Open AccessProcessing of the Man 10 GlcNAc (M 10 ) oligosaccharide by α‐mannosidases from Candida albicans
Author(s) -
VázquezReyna Ana Bertha,
BalcázarOrozco Rosalía,
CalvoMéndez Carlos,
LópezRomero Everardo,
FloresCarreón Arturo
Publication year - 2000
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2000.tb09037.x
Subject(s) - candida albicans , oligosaccharide , mannose , mannosidase , hydrolysis , biology , corpus albicans , biochemistry , glycan , stereochemistry , chemistry , glycoprotein , microbiology and biotechnology
The hydrolysis of Man 10 GlcNAc (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 .