Human cyclooxygenase-1 activity and its responses to COX inhibitors are allosterically regulated by nonsubstrate fatty acids

Recombinant human prostaglandin endoperoxide H synthase-1 (huPGHS-1) was characterized. huPGHS-1 has a single high-affinity heme binding site per dimer and exhibits maximal cyclooxygenase (COX) activity with one heme per dimer. Thus, huPGHS-1 functions as a conformational heterodimer having a cataly...

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Bibliographische Detailangaben
Hauptverfasser: Zou, Hechang, Yuan, Chong, Dong, Liang, Sidhu, Ranjinder S., Hong, Yu H., Kuklev, Dmitry V., Smith, William L.
Format: Artigo
Sprache:Inglês
Veröffentlicht: The American Society for Biochemistry and Molecular Biology 2012
Schlagworte:
Research Articles
Online Zugang:https://ncbi.nlm.nih.gov/pmc/articles/PMC3371245/
https://ncbi.nlm.nih.gov/pubmed/22547204
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1194/jlr.M026856
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