Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9277960 | FEMS Immunology and Medical Microbiology | 2005 | 6 Pages |
Abstract
Following incubation with ATP and a cAMP-dependent protein kinase under optimal conditions of lipid acceptor, phospholipid and metal ion requirements, the transfer activity of partially purified dolichol phosphate mannose synthase (DPMS) increased about 60% and this activation correlated with a 50% increase in Vmax with no alteration in the apparent Km for GDP-Manose. Phosphorylation with [γ-32P]ATP resulted in the labeling of several polypeptides, one of which exhibited the molecular weight of the enzyme (30 kDa) and was also recognized using a specific anti-DPMS monoclonal antibody. This and the fact that the phosphate label could be removed by an alkaline phosphatase indicate that Candida DPMS may be regulated by phosphorylation-dephosphorylation, a mechanism that has been proposed for the enzyme in other organisms.
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Authors
Blanca L. Arroyo-Flores, Carlos Calvo-Méndez, Arturo Flores-Carreón, Everardo López-Romero,