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Plant and Cell Physiology, 1970, Vol. 11, No. 6 899-906
© 1970

Article

L-Tyrosine carboxy-lyase of barley roots

KAZUO HOSOI, SEIICHI YOSHIDA and MASAO HASEGAWA

Department of Biology, Tokyo Metropolitan University Fukazawa, Setagaya-ku, Tokyo, Japan

L-Tyrosine carboxy-lyase (E.C. 4. 1. 1. 25) was isolated from roots of germinating barley (Hordeum vulgare). The enzyme requires pyridoxal phosphate for maximum activity. The optimum pH for activity is about 7.0. The enzyme is inhibited by p-chloromercuribenzoate and hydroxylamine at 10–3 M. Enzyme activity is found in extracts from young roots, especially from those in early stages of development, but not in extracts from shoots of the same plant. Localization and changes in the amounts of L-tyrosine carboxy-lyase and aromatic amines in developing barley seedlings were measured. Participation of carboxy-lyase in the formation of aromatic amines in barley roots is suggested.

(Received July 17, 1970; )
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