Plant Physiology 76:654-657 (1984)
© 1984 American Society of Plant Biologists
Articles
-Guanidinobutyraldehyde Dehydrogenase of Vicia faba Leaves
Hitoshi Matsuda and
Yonezo Suzuki
Science Education Institute of Osaka Prefecture, Karita, Sumiyoshi-ku, Osaka 558, Japan,
Department of Biology, Faculty of Science, Osaks City University, Sumiyoshi-ku, Osaka 558, Japan
-Guanidinobutyraldehyde dehydrogenase was purified 27-fold in 40% yield from extracts of Vicia faba leaves. High specificity exist only for -guanidinobutyraldehyde and -aminobutyraldehyde; the Km value was 3.4 micromolar for -guanidinobutyraldehyde, 25 micromolar for -aminobutyraldehyde, and 84 micromolar (case of -guanidinobutyraldehyde) for NAD, respectively. The enzyme had a molecular weight of approximately 83,000. Optimal pH and temperature for activity were 9.5 and 45°C, respectively. The enzyme was inhibited strongly by p-chloromercuribenzoate, N-ethylmaleimide, and zincon (2-carboxy-2'-hydroxy-5'-sulfoformazylbenzene).
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