Evaluación in-silico de la enzima α 1,6 - manosiltransferasa de la levadura Komagataella phaffii y cuatro de sus mutantes

Abstract

This work addressed two important aspects of the α 1,6-mannosyltransferase protein. One of them is the proposed mechanism of action of this enzyme, based on the associations with functionally similar proteins described as Leloir glycosyltransferases. The proposal of the enzymatic mechanism is of considerable importance because it has not been described at present, and that, due to the type of enzyme, it is a target of interest at the biotechnological level for the modification of glycosylation pathways in eukaryotes. The second relevant aspect of the work is the relationship found between this protein and other homologous glycosyltransferases that conserve the D-x-D motif, previously described as the active site of these proteins. In this work, it was also possible to identify a highly conserved motif in the analyzed sequences (GG-x-Y), which precedes the D-x-D motif. Additionally, other conserved motifs are found that suggest the functional specialization of the protein, in the different taxonomic groups. This finding is important for the study of the function of proteins classified as glycosyltransferases found in prokaryotes and that could be important targets for the invasion process of pathogenic organisms.