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Evidence for the reversibility of the acyl-CoA:lysophosphatidylcholine acyltransferase in microsomal preparations from developing safflower (Carthamus tinctorius L.) cotyledons and rat liver
Open accessAbstract
Acyl exchange between acyl-CoA and position 2 of sn-phosphatidylcholine occurs in the microsomal preparations of developing safflower cotyledons. Evidence is presented to show that the acyl exchange is catalysed by the combined back and forward reactions of an acyl-CoA:lysophosphatidylcholine acyltransferase (EC 2.3.1.23). The back reaction of the enzyme was demonstrated by the stimulation of the acyl exchange with free CoA and by the observation that the added CoA was acylated with acyl groups from position 2 of sn-phosphatidylcholine. Re-acylation of the, endogenously produced, lysophosphatidylcholine with added acyl-CoA occurred with the same specificity as that observed with added palmitoyl lysophosphatidylcholine. A similar acyl exchange, catalysed by an acyl-CoA:lysophosphatidylcholine acyltransferase, occurred in microsomal preparations of rat liver. The enzyme from safflower had a high specificity for oleate and linoleate, whereas arachidonate was the preferred acyl group in the rat liver microsomal preparations. The rate of the back reaction was 3-5% and 0.2-0.4% of the forward reaction in the microsomal preparations of safflower and rat liver respectively. Previous observations, that the acyl exchange in safflower microsomal preparations was stimulated by bovine serum albumin and sn-glycerol 3-phosphate, can now be explained by the lowered acyl-CoA concentrations in the incubation mixture with albumin and in the increase in free CoA in the presence of sn-glycerol 3-phosphate (by rapid acylation of sn-glycerol 3-phosphate with acyl groups from acyl-CoA to yield phosphatidic acid). Bovine serum albumin and sn-glycerol 3-phosphate, therefore, shift the equilibrium in acyl-CoA:lysophosphatidylcholine acyltransferase-catalysed reactions towards the rate-limiting step in the acyl exchange process, namely the removal of acyl groups from phosphatidylcholine. The possible role of the acyl exchange in the transfer of acyl groups between complex lipids is discussed.
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A RAPID METHOD OF TOTAL LIPID EXTRACTION AND PURIFICATION
Bligh, E. G., & Dyer, W. J. (1959) · Canadian Journal of Biochemistry and Physiology · doi:10.1139/o59-099 · Cited by 54,751
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Production of very long chain polyunsaturated omega-3 and omega-6 fatty acids in plants
Qi, B., Fraser, T., Mugford, S., Dobson, G., Sayanova, O., Butler, J., Napier, J. A., Stobart, A. K., & Lazarus, C. M. (2004) · Nature Biotechnology · doi:10.1038/nbt972 · Cited by 426
Self-citationLi-Beisson, Y., Shorrosh, B., Beisson, F., Andersson, M. X., Arondel, V., Bates, P. D., Baud, S., Bird, D., DeBono, A., Durrett, T. P., et al. (2010) · The Arabidopsis Book · doi:10.1199/tab.0133 · Cited by 367
Abbadi, A., Domergue, F., Bauer, J., Napier, J. A., Welti, R., Zähringer, U., Cirpus, P., & Heinz, E. (2004) · The Plant Cell · doi:10.1105/tpc.104.026070 · Cited by 322
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Metadata
- Authors
- Stymne, S., & Stobart, A. K.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1984-10-15
- Volume
- 223
- Issue
- 2
- Pages
- 305-314
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- OpenAlex
- W1752808615
- Cited by
- 182
- References
- 1
- FWCI
- 2.26
- Type
- journal article
- Language
- en
- Open access
- bronze
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- CoChat. (2026). Citation check: Evidence for the reversibility of the acyl-CoA:lysophosphatidylcholine acyltransferase in microsomal preparations from developing safflower (Carthamus tinctorius L.) cotyledons and rat liver. https://app.cochat.ai/papers/10.1042/bj2230305
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- Stymne, S., & Stobart, A. K. (1984). Evidence for the reversibility of the acyl-CoA:lysophosphatidylcholine acyltransferase in microsomal preparations from developing safflower (Carthamus tinctorius L.) cotyledons and rat liver. Biochemical Journal. https://doi.org/10.1042/bj2230305
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