Characterization of polyisoprenyl phosphate phosphatase activity in rat liver.

Abstract:

:The polyisoprenyl phosphate dephosphorylating activity of rat liver has been investigated with regard to substrate specificity, subcellular distribution, and transmembrane orientation. Total liver microsomes were employed as a source of enzymatic activity against a variety of 32P-labeled substrates. Susceptibility to dephosphorylation followed the order solanesyl phosphate greater than alpha-cis-polyprenyl 19-phosphate = alpha-trans-polyprenyl 19-phosphate = dihydrosolanesyl phosphate greater than (S)-dolichyl 19-phosphate = (R)-dolichyl 19-phosphate = (R,S)-dolichyl 11-phosphate. There appeared to be no major effect of chain length from 11 to 20 isoprenes. Data obtained from inhibition studies using solanesyl [32P]phosphate as substrate were consistent with the substrate specificity studies and suggested that a single activity is responsible. With dolichyl [32P]phosphate as substrate, the phosphatase specific activity of the subcellular fractions prepared from rat liver was found to follow the sequence Golgi = smooth endoplasmic reticulum greater than plasma membrane greater than lysosomes = rough endoplasmic reticulum greater than nuclei greater than mitochondria. Transmembrane topography studies, using enzyme latency as a criterion, were consistent with an orientation of the active site facing the cytoplasm.

journal_name

Arch Biochem Biophys

authors

Keller RK,Adair WL Jr,Cafmeyer N,Simion FA,Fleischer B,Fleischer S

doi

10.1016/0003-9861(86)90576-x

subject

Has Abstract

pub_date

1986-08-15 00:00:00

pages

207-14

issue

1

eissn

0003-9861

issn

1096-0384

pii

0003-9861(86)90576-X

journal_volume

249

pub_type

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