| | CHE 415 - General Biochemistry I - Mechanisms of Substrate Recognition by Enzymes (Site not responding. Last check: 2007-11-05) |
 | | O label was consistently incorporated into the 1-hydroxyl group of the NAM residue, indicating that the bond broken was that connecting the 1-carbon of NAM to the oxygen atom in the glycosidic linkage. |
 | | Water is then allowed to attack the positively charged intermediate directly, providing a hydroxyl ion to the carbocation to produce the neutral and stable product, and a proton (hydrogen ion) to reprotonate the carboxyl group at Glu35 and regenerate the enzyme. |
 | | Based on the crystallographic data and later experiments designed to check hypotheses concerning the roles of specific amino acid residues, it was determined that the key histidine residues, His12 and His119, assist in the hydrolysis of the phosphodiester linkage by trading protons through the substrate. |
| people.uis.edu /efish1/Che415/Lectur14/lectur14.htm (2543 words) |