Processing of the Man(10)GlcNAc (M(10)) oligosaccharide by alpha-mannosidases from Candida albicans.
The hydrolysis of Man(10)GlcNAc (M(10)) by purified alpha-mannosidases and its further processing by a mixed membrane preparation from Candida albicans were studied. Incubation of the oligosaccharide with purified alpha-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 alpha-mannosidases participate in N-glycan processing in C. albicans.
Vázquez-Reyna
A B
AB
Instituto de Investigación en Biología Experimental, Facultad de Química, Universidad Autónoma de Guanajuato, Apartado postal 187, Guanajuato, Mexico.
Balcázar-Orozco
R
R
Calvo-Méndez
C
C
López-Romero
E
E
Flores-Carreón
A
A
D002176:Candida albicans / Q000201:enzymology* / Q000254:growth & development; D006868:Hydrolysis; D008361:Mannosidases / Q000378:metabolism*; D008562:Membrane Glycoproteins / Q000378:metabolism; D009844:Oligosaccharides / Q000378:metabolism*
D008562:Membrane Glycoproteins; D009844:Oligosaccharides; C025363:mannoproteins; D008361:Mannosidases