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Human Cyclooxygenase-2 Is a Sequence Homodimer That Functions as a Conformational Heterodimer*
TLDR
The studies suggest that the concentration and composition of the free FA pool in the environment in which PGHS-2 functions in cells, the FA tone, is a key factor regulating PG HS-2 activity and its responses to COX inhibitors.
Human cyclooxygenase-1 activity and its responses to COX inhibitors are allosterically regulated by nonsubstrate fatty acids
TLDR
It is speculated that having an FA bound to Eallo stabilizes time-dependently inhibited conformations of Ecat also stabilizes Ecat conformers during catalysis, enabling half of sites of COX activity.
Oxanine DNA Glycosylase Activity from Mammalian Alkyladenine Glycosylase*
TLDR
AAG is a mammalian enzyme that can act on all three purine deamination bases, hypoxanthine, xanthine and oxanine, and AAG can also remove 1,N6-ethenoadenine from single-stranded DNA.
Asymmetric Acetylation of the Cyclooxygenase-2 Homodimer by Aspirin and Its Effects on the Oxygenation of Arachidonic, Eicosapentaenoic, and Docosahexaenoic Acids
TLDR
It is reported that aspirin maximally acetylates one monomer of human (hu) PGHS-2, and in vitro studies suggest that 18R- and 17R-resolvins could be formed only at low rates corresponding to less than 1 and 5%, respectively, of the rates of formation of PGH2 by native PG HS-2.
Pre-existent Asymmetry in the Human Cyclooxygenase-2 Sequence Homodimer*
TLDR
Kinetic and aspirin labeling studies indicate that COX-2 is composed of two equivalent, stable populations of conformational heterodimers, and results suggest that native PGHS-2 assumes a reasonably stable, asymmetric Eallo/Ecat form during its folding and processing.
Catalytic mechanism of endonuclease v: a catalytic and regulatory two-metal model.
TLDR
DNA cleavage and Mn(2+)-rescue analysis suggest that amino acid substitutions at D43 impede the enzymatic activity severely while mutations at E89 and D110 may be tolerated, and two metal ions are involved in endonuclease V-mediated catalysis.
Different Fatty Acids Compete with Arachidonic Acid for Binding to the Allosteric or Catalytic Subunits of Cyclooxygenases to Regulate Prostanoid Synthesis*
TLDR
The distinctive binding specificities of PGHS subunits permit different combinations of non-esterified FAs, which can be manipulated dietarily, to regulate AA binding to Eallo and/or Ecat thereby controlling COX activities.
Defining amino acid residues involved in DNA-protein interactions and revelation of 3'-exonuclease activity in endonuclease V.
TLDR
Binding and cleavage analyses of multiple mutants at positions Y80 and H116 underscore the role these residues play in protein-DNA interaction and implicate their potential involvement as a hydrogen bond donor in recognition of deaminated DNA bases.
An Activity-based Sensing Approach for the Detection of Cyclooxygenase-2 in Live Cells.
TLDR
The development of CoxFluor is reported, the first activity-based sensing approach for monitoring COX-2 within live cells with confocal microscopy and flow cytometry, and enabled the detection of oxygen-dependent changes in COX2 activity that are independent of protein expression within live macrophage cells.
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