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Enzymes and Receptors of Prostaglandin Pathways with Arachidonic Acid-derived Versus Eicosapentaenoic Acid-derived Substrates and Products*♦
TLDR
In vitro specificities of prostanoid enzymes and receptors toward EPA-derived, 3-series versus AA- derived, 2-series prostanoids substrates and products are reported and biochemical data predict that increasing phospholipid EPA/AA ratios in cells would dampen prostanoidal signaling. Expand
Structure determination of selenomethionyl S-adenosylhomocysteine hydrolase using data at a single wavelength
TLDR
The crystallographic structure determination of a selenomethionyl-incorporated AdoHcy hydrolase inhibitor complex was accomplished using single wavelength anomalous diffraction data and the direct methods program, Snb v2.0, which produced the positions of all 30 crystallographically distinct selenium atoms. Expand
Cyclooxygenase Allosterism, Fatty Acid-mediated Cross-talk between Monomers of Cyclooxygenase Homodimers*
TLDR
It is shown that, during catalysis, fatty acids (FAs) are bound at both COX sites of a PGHS-2 dimer, and the efficiency of AA oxygenation is determined by the nature of the FA bound to the allosteric monomer. Expand
Two Distinct Pathways for Cyclooxygenase-2 Protein Degradation*
TLDR
Evidence is provided from site-directed mutagenesis that a 27-amino acid instability motif (27-IM) regulates posttranslational N-glycosylation of Asn-594, which occurs at a constant rate, whereas degradation through the substrate-dependent process is coupled to the rate of substrate turnover. Expand
Coxibs interfere with the action of aspirin by binding tightly to one monomer of cyclooxygenase-1
TLDR
It is predicted that the cardioprotective effect of low-dose aspirin on COX-1 may be blunted when taken with coxibs, and administration of celecoxib to dogs interferes with the ability of a low dose of aspirin to inhibit AA-induced ex vivo platelet aggregation. Expand
Comparison of cyclooxygenase-1 crystal structures: cross-talk between monomers comprising cyclooxygenase-1 homodimers.
TLDR
It is proposed that cross-talk between monomers involves this mobile 123-129 loop, which is located at the dimer interface, and in ovine PGHS-1 crystallized in the absence of an NSAID, there is an alternative route for substrate entry into the COX site different than the well-known route through the membrane binding domain. Expand
Recent advances in S-adenosyl-L-homocysteine hydrolase inhibitors and their potential clinical applications
TLDR
The increased understanding of the biochemical properties and mechanisms of catalysis mediated by SAH hydrolase has been to generate more potent and more specific inhibitors of the enzyme. Expand
Mechanism of inactivation of S-adenosylhomocysteine hydrolase by (Z)-4',5'-didehydro-5'-deoxy-5'-fluoroadenosine.
TLDR
This study has shown that the mechanism of this inactivation of AdoHcy hydrolase (NAD+ form) includes a rapid addition of water to the 5'-position of ZDDFA and elimination of fluoride ion, resulting in the formation of the 5'carboxaldehydes 3 and 4. Expand
Chemical Modification and Site-directed Mutagenesis of Cysteine Residues in Human Placental S-Adenosylhomocysteine Hydrolase*
TLDR
Results suggested that the Cys195 is involved in the catalytic center and may play an important role in maintaining the 3′-reduction potential for effective release of the reaction products and regeneration of the active form (NAD+ form) of the enzyme. Expand
A single mutation at lysine 426 of human placental S-adenosylhomocysteine hydrolase inactivates the enzyme.
TLDR
It is shown here that lysine 426 is essential for the catalytic activity of the enzyme and that it appears to play a crucial role in the 5'-hydrolytic activity and/or stability of the quaternary structure of the human placental enzyme. Expand
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