Results 31 to 40 of about 15,910 (222)
Prostaglandin endoperoxide synthase. The aspirin acetylation region.
Journal of Biological Chemistry, 1992 Aspirin selectively acetylates Ser-530 of prostaglandin endoperoxide (PGH) synthase-1. This causes inactivation of the cyclooxygenase activity of the enzyme, but does not appreciably affect its peroxidase activity. Although the aspirin-acetylated enzyme is inactive, we found that PGH synthase-1 in which Ser-530 had been replaced with an alanine was ...
Teruhiko Shimokawa, William L. Smith
openaire +3 more sources
Prostaglandin Pathways: Opportunities for Cancer Prevention and Therapy
Cancer Research, 2021 Because of profound effects observed in carcinogenesis, prostaglandins (PG), prostaglandin-endoperoxide synthases, and PG receptors are implicated in cancer development and progression.
Qiushi Wang +3 more
semanticscholar +1 more source
Diffusion properties of single FoF1-ATP synthases in a living bacterium unraveled by localization microscopy [PDF]
, 2012 FoF1-ATP synthases in Escherichia coli (E. coli) bacteria are membrane-bound enzymes which use an internal proton-driven rotary double motor to catalyze the synthesis of adenosine triphosphate (ATP). According to the 'chemiosmotic hypothesis', a series of proton pumps generate the necessary pH difference plus an electric potential across the bacterial ...
arxiv +1 more source
Investigation of the role of cysteines in catalysis by prostaglandin endoperoxide synthase. [PDF]
Journal of Biological Chemistry, 1994 The importance of cysteine residues in the cyclooxygenase activity of prostaglandin endoperoxide synthase (PGHS) was investigated using cysteine-specific reagents and site-directed mutagenesis. N-(7-Dimethyl-amino-4-methyl-3-coumarinyl)maleimide (DACM), a hydrophobic maleimide, inactivated both cyclooxygenase and peroxidase activities of apoPGHS in a ...
Lawrence J. Marnett +2 more
openaire +2 more sources
3D-localization microscopy and tracking of FoF1-ATP synthases in living bacteria [PDF]
, 2015 FoF1-ATP synthases are membrane-embedded protein machines that catalyze the synthesis of adenosine triphosphate. Using photoactivation-based localization microscopy (PALM) in TIR-illumination as well as structured illumination microscopy (SIM), we explore the spatial distribution and track single FoF1-ATP synthases in living E.
arxiv +1 more source
Binding of the immunomodulatory drug Bz-423 to mitochondrial FoF1-ATP synthase in living cells by FRET acceptor photobleaching [PDF]
, 2016 Bz-423 is a promising new drug for treatment of autoimmune diseases. This small molecule binds to subunit OSCP of the mitochondrial enzyme FoF1-ATP synthase and modulates its catalytic activities. We investigate the binding of Bz-423 to mitochondria in living cells and how subunit rotation in FoF1-ATP synthase, i.e.
arxiv +1 more source
Arthritis &Rheumatology, Accepted Article.Objectives Chondrocyte metabolic dysfunction plays an important role in osteoarthritis (OA) development during aging and obesity. Protein post‐translational modifications (PTMs) have recently emerged as an important regulator of cellular metabolism. We aim to study one type of PTM, lysine malonylation (MaK) and its regulator Sirt5 in OA development ...
Huanhuan Liu +11 more
wiley +1 more source
Subunit rotation in a single FoF1-ATP synthase in a living bacterium monitored by FRET [PDF]
, 2011 FoF1-ATP synthase is the ubiquitous membrane-bound enzyme in mitochondria, chloroplasts and bacteria which provides the 'chemical energy currency' adenosine triphosphate (ATP) for cellular processes. In Escherichia coli ATP synthesis is driven by a proton motive force (PMF) comprising a proton concentration difference {\Delta}pH plus an electric ...
arxiv +1 more source
Journal of Biological Chemistry, 2011 Prostaglandin endoperoxide H synthase (PGHS) catalyzes the oxidation of arachidonate to prostaglandin H2. We have previously synthesized and chemically characterized nitroarachidonic acid (AANO2), a novel anti-inflammatory signaling mediator. Herein, the
A. Trostchansky +6 more
semanticscholar +1 more source
Fast ATP-dependent Subunit Rotation in Reconstituted FoF1-ATP Synthase Trapped in Solution [PDF]
arXiv, 2021 FoF1-ATP synthases are ubiquitous membrane-bound, rotary motor enzymes that can catalyze ATP synthesis and hydrolysis. Their enzyme kinetics are controlled by internal subunit rotation, by substrate and product concentrations, by mechanical inhibitory mechanisms, but also by the electrochemical potential of protons across the membrane.
arxiv