๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

Ketoconazole-induced conformational changes in the active site of cytochrome P450eryF

โœ Scribed by Jill R Cupp-Vickery; Carlos Garcia; Andy Hofacre; Kathleen McGee-Estrada


Book ID
115631159
Publisher
Elsevier Science
Year
2001
Tongue
English
Weight
530 KB
Volume
311
Category
Article
ISSN
0022-2836

No coin nor oath required. For personal study only.


๐Ÿ“œ SIMILAR VOLUMES


Solvation of the active site of cytochro
โœ Rebecca C. Wade ๐Ÿ“‚ Article ๐Ÿ“… 1990 ๐Ÿ› Springer Netherlands ๐ŸŒ English โš– 372 KB

Energetically favorable water binding sites in the substrate pocket ofcytochrome P450-cam have been predicted by a molecular mechanics method. Binding sites corresponding to all the experimentally observed water sites in this region of the enzyme were located. The calculations also indicate the pres

Hydration energy landscape of the active
โœ Volkhard Helms; Rebecca C. Wade ๐Ÿ“‚ Article ๐Ÿ“… 1998 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 221 KB

Hydration of protein cavities influences protein stability, dynamics, and function. Protein active sites usually contain water molecules that, upon ligand binding, are either displaced into bulk solvent or retained to mediate protein-ligand interactions. The contribution of water molecules to ligand

The Role of Serine-246 in Cytochrome P45
โœ Kim Choonkeun; Kim Haeyoung; Han Oksoo ๐Ÿ“‚ Article ๐Ÿ“… 2000 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 91 KB

A strongly conserved threonine residue in the I-helix of cytochrome P450 enzymes participates in a proton delivery system for binding and cleavage of dioxygen molecules. 6-Deoxyerythronol ide B hydroxylase (P450eryF) is unusual in that the conserved threonine residue is replaced by alanine in this e