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...

Celý popis

Uloženo v:
Podrobná bibliografie
Hlavní autoři: Ellis, S W, Hayhurst, G P, Lightfoot, T, Smith, G, Harlow, J, Rowland-Yeo, K, Larsson, C, Mahling, J, Lim, C K, Wolf, C R, Blackburn, M G, Lennard, M S, Tucker, G T
Médium: Artigo
Jazyk:Inglês
Vydáno: 2000
Témata:
Research Article
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC1220791/
https://ncbi.nlm.nih.gov/pubmed/10642515
Tagy: Přidat tag
Žádné tagy, Buďte první, kdo otaguje tento záznam!

Podobné jednotky