic trees. The average frequency of amino acid glycine was found to be 10.2% which was high compared with other amino acids. Ten motifs unique for their group were identified.
Keywords: GLDH. MSA. Phylogenetic analysis. Conserved regions. Motifs. Domains. Amino acid composition.