Purification and some properties of L-tyrosine carboxy-lyase from barley roots

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概要

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• L-Tyrosine carboxy-lyase (E. C. 4. 1. 1. 25) was extracted from the roots of barley seedlings and purified approximately 25 fold. Optimum pH for the enzyme activity was found to be 7.3. The Km value for L-tyrosine was calculated as 4.5 × 10^<-4> M. D-Isomer did not react with the enzyme. L-DOPA, m-tyrosine and o-tyrosine were decarboxylated to some extent. Pyridoxal phosphate activated the enzyme 4 fold. Caffeic acid and p-coumaric acid are competitive inhibitors. Ki values were 4.5 × 10^<-5> M for caffeic acid and 1.6 × 10^<-4> M for p-coumaric acid. L-DOPA and m-tyrosine had an inhibitory effect on the decarboxylation of L-tyrosine. Hydroxylamine, semi-carbazide, p-CMB, Fe^<++>, Cu^<++>, and Hg^<++> inhibited the decarboxylation of tyrosine. Enzyme activity was also found in extracts from Triticum aestivum, Zea mays and Cytisus scoparius.

• 日本植物生理学会の論文

著者

• Hosoi Kazuo

  Department Of Biology Faculty Of Science Tokyo Metropolitan University

関連論文

• Expression of an Allozyme of Prorenin-Converting Enzyme in the Submandibular Gland of DBA/2N Mice
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• Purification and some properties of L-tyrosine carboxy-lyase from barley roots
• Effects of aromatic acids on tyrosine carboxy-lyase from barley roots
• Expression of an Allozyme of Prorenin-Converting Enzyme in the Submandibular Gland of DBA/2N Mice.

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