Multiple Mannosyl Transferases in Cryptococcus laurentii
نویسندگان
چکیده
منابع مشابه
Mannosyl transfer in Cryptococcus laurentii.
A particle-bound enzyme from the fungus imperfectus Cryfitococcus taurentii var. flavescens (NRRL Y-1401) mediates transfer of mannosyl units from GDP-mannose to endogenous primer. The enzyme requires divalent cations for activity. The pH optimum is ‘7.5 and the apparent K, for GDP-mannose is 0.14 mbr. A polysaccharide fraction that is associated with the enzyme was found to be similar to a pol...
متن کاملHeteroglycan synthesis in Cryptococcus laurentii.
An enzyme preparation from Cryptococcus laurentii catalyzes the transfer of glycosyl units from sugar nucleotides to exogenous acceptor resulting in the stepwise synthesis of a heteroglycan with the following structure: Z-O-a-n-mannosyl6-O-oc-D-mannosyl-3-~-~-D-mannosyl-(2 -0 -0 -D -xylosyl-) D-mannose. The same enzyme preparation transfers D-[‘T]mannosyl from GDP [WJmannose to an endogenous gl...
متن کاملMannosyl Transfer in Cryptococcus Zuurentii*
A particle-bound enzyme from the fungus imperfectus Cryfitococcus taurentii var. flavescens (NRRL Y-1401) mediates transfer of mannosyl units from GDP-mannose to endogenous primer. The enzyme requires divalent cations for activity. The pH optimum is ‘7.5 and the apparent K, for GDP-mannose is 0.14 mbr. A polysaccharide fraction that is associated with the enzyme was found to be similar to a pol...
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Ten Cryptococcus strains were screened for phytase activity, of which the Cryptococcus laurentii ABO 510 strain showed the highest level of activity. The cell wall-associated enzyme displayed temperature and pH optima of 62 degrees C and 5.0, respectively. The enzyme was thermostable at 70 degrees C, with a loss of 40% of its original activity after 3 h. The enzyme was active on a broad range o...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1971
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)77206-8