Heteronuclear NMR studies of 13C-labeled yeast cell wall beta-glucan oligosaccharides.

Yu L, Goldman R, Sullivan P, Walker GF, Fesik SW
J Biomol NMR. 1993 3 (4): 429-41

PMID: 8400831 · DOI:10.1007/bf00176009

The structures of uniformly 13C-labeled beta-glucan octa- and undeca-oligosaccharides enzymatically prepared by the yeast cell wall glucanosyl transferase of Candida albicans were characterized by using a combination of HCCH-COSY, HCCH-TOCSY, and HMBC experiments. The oligosaccharide structures indicate that the cell wall glucanosyl transferase cleaves two glucosyl units from the reducing end of the initial linear beta(1-->3) penta-oligosaccharide and subsequently transfers the remainder to another oligosaccharide at the nonreducing end via a beta(1-->6) linkage. These results indicate that the combined action of cell wall glucanase and glucanosyl transferase activities could not only introduce intrachain beta(1-->6) linkages within a single glucan strand, but also result in cross-linking of two initially separate glucan strands with concurrent introduction of intrachain beta(1-->6) linkages. Since isolated fungal membranes only synthesize linear beta(1-->3) glucan strands, wall-associated enzymes probably participate in the assembly of the final wall glucan structure during cell growth and division.

MeSH Terms (10)

Candida albicans Carbohydrate Conformation Carbohydrate Sequence Cell Wall Glucans Glucosyltransferases Magnetic Resonance Spectroscopy Molecular Sequence Data Molecular Structure Oligosaccharides

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