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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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| Autores principales: | , , , , , , |
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| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
The American Society for Biochemistry and Molecular Biology
2012
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| Materias: | |
| Acceso en línea: | 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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