DOI: 10.36347/sajb.2014.v02i04.009

Pages: 290-294

In order to know the evolutionary relationships of the LDH we have investigated and characterized (in silico) unnamed protein product of Mus musculus and described protein subunit structures, domain present as well as the phylogenetic relationships for mammalian unnamed protein product of Mus musculus. The unnamed protein product of Mus musculus show 99% similarity with L-lactate dehydrogenase A chain isoform 2 of Mus musculus at the amino acid level. The secondary structure of unnamed protein product of Mus musculus is single peptide & contains 43% helix, 19% beta sheet, 37%loop and contains lactate/malate dehydrogenase, NAD binding domain and lactate/malate dehydrogenase, alpha/beta C-terminal domain. Phylogenetic analysis of 22 subunits indicated that mammalian and rodents L-lactate dehydrogenase form distinct clades. These results indicate a relatively distant evolutionary relationship between mammals and rodents.