Characterizing the polymorphism K232A of the diacylglycerol-acyltransferase-1 lipogenic enzyme of bovine Bos taurus using in silico comparative protein prediction analyses

The diacylglycerol-acyltransferase-1 lipogenic enzyme (DGAT1) is a multi-pass transmembrane protein that catalyzes the conversion of diacylglycerol and fatty acyl CoA to triacylglycerol or retinol. The lysine to alanine polymorphism in the DGAT1 (K232A) is directly associated with 50% of the genetic...

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Published inBrazilian journal of biology Vol. 78; no. 2; pp. 389 - 390
Main Authors Costa, F F P, Nogueira, J F, Gouveia, J J S, Gabriel, J E
Format Journal Article
LanguageEnglish
Published Brazil Instituto Internacional de Ecologia 01.05.2018
Subjects
Acyltransferase
Alanine
BIOLOGY
Bos taurus
Diglycerides
Enzymes
Fatty acid composition
Fatty acids
Gene polymorphism
Genetic diversity
Ligands
Lysine
Metabolism
Milk
Mutation
Polymorphism
Proteins
Structure-function relationships
Triglycerides
Vitamin A
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Summary:The diacylglycerol-acyltransferase-1 lipogenic enzyme (DGAT1) is a multi-pass transmembrane protein that catalyzes the conversion of diacylglycerol and fatty acyl CoA to triacylglycerol or retinol. The lysine to alanine polymorphism in the DGAT1 (K232A) is directly associated with 50% of the genetic variation in milk-fat percentage and exerts a strong effect on milk fatty acid composition. Here, Costa et al detail a study that aimed to predict potential structural and functional effects of the polymorphism K232A on DGAT1 protein sequences of bovine taurus using in silico comparative modelling prediction analyses.
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content type line 23
ISSN:1519-6984
1678-4375
1678-4375
DOI:10.1590/1519-6984.167755