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  • Title: Enzyme affinity in the acylation of lysophosphatidylcholine.
    Author: Wittels B, Hurlbert S.
    Journal: Biochim Biophys Acta; 1977 Oct 24; 489(1):72-8. PubMed ID: 911874.
    Abstract:
    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.
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