Emil Fischer's lock and key model assumes that the active site is a perfect fit for a specific substrate and that once the substrate binds to the enzyme no further modification occurs.
World Heritage Site | Site of Special Scientific Interest | Fort McKavett State Historic Site | Fort Davis National Historic Site | Active Server Pages | Active Directory | Virgin Active | Active–stative language | World Trade Center site | Hanford Site | Caughnawaga Indian Village Site | Topper (archaeological site) | Savannah River Site | Active Space Technologies | Active pixel sensor | active duty | Steamtown National Historic Site | Eaton Site | World Heritage site | The Site | Starfish site | Site-specific art | site | Ostia Antica (archaeological site) | National Historic Site | Active suspension | Active Phased Array Radar | Active duty | active | world heritage site |
The spectroscopic properties of the flavin cofactor make it a natural reporter for changes occurring within the active site; this makes flavoproteins one of the most-studied enzyme families.
According to Fisher’s lock-and-key model proposed by Hermann Emil Fischer in 1884 and Koshland’s induced fit theory by Daniel E. Koshland, Jr. in 1958, given a peptide, the prerequisite condition for it to be cleaved by HIV-protease is a good fit and binding between the substrate and the enzyme’s active site.
This ligation of the thiolate to the iron center anchors the ACV within the active site.
Gallium inhibits RNR2 by substituting for Fe3+ in the active site.