Lipid activation of undecaprenol kinase from Lactobacillus plantarum

Biochim Biophys Acta. 1980 Jul 14;619(1):76-89. doi: 10.1016/0005-2760(80)90244-1.

Abstract

Extraction of membranes of Lactobacillus plantarum with Triton X-100/glycerol solubilized up to 80% of the undecaprenol kinase activity. Fractionation of the extract by gel chromatography separated endogenous phospholipid from the enzyme but simultaneously inactivated the enzyme. The kinase was reactivated by reconstitution with various synthetic phosphatidylcholines and purified L. plantarum phospholipids. Ditetradecanoylphosphatidylcholine and lysylphosphatidylglycerol were the best activators. Furthermore, the optimal environment for enzyme stimulation was provided by different defined molar ratios of Triton X-100/phospholipid. The ratios for the phospholipids tested ranged from 1.25 to 6.3. Similar substrate specificity and kinetic constants were observed for both the solubilized and reconstituted enzymes suggesting that no fundamental changes in the enzyme activity occurred during the delipidation-reconstitution process.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Enzyme Activation
  • Lactobacillus / enzymology*
  • Phosphatidylcholines / pharmacology*
  • Phosphatidylglycerols / metabolism
  • Phospholipids / pharmacology*
  • Phosphotransferases (Alcohol Group Acceptor)*
  • Phosphotransferases / isolation & purification*
  • Phosphotransferases / metabolism
  • Substrate Specificity
  • Terpenes / isolation & purification

Substances

  • Phosphatidylcholines
  • Phosphatidylglycerols
  • Phospholipids
  • Terpenes
  • Phosphotransferases
  • Phosphotransferases (Alcohol Group Acceptor)
  • undecaprenol kinase