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Substrate selectivity of acyl-CoA:lysolecithin acyltransferase from rabbit lung

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Summary

The influence of both polar head and acyl chain of lysophospholipid on the activity of partially purified acyl-CoA:lysolecithin acyltransferase from rabbit lung was studied. It was concluded that the presence of methyl groups on the nitrogen of the base was essential for recognition of lysophospholipid as substrate by the enzyme. With respect to the acyl chain length and saturation, the activity followed the order:

$$16:0 \simeq 18:1 > 14:0 > > > 18:0 \simeq 12:0.$$

Also, the effect on the activity of the acyl chain on acyl-CoA was studied. The activity showed great selectivity for saturated acyl-CoAs. The activity with polyunsaturated fatty acids was very low and in the case of arachidonoyl-CoA was almost negligible.

The comparison between crude microsomal preparations and partially purified preparations allowed to suggest that it could exist two different acyl-CoA:lysolecithin acyltransferases differing in their selectivity towards saturated and unsaturated fatty acids.

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Abbreviations

LPC:

lysophosphatidylcholine

LPDME:

lysophosphatidyldimethylethanolamine

LPE:

lysophosphatidylethanolamine

PC:

phosphatidylcholine

PDME:

phosphatidyldimethylethanolamine

PE:

phosphatidylethanolamine.

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Authors and Affiliations

  1. Departamento de Bioquimica. Facultad de Ciencias Quimicas, Universidad Complutense, 28040, Madrid, Spain

    Pilar Estrada, Carmen Acebal & Roberto Arche

Authors
  1. Pilar Estrada
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  2. Carmen Acebal
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  3. Roberto Arche
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Estrada, P., Acebal, C. & Arche, R. Substrate selectivity of acyl-CoA:lysolecithin acyltransferase from rabbit lung. Mol Cell Biochem 69, 49–54 (1985). https://doi.org/10.1007/BF00225926

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  • DOI: https://doi.org/10.1007/BF00225926

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