ロード中...

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...

詳細記述

保存先:
書誌詳細
主要な著者: 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
フォーマット: Artigo
言語:Inglês
出版事項: 2000
主題:
オンライン・アクセス:https://ncbi.nlm.nih.gov/pmc/articles/PMC1220791/
https://ncbi.nlm.nih.gov/pubmed/10642515
タグ: タグ追加
タグなし, このレコードへの初めてのタグを付けませんか!