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Evidence that serine 304 is not a key ligand-binding residue in the active site of cytochrome P450 2D6.
Homology models of cytochrome P450 2D6 (CYP2D6) have identified serine 304 as an active-site residue and implicated a putative role for this residue in substrate enantioselectivity and the differential inhibition of enzyme activity by the diastereoisomers quinine and quinidine. The role of serine 30...
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| Hlavní autoři: | , , , , , , , , , , , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
2000
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1220791/ https://ncbi.nlm.nih.gov/pubmed/10642515 |
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