PMID:2828054
| Citation |
Russ, E, Kaiser, U and Sandermann, H Jr (1988) Lipid-dependent membrane enzymes. Purification to homogeneity and further characterization of diacylglycerol kinase from Escherichia coli. Eur. J. Biochem. 171:335-42 |
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| Abstract |
1. Diacylglycerol kinase apoprotein was purified from membranes of Escherichia coli K12 by a six-step procedure that included HPLC. The proposed assignment of the enzyme to the dgkA gene [Lightner et al. (1983) J. Biol. Chem. 258, 10856-10861] could be supported by molecular mass determination (approximately 14 kDa), N-terminal sequencing (Met-Ala-Asn), cyanogen bromide fragmentation and amino acid analysis. As predicted, proline was absent. 2. The membrane-associated as well as the butan-1-ol-dissolved enzyme survived heating to 100 degrees C. 3. Alkylglycoside detergents were found to constitute an additional class of lipid activators. 4. The enzyme apoprotein in a non-activating substrate/detergent solution was capable of autocatalytic self-activation which was attributed to a novel feedback activation mechanism involving phosphatidic acid (diacylglycerol 3-phosphate). |
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| Keywords |
Amino Acid Sequence; Amino Acids/analysis; Cell Membrane/enzymology; Cyanogen Bromide/diagnostic use; Detergents/pharmacology; Diacylglycerol Kinase; Enzyme Activation; Escherichia coli/enzymology; Hot Temperature; Peptide Fragments/analysis; Phosphotransferases/isolation & purification; Phosphotransferases/metabolism |
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