an evolutionary relationship between stearoyl-coa desaturase (scd) protein sequences involved in fatty acid metabolism

background: stearoyl-coa desaturase (scd) is a key enzyme that converts saturated fatty acids (sfas) to monounsaturated fatty acids (mufas) in fat biosynthesis. despite being crucial for interpreting scds’ roles across species, the evolutionary relationship of scd proteins across species has yet to be elucidated. this study aims to present this evolutionary relationship based on amino acid sequences. methods: using multiple sequence alignment (msa) and phylogenetic construction methods, a hypothetical evolutionary relationship was generated between the stearoyl-coa desaturase (scd) protein sequences between 18 different species. results: scd protein sequences from homo sapiens, pan troglodytes (chimpanzee), and pongo abelii (orangutan) have the lowest genetic distances of 0.006 of the 18 species studied. capra hircus (goat) and ovis aries (sheep) had the next lowest genetic distance of 0.023. these farm animals are 99.987% identical at the amino acid level. conclusions: the scd proteins are conserved in these 18 species, and their evolutionary relationships are similar.