Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.4.1.18 (branching enzyme)
 628 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The molecular mechanisms regulating hemicelluloses and pectin biosynthesis are poorly understood. An important question in this regard is how glycosyltransferases are oriented in the Golgi cisternae, and how nucleotide sugars are made available for the synthesis of the polymers. Here we show that the branching enzyme xyloglucan alpha,1-2 fucosyltransferase (XG-FucTase) from growing pea (Pisum sativum) epicotyls was latent and protected against proteolytic inactivation on intact, right-side-in pea stem Golgi vesicles. Moreover, much of the XG-FucTase activity was membrane associated. These data indicate that XG-FucTase is a membrane-bound luminal enzyme. GDP-Fuc uptake studies demonstrated that GDP-Fuc was taken up into Golgi vesicles in a protein-mediated process, and that this uptake was not competed by UDP-Glc, suggesting that a specific GDP-Fuc transporter is involved in xyloglucan biosynthesis. Once in the lumen, Fuc was transferred onto endogenous acceptors, including xyloglucan. GDPase activity was detected in the lumen of the vesicles, suggesting than the GDP produced upon transfer of Fuc was hydrolyzed to GMP and inorganic phosphate. We suggest than the GDP-Fuc transporter and GDPase may be regulators of xyloglucan fucosylation in the Golgi apparatus from pea epicotyls.
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PMID:GDP-fucose uptake into the Golgi apparatus during xyloglucan biosynthesis requires the activity of a transporter-like protein other than the UDP-glucose transporter. 1071 51

Transfection of sense cDNA of N-acetylglucosaminyltransferase V (GnTV) into H7721 human hepatocellular carcinoma cells resulted in the decreased expression of surface sialyl Lewis X (SLe(x)), a sialylated fucose-containing antigen. The enzymatic mechanisms were speculated to be the concomitantly decreased expression of alpha1,3-fucosyltransferase (FucT)-III, -VI, -VII and the branching enzyme of O-glycans, core 2-beta1,6-N-acetylglucosaminyltransferase (C2GnT)-I, -II. These two glycosyltransferase families were suggested to be the key enzymes in the synthesis of SLe(x). The expression of alpha2,3-sialyltransferase (ST3)-IV, but not ST3-I, -II and -III was elevated by sense GnTV. However, it did not cause the increase of SLe(x) synthesis. Transfection of antisense GnTV into H7721 cells showed entirely opposite effects on the expression of above-mentioned SLe(x) and glycosyltransferases as the sense GnTV.
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PMID:Effect of N-acetylglucosaminyltransferase V on the expressions of other glycosyltransferases. 1504 7