Discussion

=**DISCUSSION:**=

After producing the phylogeny trees through bioinformatic identifications, it was observed that across species it seems that the MCAD enzyme has a higher conservation correlation than the nucleotide sequences. MCAD is a small protein of 386 residues, this is relative across the board for the selected species. The ACADM gene however diverges and varies to a greater margin, this is due to nonsense alterations/mutations that did not alter the function and structure of the enzyme. Next was protein structure analysis and w hen comparing the structures of wildtype MCAD and the most common variant K304E, we know it is a single base pair and the structure would not be much different. The %ID of the mutant is 99%. Examining the protein interaction of MCAD between human and mouse, it was observed that they have the same enzymes and mechanisms as each other in fatty acid beta oxidation. Reviewing the protein homologs list for // Homo sapiens //and comparing it with the species lists that was used here, half the list were found along the range of 780.0 - 840.0 bitscore indicting strong similarity / topology as the phylogenic trees had demonstrated earlier in MEGA7. The data suggests evolutionary correlation in fatty acid metabolism enzymes in mammals but the mutations are not. MCAD deficiency mutations are individual cases and not through evolution.

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