Abstract
The hydrolysis of Man 10GlcNAc (M 10) by purified α-mannosidases and its further processing by a mixed membrane preparation from Candida albicans were studied. Incubation of the oligosaccharide with purified α-mannosidases I (E-I) or II (E-II) from C. albicans released 1 and 2 mol of mannose per mol of M 10, respectively. This treatment converted M 10 into an acceptor substrate of further mannose residues from GDP-Man as catalyzed by membrane-bound mannosyltransferases. Elongation of E-I- or E-II-trimmed M 10 yielded a low molecular mass product (14–17 mannose residues added), and in the case of E-II, a minor amount of an additional product of a higher molecular mass. Our results indicate that purified α-mannosidases participate in N-glycan processing in C. albicans.
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