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An evolutionary relationship between Stearoyl-CoA Desaturase (SCD) protein sequences involved in fatty acid metabolism.
Salmani Izadi, Mohammad; Naserian, Abbas Ali; Nasiri, Mohammad Reza; Majidzadeh Heravi, Reza.
Afiliación
  • Salmani Izadi M; Department of Animal Sciences, Faculty of Agriculture, Ferdowsi University of Mashhad, International Campus, Mashhad, Iran.
  • Naserian AA; Department of Animal Sciences, College of Agriculture, Ferdowsi University of Mashhad, Mashhad, Iran.
  • Nasiri MR; Department of Animal Sciences, College of Agriculture, Ferdowsi University of Mashhad, Mashhad, Iran.
  • Majidzadeh Heravi R; Department of Animal Sciences, College of Agriculture, Ferdowsi University of Mashhad, Mashhad, Iran.
Rep Biochem Mol Biol ; 3(1): 1-6, 2014 Oct.
Article en En | MEDLINE | ID: mdl-26989730
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.
Palabras clave

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Rep Biochem Mol Biol Año: 2014 Tipo del documento: Article País de afiliación: Irán

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Rep Biochem Mol Biol Año: 2014 Tipo del documento: Article País de afiliación: Irán