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GalT encodes for the protein galactosyltransferase which catalyzes the transfer of a galactose sugar to an acceptor, forming a glycosidic bond. [5] GalK encodes for a kinase that phosphorylates α-D-galactose to galactose 1-phosphate. [6] Lastly, galM catalyzes the conversion of β-D-galactose to α-D-galactose as the first step in galactose ...
The two proteins responsible for inhibiting transcription from the gal regulon are GalR and GalS (Figure 4) (11). GalR and GalS have very similar primary structure sequences, and have the same binding sites on the operator (11). In the presence of D-galactose, GalR and GalS are inhibited since they are repressors (5, 11).
galactose. Galactosyltransferase is a type of glycosyltransferase which catalyzes the transfer of galactose. An example is B-N-acetylglucosaminyl-glycopeptide b-1,4-galactosyltransferase. The biosynthesis of disaccharides, oligosaccharides and polysaccharides involves the action of hundreds of different glycosyltransferases.
Uridine diphosphate (UDP)-galactose is relevant in glycolysis. UDP-galactose is the activated form of Gal, a crucial monosaccharide building block for human milk oligosaccharide (HMO). [2]
Secondary structure [4] [5] α-Helices Cylindrical spiral ribbons, with ribbon plane approximately following plane of peptides. β-Strands Arrows with thickness, about one-quarter as thick as they are wide, showing direction and twist of the strand from amino to carboxy end. β-sheets are seen as unified because neighboring strands twist in unison.
The Gal4 transcription factor is a positive regulator of gene expression of galactose-induced genes. [1] This protein represents a large fungal family of transcription factors, Gal4 family, which includes over 50 members in the yeast Saccharomyces cerevisiae e.g. Oaf1, Pip2, Pdr1, Pdr3, Leu3. [2]
In molecular biology, the galactose binding lectin domain is a protein domain. It is found in many proteins including the lectin purified from sea urchin ( Anthocidaris crassispina ) eggs, SUEL. This lectin exists as a disulfide -linked homodimer of two subunits; the dimeric form is essential for hemagglutination activity. [ 1 ]
The type of galectin-8 that is expressed is dependent on the tissue. [4] Galectin-9 has three different isoforms which differ in the length of the linker region. [4] The galectin carbohydrate recognition domain (CRD) is constructed from beta-sheet of about 135 amino acids. The two sheets are slightly bent with 6 strands forming the concave side ...