Sandbox Reserved 770: Difference between revisions
From Proteopedia
Jump to navigationJump to search
Bryan Toton (talk | contribs) |
Bryan Toton (talk | contribs) |
||
| Line 69: | Line 69: | ||
Most of the conserved active site residues are contained within seven stabilizing alpha helices, represented by Figure 6. These residues include: Leu266, Asn270, Val269, Leu215, Lys486, and Ile472.<ref name=rutgers>http://maptest.rutgers.edu/drupal/?q=node/408</ref> Six positive alpha helices point toward the active site in association with MIO cofactor. This association will not only increase the electrophilicity of MIO, but also increases he positive charge of highly conserved Lys468 residue. The positive poles are suitable for stabilizing a carbanionic charge produced by an elimination unimolecular conjugate base (E1cB) mechanism of substrate phenylalanine, in accordance with MIO cofactor. Stabilization of the carbanion reduces pKa of the C3 methylidine group of phenylalanine, promoting the interactions between the negatively charged carboxylate end of phenylalanine to the active site of PAL. | Most of the conserved active site residues are contained within seven stabilizing alpha helices, represented by Figure 6. These residues include: Leu266, Asn270, Val269, Leu215, Lys486, and Ile472.<ref name=rutgers>http://maptest.rutgers.edu/drupal/?q=node/408</ref> Six positive alpha helices point toward the active site in association with MIO cofactor. This association will not only increase the electrophilicity of MIO, but also increases he positive charge of highly conserved Lys468 residue. The positive poles are suitable for stabilizing a carbanionic charge produced by an elimination unimolecular conjugate base (E1cB) mechanism of substrate phenylalanine, in accordance with MIO cofactor. Stabilization of the carbanion reduces pKa of the C3 methylidine group of phenylalanine, promoting the interactions between the negatively charged carboxylate end of phenylalanine to the active site of PAL. | ||
==Conserved Residues in Catalysis== | ==Conserved Residues in Catalysis== | ||
