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Enzyme affinity in the acylation of lysophosphatidylcholine

1977; Elsevier BV; Volume: 489; Issue: 1 Linguagem: Inglês

10.1016/0005-2760(77)90233-8

1879-145X

Benjamin Wittels, Stuart Hurlbert,

Enzyme Catalysis and Immobilization

Analogues of 1-palmitoyl-sn-glycero-3-phosphorylcholine were used to ascertain the respective roles of the 1-palmitoyl-sn-glycero and choline groups in binding this substrate to the transferase catalyzing the acylation reaction. 1-Palmitoyl-sn-glycero-3-phosphorylhomocholine proved to be an effective competitive inhibitor whereas 1-palmitoyl-2-deoxyglycero-3-phosphorylcholine was totally ineffective. The data support the view that the 1-palmitoyl-sn-glycero group plays the major role in determining enzyme affinity whereas the choline group functions primarily in the subsequent steps of the acylation reaction.