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OJBTM
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
Abstract
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.
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