Identification of bile acid-CoA:amino acid N-acyltransferase as the hepatic N-acyl taurine synthase for polyunsaturated fatty acids

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Identification of bile acid-CoA:amino acid N-acyltransferase as the hepatic N-acyl taurine synthase for polyunsaturated fatty acids. / Trammell, Samuel A.J.; Gamon, Luke F.; Gotfryd, Kamil; Michler, Katja Thorøe; Alrehaili, Bandar D.; Rix, Iben; Knop, Filip K.; Gourdon, Pontus; Lee, Yoon Kwang; Davies, Michael J.; Gillum, Matthew P.; Grevengoed, Trisha J.

In: Journal of Lipid Research, Vol. 64, No. 9, 100361, 2023.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Trammell, SAJ, Gamon, LF, Gotfryd, K, Michler, KT, Alrehaili, BD, Rix, I, Knop, FK, Gourdon, P, Lee, YK, Davies, MJ, Gillum, MP & Grevengoed, TJ 2023, 'Identification of bile acid-CoA:amino acid N-acyltransferase as the hepatic N-acyl taurine synthase for polyunsaturated fatty acids', Journal of Lipid Research, vol. 64, no. 9, 100361. https://doi.org/10.1016/j.jlr.2023.100361

APA

Trammell, S. A. J., Gamon, L. F., Gotfryd, K., Michler, K. T., Alrehaili, B. D., Rix, I., Knop, F. K., Gourdon, P., Lee, Y. K., Davies, M. J., Gillum, M. P., & Grevengoed, T. J. (2023). Identification of bile acid-CoA:amino acid N-acyltransferase as the hepatic N-acyl taurine synthase for polyunsaturated fatty acids. Journal of Lipid Research, 64(9), [100361]. https://doi.org/10.1016/j.jlr.2023.100361

Vancouver

Trammell SAJ, Gamon LF, Gotfryd K, Michler KT, Alrehaili BD, Rix I et al. Identification of bile acid-CoA:amino acid N-acyltransferase as the hepatic N-acyl taurine synthase for polyunsaturated fatty acids. Journal of Lipid Research. 2023;64(9). 100361. https://doi.org/10.1016/j.jlr.2023.100361

Author

Trammell, Samuel A.J. ; Gamon, Luke F. ; Gotfryd, Kamil ; Michler, Katja Thorøe ; Alrehaili, Bandar D. ; Rix, Iben ; Knop, Filip K. ; Gourdon, Pontus ; Lee, Yoon Kwang ; Davies, Michael J. ; Gillum, Matthew P. ; Grevengoed, Trisha J. / Identification of bile acid-CoA:amino acid N-acyltransferase as the hepatic N-acyl taurine synthase for polyunsaturated fatty acids. In: Journal of Lipid Research. 2023 ; Vol. 64, No. 9.

Bibtex

@article{de806396e4374a2c95ba14cbc0b0212c,
title = "Identification of bile acid-CoA:amino acid N-acyltransferase as the hepatic N-acyl taurine synthase for polyunsaturated fatty acids",
abstract = "N-acyl taurines (NATs) are bioactive lipids with emerging roles in glucose homeostasis and lipid metabolism. The acyl chains of hepatic and biliary NATs are enriched in polyunsaturated fatty acids (PUFAs). Dietary supplementation with a class of PUFAs, the omega-3 fatty acids, increases their cognate NATs in mice and humans. However, the synthesis pathway of the PUFA-containing NATs remains undiscovered. Here, we report that human livers synthesize NATs and that the acyl-chain preference is similar in murine liver homogenates. In the mouse, we found that hepatic NAT synthase activity localizes to the peroxisome and depends upon an active-site cysteine. Using unbiased metabolomics and proteomics, we identified bile acid-CoA:amino acid N-acyltransferase (BAAT) as the likely hepatic NAT synthase in vitro. Subsequently, we confirmed that BAAT knockout livers lack up to 90% of NAT synthase activity and that biliary PUFA-containing NATs are significantly reduced compared with wildtype. In conclusion, we identified the in vivo PUFA-NAT synthase in the murine liver and expanded the known substrates of the bile acidconjugating enzyme, BAAT, beyond classic bile acids to the synthesis of a novel class of bioactive lipids.",
keywords = "bile acids and salts/biosynthesis, bile acids and salts/metabolism, liver, omega-3 fatty acids, peroxisomes",
author = "Trammell, {Samuel A.J.} and Gamon, {Luke F.} and Kamil Gotfryd and Michler, {Katja Thor{\o}e} and Alrehaili, {Bandar D.} and Iben Rix and Knop, {Filip K.} and Pontus Gourdon and Lee, {Yoon Kwang} and Davies, {Michael J.} and Gillum, {Matthew P.} and Grevengoed, {Trisha J.}",
note = "Publisher Copyright: {\textcopyright} 2023 THE AUTHORS.",
year = "2023",
doi = "10.1016/j.jlr.2023.100361",
language = "English",
volume = "64",
journal = "Journal of Lipid Research",
issn = "0022-2275",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "9",

}

RIS

TY - JOUR

T1 - Identification of bile acid-CoA:amino acid N-acyltransferase as the hepatic N-acyl taurine synthase for polyunsaturated fatty acids

AU - Trammell, Samuel A.J.

AU - Gamon, Luke F.

AU - Gotfryd, Kamil

AU - Michler, Katja Thorøe

AU - Alrehaili, Bandar D.

AU - Rix, Iben

AU - Knop, Filip K.

AU - Gourdon, Pontus

AU - Lee, Yoon Kwang

AU - Davies, Michael J.

AU - Gillum, Matthew P.

AU - Grevengoed, Trisha J.

N1 - Publisher Copyright: © 2023 THE AUTHORS.

PY - 2023

Y1 - 2023

N2 - N-acyl taurines (NATs) are bioactive lipids with emerging roles in glucose homeostasis and lipid metabolism. The acyl chains of hepatic and biliary NATs are enriched in polyunsaturated fatty acids (PUFAs). Dietary supplementation with a class of PUFAs, the omega-3 fatty acids, increases their cognate NATs in mice and humans. However, the synthesis pathway of the PUFA-containing NATs remains undiscovered. Here, we report that human livers synthesize NATs and that the acyl-chain preference is similar in murine liver homogenates. In the mouse, we found that hepatic NAT synthase activity localizes to the peroxisome and depends upon an active-site cysteine. Using unbiased metabolomics and proteomics, we identified bile acid-CoA:amino acid N-acyltransferase (BAAT) as the likely hepatic NAT synthase in vitro. Subsequently, we confirmed that BAAT knockout livers lack up to 90% of NAT synthase activity and that biliary PUFA-containing NATs are significantly reduced compared with wildtype. In conclusion, we identified the in vivo PUFA-NAT synthase in the murine liver and expanded the known substrates of the bile acidconjugating enzyme, BAAT, beyond classic bile acids to the synthesis of a novel class of bioactive lipids.

AB - N-acyl taurines (NATs) are bioactive lipids with emerging roles in glucose homeostasis and lipid metabolism. The acyl chains of hepatic and biliary NATs are enriched in polyunsaturated fatty acids (PUFAs). Dietary supplementation with a class of PUFAs, the omega-3 fatty acids, increases their cognate NATs in mice and humans. However, the synthesis pathway of the PUFA-containing NATs remains undiscovered. Here, we report that human livers synthesize NATs and that the acyl-chain preference is similar in murine liver homogenates. In the mouse, we found that hepatic NAT synthase activity localizes to the peroxisome and depends upon an active-site cysteine. Using unbiased metabolomics and proteomics, we identified bile acid-CoA:amino acid N-acyltransferase (BAAT) as the likely hepatic NAT synthase in vitro. Subsequently, we confirmed that BAAT knockout livers lack up to 90% of NAT synthase activity and that biliary PUFA-containing NATs are significantly reduced compared with wildtype. In conclusion, we identified the in vivo PUFA-NAT synthase in the murine liver and expanded the known substrates of the bile acidconjugating enzyme, BAAT, beyond classic bile acids to the synthesis of a novel class of bioactive lipids.

KW - bile acids and salts/biosynthesis

KW - bile acids and salts/metabolism

KW - liver

KW - omega-3 fatty acids

KW - peroxisomes

UR - http://www.scopus.com/inward/record.url?scp=85172425856&partnerID=8YFLogxK

U2 - 10.1016/j.jlr.2023.100361

DO - 10.1016/j.jlr.2023.100361

M3 - Journal article

C2 - 36958721

AN - SCOPUS:85172425856

VL - 64

JO - Journal of Lipid Research

JF - Journal of Lipid Research

SN - 0022-2275

IS - 9

M1 - 100361

ER -

ID: 369136603