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. © 2005 Federation of European Microbiological Societies. Published by Elsevier B.V. All rights reserved.
Arroyo-Flores, B. L., Calvo-Méndez, C., Flores-Carreón, A., & López-Romero, E. (2005). Biosynthesis of glycoproteins in the pathogenic fungus Candida albicans: Activation of dolichol phosphate mannose synthase by cAMP-mediated protein phosphorylation. FEMS Immunology and Medical Microbiology, 45(3), 429–434. https://doi.org/10.1016/j.femsim.2005.05.016