. 1984 Nov;76(3):654–657. doi:10.1104/pp.76.3.654
γ-Guanidinobutyraldehyde Dehydrogenase ofVicia faba Leaves
Hitoshi Matsuda1,2,Yonezo Suzuki1,2
Hitoshi Matsuda
1Science Education Institute of Osaka Prefecture, Karita, Sumiyoshi-ku, Osaka 558, Japan
2Department of Biology, Faculty of Science, Osaks City University, Sumiyoshi-ku, Osaka 558, Japan
Find articles byHitoshi Matsuda
Yonezo Suzuki
1Science Education Institute of Osaka Prefecture, Karita, Sumiyoshi-ku, Osaka 558, Japan
2Department of Biology, Faculty of Science, Osaks City University, Sumiyoshi-ku, Osaka 558, Japan
Find articles byYonezo Suzuki
1Science Education Institute of Osaka Prefecture, Karita, Sumiyoshi-ku, Osaka 558, Japan
2Department of Biology, Faculty of Science, Osaks City University, Sumiyoshi-ku, Osaka 558, Japan
PMCID: PMC1064350 PMID:16663901
Abstract
γ-Guanidinobutyraldehyde dehydrogenase was purified 27-fold in 40% yield from extracts ofVicia faba leaves. High specificity exist only for γ-guanidinobutyraldehyde and γ-aminobutyraldehyde; theKm value was 3.4 micromolar for γ-guanidinobutyraldehyde, 25 micromolar for γ-aminobutyraldehyde, and 84 micromolar (case of γ-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 byp-chloromercuribenzoate,N-ethylmaleimide, and zincon (2-carboxy-2′-hydroxy-5′-sulfoformazylbenzene).
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