N-Formylation and N-methylation of the α-amino group of L-phenylalanine result in extremely decreased responses of the labellar sugar receptor of the fleshfly, whereas the same structural alteration of L-valine hardly affects the response. Methyl esterification of the α-carboxyl group of phenylalanine, on the other hand, maintains the response to some extent, but similar treatment of valine completely diminishes the response. The aromatic structure in phenylalanine is not essential for stimulation. These results suggest a substantial difference in the stereospecificities and functional group specificities of the furnase (F) and aliphatic carboxylate (T) sites in the sugar receptor. The effect of small peptides on the sugar receptor was examined systematically. Their effectiveness depends mainly on the place of the constituent amino acids rather than on their composition, indicating the decisive role that certain aliphatic amino acids in the C-terminal position play in stimulation. Remarkable regularities in the stimulating effectiveness of small peptides exactly correspond to the stereospecificity of each receptor site. We propose two hypothetical models of the F and T sites, which involve three and two subsites, respectively, that are capable of hydrogen bond formation. The F and T sites also have a hydrophobic subsite that discriminates the R groups of the stimulants and a few spatial barriers.
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