Title of article :
An Evolutionary Relationship between Stearoyl-CoA Desaturase (SCD) Protein Sequences Involved in Fatty Acid Metabolism
Author/Authors :
Salmani Izadi، Mohammad نويسنده Department of Animal Sciences, Faculty of Agriculture, Ferdowsi University of Mashhad, International Campus, Mashhad, Iran Salmani Izadi, Salmani Izadi , Naserian، Abbas Ali نويسنده Department of Animal Sciences, College of Agriculture, Ferdowsi University of Mashhad, Mashhad, Iran Naserian, Abbas Ali , Nasiri، Mohammad Reza نويسنده Department of Animal Sciences, Faculty of Agriculture, Ferdowsi University of Mashhad, International Campus, Mashhad, Iran Nasiri, Mohammad Reza , Majidzadeh Heravi، Reza نويسنده Department of Animal Sciences, Faculty of Agriculture, Ferdowsi University of Mashhad, International Campus, Mashhad, Iran Majidzadeh Heravi, Reza
Issue Information :
دوفصلنامه با شماره پیاپی 0 سال 2014
Pages :
6
From page :
1
To page :
6
Abstract :
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.
Journal title :
Reports of Biochemistry and Molecular Biology (RBMB)
Serial Year :
2014
Journal title :
Reports of Biochemistry and Molecular Biology (RBMB)
Record number :
1987117
Link To Document :
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