A differentiation-dependent polyisoprenol kinase in Dictyostelium discoideum

Crude membrane fractions of Dictyostelium discoideum show the capacity to synthesize (1--3H)dolicholphosphate from (1--3H)dolichol. Formation of dolicholphosphate increased continuously over the first 15 min. The reaction rate was nearly linear with respect to the dolichol content up to 150 microM....

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Bibliographic Details
Published in:Molecular and cellular biochemistry 1982-10, Vol.48 (3), p.183-189
Main Authors: Rössler, H H, Zimpfer, A, Risse, H J
Format: Article
Language:English
Subjects:
Cell Differentiation
Cytidine Triphosphate - metabolism
Dictyostelium - cytology
Dictyostelium - enzymology
Dictyostelium discoideum
Dolichol Phosphates - biosynthesis
Mannose - metabolism
Microsomes - metabolism
Phosphotransferases (Alcohol Group Acceptor)
Phosphotransferases - metabolism
polyisoprenol kinase
Substrate Specificity
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Summary:Crude membrane fractions of Dictyostelium discoideum show the capacity to synthesize (1--3H)dolicholphosphate from (1--3H)dolichol. Formation of dolicholphosphate increased continuously over the first 15 min. The reaction rate was nearly linear with respect to the dolichol content up to 150 microM. The phosphate donor for the reaction is CTP. The optimum concentration of CTP is about 0,75 mM. The reaction is dependent on divalent metal ions, magnesium being more effective than calcium or manganese. The activity of the polyisoprenol kinase depends on the course of the early development. Maximum enzyme activities are present 4--6 h after the induction of the differentiation.
ISSN:0300-8177
DOI:10.1007/BF00421227