Isolation of Two Kinds of E. coli K-12 Mutants for Lysophospholipase L2: One with an Elevated Level of the Enzyme and the Other Defective in It1
- 1 July 1984
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 96 (1), 137-145
- https://doi.org/10.1093/oxfordjournals.jbchem.a134805
Abstract
Two kinds of E. coil K-12 mutants for lysophospholipase L 2 , (located in the inner membrane) were isolated, using an improved version of the colony autoradiographic method developed by Raetz; these were, 1) strains carrying an elevated level of the enzyme and 2) strains defective or temperature-sensitive in the enzyme. Characterization of the crude lysates of these mutants revealed that the differences of lysophospholipase L 2 activity are not due to the presence or absence of regulatory factors. Evidence was obtained, by using these mutants, that this lysophospholipase L 2 transfers the acyl group of 2-acyl lysophospholipid to phosphatidylglycerol, forming acyl phosphatidyiglycerol.Keywords
This publication has 2 references indexed in Scilit:
- Synthesis of Various Phospholipids from 2-Acyl Lysophospholipids by Escherichia Coli Extract1The Journal of Biochemistry, 1982
- Identification of acyl phosphatidylglycerol as a minor phospholipid of Pseudomonas BAL-31Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1976