Results 1 to 10 of about 50 (50)

Acyltransferases in Bacteria [PDF]

open access: yesMicrobiology and Molecular Biology Reviews, 2013
SUMMARY Long-chain-length hydrophobic acyl residues play a vital role in a multitude of essential biological structures and processes. They build the inner hydrophobic layers of biological membranes, are converted to intracellular storage compounds, and are used to modify protein properties or function as membrane anchors, to name only a few ...
Alexander Steinbüchel   +2 more
openaire   +3 more sources

Glycerophosphate/Acylglycerophosphate Acyltransferases [PDF]

open access: yesBiology, 2014
Acyl-CoA:glycerol-3-phosphate acyltransferase (GPAT) and acyl-CoA: 1-acyl-glycerol-3-phosphate acyltransferase (AGPAT) are involved in the de novo synthesis of triacylglycerol (TAG) and glycerophospholipids. Many enzymes belonging to the GPAT/AGPAT family have recently been identified and their physiological or pathophysiological roles have been ...
Takashi Tanikawa   +6 more
openaire   +3 more sources

The zDHHC family of S-acyltransferases [PDF]

open access: yesBiochemical Society Transactions, 2015
The discovery of the zDHHC family of S-acyltransferase enzymes has been one of the major breakthroughs in the S-acylation field. Now, more than a decade since their discovery, major questions centre on profiling the substrates of individual zDHHC enzymes (there are 24 ZDHHC genes and several hundred S-acylated proteins), defining the mechanisms of ...
Lemonidis, Kimon   +7 more
openaire   +4 more sources

Acyl-CoA:Lysophospholipid Acyltransferases [PDF]

open access: yesJournal 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
openaire   +3 more sources

Structural Basis for the Acyltransferase Activity of Lecithin:Retinol Acyltransferase-like Proteins [PDF]

open access: yesJournal 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 ...
Krzysztof Palczewski   +5 more
openaire   +3 more sources

Alcohol acyltransferases for the biosynthesis of esters

open access: yesBiotechnology for Biofuels and Bioproducts, 2023
AbstractEsters are widely used in food, energy, spices, chemical industry, etc., becoming an indispensable part of life. However, their production heavily relies on the fossil energy industry, which presents significant challenges associated with energy shortages and environmental pollution. Consequently, there is an urgent need to identify alternative
Gaofei Liu, Lei Huang, Jiazhang Lian
openaire   +3 more sources

Acyltransferases in Protease’s Clothing [PDF]

open access: yesThe Plant Cell, 2000
One of the most intriguing questions in plant secondary metabolism concerns the evolution of the genes required for the rapid diversification of plant chemistry. In particular, the mechanisms are beginning to be understood by which evolution recruits primary and intermediary metabolism genes ...
openaire   +3 more sources

In Vitro Analysis of Hedgehog Acyltransferase and Porcupine Fatty Acyltransferase Activities [PDF]

open access: yes, 2019
Hedgehog and Wnt proteins are modified by covalent attachment of the fatty acids palmitate and palmitoleate, respectively. These lipid modifications are essential for Hedgehog and Wnt protein signaling activities and are catalyzed by related, but distinct fatty acyltransferases: Hedgehog acyltransferase (Hedgehog) and Porcupine (Wnt).
James J. Asciolla   +4 more
openaire   +2 more sources

Structure, mechanism, and inhibition of Hedgehog acyltransferase [PDF]

open access: yesMolecular Cell, 2021
The Sonic Hedgehog (SHH) morphogen pathway is fundamental for embryonic development and stem cell maintenance and is implicated in various cancers. A key step in signaling is transfer of a palmitate group to the SHH N terminus, catalyzed by the multi-pass transmembrane enzyme Hedgehog acyltransferase (HHAT).
Coupland, Claire E.   +14 more
openaire   +5 more sources

Membrane Topology of Hedgehog Acyltransferase [PDF]

open access: yesJournal of Biological Chemistry, 2015
Hedgehog acyltransferase (Hhat) is a multipass transmembrane enzyme that mediates the covalent attachment of the 16-carbon fatty acid palmitate to the N-terminal cysteine of Sonic Hedgehog (Shh). Palmitoylation of Shh by Hhat is critical for short and long range signaling.
Armine Matevossian, Marilyn D. Resh
openaire   +2 more sources

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