Characterization of undecaprenol kinase from Lactobacillus plantarum.
A membrane-bound undecaprenol kinase from Lactobacillus has been identified by observing the ATP-dependent phosphorylation of [14C]undercaprenol. The product of this reaction was shown to be [14C]undecaprenyl monophosphate by comparison of its chromatographic mobilities with authentic undecaprenyl monophosphate. It was shown that 32P from [gamma-32P]ATP was incorporated into undecaprenyl monophosphate. The kinase was partially solubilized by a variety of methods utilizing Triton X-100. Both the membrane-associated and solubilized enzymes required Mg2+, Triton X-100 and dimethylsulfoxide for activity. The enzyme preferentially phosphorylated the C34, C50 AND C 55 polyprenols. Geranylgeraniol (C20) and dolichol (C100), however, were utilized only 6% and 13% as well as undecaprenol, respectively. Despite the 8-fold difference in apparent V values, the apparent Km values for dolichol and undecaprenol were both 14 microM. The apparent Km for the nucleotide cosubstrate, ATP, was 2 mM. No other nucleoside triphosphate could substitute for ATP.
D004224:Diterpenes / Q000378:metabolism; D004286:Dolichols / Q000378:metabolism; D007700:Kinetics; D007778:Lactobacillus / Q000201:enzymology*; D010770:Phosphotransferases / Q000302:isolation & purification*; D017853:Phosphotransferases (Alcohol Group Acceptor); D013379:Substrate Specificity; D013729:Terpenes
D004224:Diterpenes; D004286:Dolichols; D013729:Terpenes; D010770:Phosphotransferases; D017853:Phosphotransferases (Alcohol Group Acceptor); C021454:undecaprenol kinase