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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 (M.Sc.) 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, Online 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.