Effects of various compounds on histidine decarboxylase activity: Active site mapping |
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Authors: | Yoshiteru Sakamoto Dr Takehiko Watanabe Hideyuki Hayashi Yoshitaka Taguchi Hiroshi Wada |
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Affiliation: | (1) Department of Pharmacology II, Osaka University School of Medicine, 3-57 Nakanoshima 4-chome, Kita-ku, 530 Osaka, Japan;(2) Present address: Central Research Laboratory, Oska University School of Medicine, Osaka, Japan |
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Abstract: | The effect of about one hundred compounds on the activity of histidine decarboxylase partially purified from whole bodies of fetal rats was determined. Most of them at their 10 mM concentration had little effect on the enzyme activity; but 12 compounds inhibited the enzyme to a greater extent than 30%. Among these, except for -methylhistidine that has been known to be a strong and specific inhibitor, DOPA, homocysteine, cysteine, methionine and urocanic acid were the best inhibitors; -phenyllactic acid, phenylpyruvic acid and carnosine were less strong inhibitors; valine, oxaloacetic acid andN-methylimidazole acetic acid were weak inhibitors. Histamine had no inhibitory action. Thus, the substrate binding site of histidine decarboxylase is very rigid and specific forl-histidine. |
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