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Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
Published on: May 26, 2011
Characterization of trehalase in Rhodotorula rubra
J J Mansure1, J T Silva, A D Panek
1Depart. de Bioquímica, Universidade Federal do Rio de Janeiro, Brasil.
Abstract:
Trehalase activity in Rhodotorula rubra was found to be bound to the particulate fraction of a cell-free extract in contrast with the soluble trehalase activity of Saccharomyces cerevisiae. The enzyme was strongly repressed by glucose and derepressed during growth on maltose, trehalose and glycerol. This increase in activity was due to a "de novo" synthesis as seen by inhibition with cycloheximide, a mechanism not described for Saccharomyces cerevisiae. Catabolite inactivation by addition of glucose was also demonstrated. This particulate enzyme does not respond to activation by the cAMP-dependent protein kinase.
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