Mechanism of inactivation of hexokinase PII of Saccharomyces cerevisiae by D-xylose.
The mechanism of inactivation of hexokinase PII of Saccharomyces cerevisiae by D-xylose was characterized. Inactivation was dependent on the presence of MgATP and was irreversible. Inactivation involved phosphorylation of the protein. Observation of the carbon catabolite repression of selected enzymes showed that invertase and maltase synthesis were not repressed when hexokinase PII was phosphorylated.
Fernández
R
R
Departamento Interfacultativo de Bioquimica, Facultad de Medicina, Universidad de Oviedo, Spain.
Herrero
P
P
Fernández
M T
MT
Moreno
F
F
D000255:Adenosine Triphosphate / Q000502:physiology; D004794:Enzyme Repression / Q000187:drug effects; D006593:Hexokinase / Q000037:antagonists & inhibitors*; D007527:Isoenzymes / Q000037:antagonists & inhibitors*; D010710:Phosphates / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000187:drug effects / Q000201:enzymology*; D014994:Xylose / Q000494:pharmacology*
D007527:Isoenzymes; D010710:Phosphates; D000255:Adenosine Triphosphate; D014994:Xylose; D006593:Hexokinase