Characterization of trehalase in Rhodotorula rubra.
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.
Mansure
J J
JJ
Depart. de Bioquímica, Universidade Federal do Rio de Janeiro, Brasil.
Silva
J T
JT
Panek
A D
AD
D003513:Cycloheximide / Q000494:pharmacology; D004789:Enzyme Activation / Q000187:drug effects; D005947:Glucose / Q000494:pharmacology; D005990:Glycerol / Q000494:pharmacology; D006358:Hot Temperature; D008320:Maltose / Q000494:pharmacology; D012248:Rhodotorula / Q000201:enzymology*; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D014198:Trehalase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D014199:Trehalose / Q000494:pharmacology
D008320:Maltose; D003513:Cycloheximide; D014199:Trehalose; D014198:Trehalase; D005947:Glucose; D005990:Glycerol