Glucans biosynthesis

Li X, Burton R.A., Harvey A.X., Hrmova M., Wardak A.Z., Stone B.A., and Fincher G.B. 2003. Biochemical evidence linking a putative callose synthase gene with (1 3)-P-D-glucan biosynthesis in barley. Plant Mol Biol 53 213-225. 

Kontani, M., Sakagami. Y, and Mammo, S. (1994) First p-l,6-glucan biosynthesis inhibitor, bisvertinolone isolated from fungus, Acremonium strictum and its absolute stereochemistry. Tetrahedron Lett., 35,2577-2580. 

PF had been proposed as the terminal complex (23) and associated pores were reported on the outer membrane EF (24). Due to their proximity to the site of cellulose ribbon extrusion from the cell surface, these structures were assumed to be responsible for cellulose synthesis. A model was advanced in which cellulose synthase was localized on the outer membrane, which invoked adhesion sites between the outer and plasma membranes as a mechanism to explain the transfer of uridine-diphosphoryl-glucose (UDPG) from the cytoplasm to the cellulose synthases (25,26). However, when the outer and plasma membranes of Acetobacter were isolated separately by density-gradient centrifugation, the cellulose synthase activity was localized only in the plasma membrane fraction (27). Therefore, the linear structures observed on the Acetobacter outer membrane, while they may be associated in some manner with cellulose biosynthesis, are probably not the cellulose synthase terminal complexes. Since no ultrastructural evidence for adhesion sites between the outer and plasma membranes has been presented, a thorough investigation of the mechanism of / (1-4) glucan chain translocation from the cytoplasmic membrane to the outer membrane in Acetobacter xylinvm is now in order. 

Functionally, starch can be considered as a polysaccharide synthesized in a manner permitting its efficient degradation. Hence, biosynthesis of the starch granule is a delicate balance between efficient packing of the glucan chains and the possibility of breaking these structures at degradation. To complete this enzymatically catalyzed process in the potato tuber, a multitude of different enzyme activities are required. 

A characteristic feature of the SuSy isoforms is a conserved phosphorylated serine residue near the N-terminus [8-10]. In-vivo studies have demonstrated that phosphorylation and dephosphorylation direct the distribution of SuSy isoforms in the plant cell [10-12]. The soluble phosphorylated SuSy interacts with the actin cytoskeleton in the cytoplasm [13], and the dephosphorylated SuSy isoforms are targeted to the cell membrane to form complexes with other enzymes, e.g., glucan synthase, catalyzing cellulose biosynthesis from sucrose [4, 10, 14]. In this respect, recent studies on the dephosphorylated enzymes by cloning and expression of SMS genes in E. coli have shown differences in some biochemical features when compared to the enzymes isolated from the corresponding plant material. Recom-... 

---