Results 21 to 30 of about 12,733 (207)
Open Biology: overview for special issue on dynamics of protein fatty acylation
Open Biology, 2021 Fatty acylation is a widespread form of protein modification that occurs on specific intracellular and secreted proteins. Beyond increasing hydrophobicity and the affinity of the modified protein for lipid bilayers, covalent attachment of a fatty acid ...
Marilyn D. Resh
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Frontiers in Plant Science, 2023 The BAHD acyltransferase family is a class of proteins in plants that can acylate a variety of primary and specialized secondary metabolites. The typically acylated products have greatly improved stability, lipid solubility, and bioavailability and thus ...
Donghuan Xu +5 more
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Acyl-CoA:Lysophospholipid Acyltransferases [PDF]
Journal of Biological Chemistry, 2009 Cell membranes contain several classes of glycerophospholipids, which have numerous structural and functional roles in the cells. Polyunsaturated fatty acids, including arachidonic acid and eicosapentaenoic acid, are located at the sn-2 (but not sn-1)-position of glycerophospholipids in an asymmetrical manner.
Hideo, Shindou, Takao, Shimizu
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Substrate recruitment by zDHHC protein acyltransferases
Open Biology, 2021 Protein palmitoylation is the post-translational attachment of fatty acids, most commonly palmitate (C16 : 0), onto a cysteine residue of a protein. This reaction is catalysed by a family of integral membrane proteins, the zDHHC protein acyltransferases (
Martin Ian P. Malgapo, Maurine E. Linder
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Regulation of T cell function by protein S-acylation
Frontiers in Physiology, 2022 S-acylation, the reversible lipidation of free cysteine residues with long-chain fatty acids, is a highly dynamic post-translational protein modification that has recently emerged as an important regulator of the T cell function. The reversible nature of
Savannah J. West +4 more
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Structural Basis for the Acyltransferase Activity of Lecithin:Retinol Acyltransferase-like Proteins [PDF]
Journal of Biological Chemistry, 2012 Lecithin:retinol acyltransferase-like proteins, also referred to as HRAS-like tumor suppressors, comprise a vertebrate subfamily of papain-like or NlpC/P60 thiol proteases that function as phospholipid-metabolizing enzymes. HRAS-like tumor suppressor 3, a representative member of this group, plays a key role in regulating triglyceride accumulation and ...
Marcin, Golczak +5 more
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Intestinal triacylglycerol synthesis in fat absorption and systemic energy metabolism
Journal of Lipid Research, 2015 The intestine plays a prominent role in the biosynthesis of triacylglycerol (triglyceride; TAG). Digested dietary TAG is repackaged in the intestine to form the hydrophobic core of chylomicrons, which deliver metabolic fuels, essential fatty acids, and ...
Chi-Liang Eric Yen +2 more
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Local and substrate-specific S-palmitoylation determines subcellular localization of Gαo
Nature Communications, 2022 How palmitoylated proteins specifically localize is not fully understood. Here, authors created the SwissKASH assay to visualize S-palmitoylation in cells and uncovered a striking substrate selectivity of acyltransferases at the core of this process.
Gonzalo P. Solis +6 more
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Characterisation of two alcohol acyltransferases from kiwifruit (Actinidia spp.) reveals distinct substrate preferences. [PDF]
, 2011 Volatile esters are key compounds of kiwifruit flavour and are formed by alcohol acyltransferases that belong to the BAHD acyltransferase superfamily.
Souleyre, Edwige J. F. +13 more
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MOGAT2: A New Therapeutic Target for Metabolic Syndrome
Diseases, 2015 Metabolic syndrome is an ever-increasing health problem among the world’s population. It is a group of intertwined maladies that includes obesity, hypertriglyceridemia, hypertension, nonalcoholic fatty liver disease (NAFLD), and diabetes mellitus type II
Muhua Yang, Joseph T. Nickels
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