Sandbox Reserved 770: Difference between revisions
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[[Image:Stabilizing_residues_of_PAL_active_site.png|thumb|left|Figure 7. Lys468 residue always adjacent to Gly residue]] | [[Image:Stabilizing_residues_of_PAL_active_site.png|thumb|left|Figure 7. Lys468 residue always adjacent to Gly residue]] | ||
'''Lysine468''' | '''Lysine468''' | ||
The positively charged side chain of Lys468 recognizes the carboxyl group of substrate by forming a salt bridge, when it is located in the mouth of the funnel. Before the side chain encloses, Lysine chaperones the substrate to its reactive position for sharing additional interactions between substrate's carboxyl group and side chains Glu496 and Gln500. Lys468 is strictly conserved with almost always adjacent Gly residue, which would improve mobility of Lys486 chaperone ability for substrate. Lys486 also acts to place the NH2 group of the substrate near MIO to ensure the carboxylate group of substrate does not react nonproductively with methylidene of MIO by forming an ester. | The positively charged side chain of Lys468 recognizes the carboxyl group of substrate by forming a salt bridge, when it is located in the mouth of the funnel. Before the side chain encloses, Lysine chaperones the substrate to its reactive position for sharing additional interactions between substrate's carboxyl group (Figure 8) and side chains Glu496 and Gln500. Lys468 is strictly conserved with almost always adjacent Gly residue (Figure 7), which would improve mobility of Lys486 chaperone ability for substrate. Lys486 also acts to place the NH2 group of the substrate near MIO to ensure the carboxylate group of substrate does not react nonproductively with methylidene of MIO by forming an ester. | ||
'''Histidine137''' | '''Histidine137''' | ||
