Back to Search
Start Over
On the specificity of dolichol kinase and DolPMan synthase towards isoprenoid alcohols of different chain length in rat liver microsomal membrane
- Source :
- International Journal of Biochemistry. 24:1151-1157
- Publication Year :
- 1992
- Publisher :
- Elsevier BV, 1992.
-
Abstract
- 1. A wide range of dolichols differing in the length of hydrocarbon chain (from 11 to 32 isoprene residues) were found to be phosphorylated in the presence of CTP in rat liver microsomes. 2. Fully unsaturated polyprenols of the same chain length as dolichols were poor substrates for dolichol kinase at low detergent (Nonidet P-40) concentration. At higher concentration of detergent, both dolichols and polyprenols were equally effective. 3. In the transfer of mannosyl residues from GDPMan, the dolichyl phosphates generated in rat liver microsomes were all good lipid acceptors, while fully unsaturated polyprenyl phosphates were not.
- Subjects :
- Stereochemistry
Mannosyltransferases
Biochemistry
Substrate Specificity
chemistry.chemical_compound
Sugar Alcohols
Polyisoprenyl Phosphates
Animals
Phosphorylation
Isoprene
Dolichol kinase
chemistry.chemical_classification
ATP synthase
biology
Phosphotransferases
Terpenoid
Rats
Phosphotransferases (Alcohol Group Acceptor)
Enzyme
Membrane
chemistry
Microsomes, Liver
Microsome
biology.protein
lipids (amino acids, peptides, and proteins)
Mannose
Subjects
Details
- ISSN :
- 0020711X
- Volume :
- 24
- Database :
- OpenAIRE
- Journal :
- International Journal of Biochemistry
- Accession number :
- edsair.doi.dedup.....560efb24ee92bbe4060b427edb3af941
- Full Text :
- https://doi.org/10.1016/0020-711x(92)90386-f