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• W2028321350 abstract "The kinetic constants of the transphosphatidylation reaction between a phospholipid (phos phatidylcholine) and a nucleophile (3-dimethylamino-1-propanol), catalyzed by phospholipase D from Streptomyces PMF in a water-ethyl acetate emulsion system, have been determined. The Km of the phospholipid was 16.6mM, the Km for the nucleophile 1.3 M and the catalytic constant 1.5 × 105min−1 at pH 5.6 and 25°C. The kinetic pattern was consistent with a ping-pong mechanism modified by a hydrolytic branch. Furthermore, by studying the intermediate partitioning between competing acceptors, it was found that transphosphatidylation hydrolysis of different phospholipids occurred through the formation of a common intermediate. These results support the view that phospholipase D-catalyzed reactions take place through the formation, as the first step, of a phosphatidyl-enzyme intermediate. Finally, experiments carried out at different concentrations of phospholipase D showed the phenomenon of inter-facial saturation by the enzyme, thus suggesting that only the phospholipase D located at the interface of the water-organic solvent emulsion was active." @default.
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• W2028321350 date "1997-01-01" @default.
• W2028321350 modified "2023-10-14" @default.
• W2028321350 title "On the Kinetic Mechanism of Phospholipase D from<i>Streptomyces</i>SP. In an Emulsion System" @default.
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• W2028321350 doi "https://doi.org/10.3109/10242429709003193" @default.
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