N-Acylation of stimulatory amino acids changes chiral recognition of the fleshfly labellar sugar receptor
作者:
IchiroShimada,
YujiMaki,
HiroshiSugiyama,
期刊:
Journal of Comparative Physiology A
(Springer Available online 2004)
卷期:
Volume 165,
issue 2
页码: 193-196
ISSN:0340-7594
年代: 2004
DOI:10.1007/BF00619193
出版商: Springer-Verlag-Berlin-Heidelberg
数据来源: Springer
摘要:
N-Acylation changed nonstimulatory Dvaline into a clear stimulant of the sugar receptor of the fleshfly,Boettcherisca peregrina.Of theN-acyl-D-valines, the most stimulatory wasN-acetyl-D-valine. Similar changes into stimulants were also observed in other aliphatic amino acids such as leucine and methionine. Dose-response curves ofN-acetyl-D-valine suggested an increase of binding affinity, compared with that ofN-acetyl-L-valine. By treatment experiment with pronase 10 mg/ml, stimulatoryN-acetyl-D-amino acids were suggested to react with the specific alkyl site (R site), which was presumed to discriminate between L- and D-forms of the amino acids through steric hindrance between its own spatial barrier and D-amino acids (Shimada and Isono 1978; Shimada and Tanimura 1981).
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