Plant Acyl-CoA:lysophosphatidylcholine acyltransferases (LPCATs) have different specificities in their forward and reverse reactions

Ida Lager; Jenny Lindberg Yilmaz; Xue Rong Zhou; Katarzyna Jasieniecka; Michael Kazachkov; Peng Wang; Jitao Zou; Randall Weselake; Mark A. Smith; Shen Bayon; John M. Dyer; Jay M. Shockey; Ernst Heinz; Allan Green; Antoni Banas; Sten Stymne

doi:10.1074/jbc.M113.521815

Plant Acyl-CoA:lysophosphatidylcholine acyltransferases (LPCATs) have different specificities in their forward and reverse reactions

Ida Lager
, Jenny Lindberg Yilmaz
, Xue Rong Zhou
, Katarzyna Jasieniecka
, Michael Kazachkov
, Peng Wang
, Jitao Zou
, Randall Weselake
, Mark A. Smith
, Shen Bayon
, John M. Dyer
, Jay M. Shockey
, Ernst Heinz
, Allan Green
, Antoni Banas
, Sten Stymne

Research output: Contribution to journal › Article › peer-review

121 Scopus citations

Abstract

Background: Acyl-CoA:lysophosphatidylcholine acyltransferase (LPCAT) enzymes have central roles in acyl editing of phosphatidylcholine. Results: Plant LPCATs were expressed in yeast and biochemically characterized. Conclusion: LPCATs can edit acyl composition of phosphatidylcholine through their combined forward and reverse reactions. Significance: Plant LPCATs play a role in editing both sn-positions of PC and remove ricinoleic acid with high selectivity from this lipid.

Original language	English (US)
Pages (from-to)	36902-36914
Number of pages	13
Journal	Journal of Biological Chemistry
Volume	288
Issue number	52
DOIs	https://doi.org/10.1074/jbc.M113.521815
State	Published - Dec 27 2013

All Science Journal Classification (ASJC) codes

Biochemistry
Molecular Biology
Cell Biology

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10.1074/jbc.M113.521815

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Lager, I., Yilmaz, J. L., Zhou, X. R., Jasieniecka, K., Kazachkov, M., Wang, P., Zou, J., Weselake, R., Smith, M. A., Bayon, S., Dyer, J. M., Shockey, J. M., Heinz, E., Green, A., Banas, A., & Stymne, S. (2013). Plant Acyl-CoA:lysophosphatidylcholine acyltransferases (LPCATs) have different specificities in their forward and reverse reactions. Journal of Biological Chemistry, 288(52), 36902-36914. https://doi.org/10.1074/jbc.M113.521815

@article{c488a209b277461f88d78d0fa0d1e3eb,

title = "Plant Acyl-CoA:lysophosphatidylcholine acyltransferases (LPCATs) have different specificities in their forward and reverse reactions",

abstract = "Background: Acyl-CoA:lysophosphatidylcholine acyltransferase (LPCAT) enzymes have central roles in acyl editing of phosphatidylcholine. Results: Plant LPCATs were expressed in yeast and biochemically characterized. Conclusion: LPCATs can edit acyl composition of phosphatidylcholine through their combined forward and reverse reactions. Significance: Plant LPCATs play a role in editing both sn-positions of PC and remove ricinoleic acid with high selectivity from this lipid.",

author = "Ida Lager and Yilmaz, \{Jenny Lindberg\} and Zhou, \{Xue Rong\} and Katarzyna Jasieniecka and Michael Kazachkov and Peng Wang and Jitao Zou and Randall Weselake and Smith, \{Mark A.\} and Shen Bayon and Dyer, \{John M.\} and Shockey, \{Jay M.\} and Ernst Heinz and Allan Green and Antoni Banas and Sten Stymne",

year = "2013",

month = dec,

day = "27",

doi = "10.1074/jbc.M113.521815",

language = "English (US)",

volume = "288",

pages = "36902--36914",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology Inc.",

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Lager, I, Yilmaz, JL, Zhou, XR, Jasieniecka, K, Kazachkov, M, Wang, P, Zou, J, Weselake, R, Smith, MA, Bayon, S, Dyer, JM, Shockey, JM, Heinz, E, Green, A, Banas, A & Stymne, S 2013, 'Plant Acyl-CoA:lysophosphatidylcholine acyltransferases (LPCATs) have different specificities in their forward and reverse reactions', Journal of Biological Chemistry, vol. 288, no. 52, pp. 36902-36914. https://doi.org/10.1074/jbc.M113.521815

TY - JOUR

T1 - Plant Acyl-CoA:lysophosphatidylcholine acyltransferases (LPCATs) have different specificities in their forward and reverse reactions

AU - Lager, Ida

AU - Yilmaz, Jenny Lindberg

AU - Zhou, Xue Rong

AU - Jasieniecka, Katarzyna

AU - Kazachkov, Michael

AU - Wang, Peng

AU - Zou, Jitao

AU - Weselake, Randall

AU - Smith, Mark A.

AU - Bayon, Shen

AU - Dyer, John M.

AU - Shockey, Jay M.

AU - Heinz, Ernst

AU - Green, Allan

AU - Banas, Antoni

AU - Stymne, Sten

PY - 2013/12/27

Y1 - 2013/12/27

N2 - Background: Acyl-CoA:lysophosphatidylcholine acyltransferase (LPCAT) enzymes have central roles in acyl editing of phosphatidylcholine. Results: Plant LPCATs were expressed in yeast and biochemically characterized. Conclusion: LPCATs can edit acyl composition of phosphatidylcholine through their combined forward and reverse reactions. Significance: Plant LPCATs play a role in editing both sn-positions of PC and remove ricinoleic acid with high selectivity from this lipid.

AB - Background: Acyl-CoA:lysophosphatidylcholine acyltransferase (LPCAT) enzymes have central roles in acyl editing of phosphatidylcholine. Results: Plant LPCATs were expressed in yeast and biochemically characterized. Conclusion: LPCATs can edit acyl composition of phosphatidylcholine through their combined forward and reverse reactions. Significance: Plant LPCATs play a role in editing both sn-positions of PC and remove ricinoleic acid with high selectivity from this lipid.

UR - https://www.scopus.com/pages/publications/84891466456

UR - https://www.scopus.com/pages/publications/84891466456#tab=citedBy

U2 - 10.1074/jbc.M113.521815

DO - 10.1074/jbc.M113.521815

M3 - Article

C2 - 24189065

AN - SCOPUS:84891466456

SN - 0021-9258

VL - 288

SP - 36902

EP - 36914

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 52

ER -

Plant Acyl-CoA:lysophosphatidylcholine acyltransferases (LPCATs) have different specificities in their forward and reverse reactions

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