Inhibition of Aromatic L-Amino Acid Decarboxylase from Micrococcus percitreus by Substrate Analogs
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概要
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Inhibition of a constitutive aromatic L-amino acid decarboxylase from Micrococcus percitreus AJ 1065 was investigated to obtain some information about the reaction mechanism of the enzyme and the physiological role of the enzyme in the bacterium. Decarboxylation of L-tryptophan by the enzyme was inhibited by the other substrates and by aromatic amines such as β-phenylethylamine, tyramine, dopamine, epinephrine, norepinephrine, and 3-indoleacetamide and 3-indolealdehyde which correspond to or are related to the substrates of the enzyme. To study the mechanism of inhibition by 3, 4-dihydroxyphenyl-L-alanine, the nonenzymatic reaction product of pyridoxal 5-phosphate and 3, 4-dihydroxyphenyl-L-alanine was prepared and was identified as 7, 8-dihydroxy-1-[2-methyl-3-hydroxy-5-phosphohydroxymethyl-4-pyridyl]-3-carboxy-l, 2, 3, 4-tetrahydroisoquinoline.
- 社団法人 日本農芸化学会の論文
著者
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Yamada Hideaki
Department Of Agricultural Chemistry Faculty Of Agriculture Kyoto University
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KUMAGAI Hidehiko
Department of Agricultural Chemistry, Faculty of Agriculture, Kyoto University
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NAKAZAWA Hidetsugu
The Central Research Laboratories, Ajinomoto Co., Inc.
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