Purification and Characterization of Novel N-Acyl-D-aspartate Amidohydrolase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6
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概要
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Alcaligenes xylosoxydans subsp. xylosoxydans A-6 (Alcaligenes A-6) produced N-acyl-D-aspartate amidohydrolase (D-AAase) in the presence of N-acetyl-D-aspartate as an inducer. The enzyme was purified to homogeneity. The enzyme had a molecular mass of 56 kDa and was shown by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE) to be a monomer. The isoelectric point was 4.8. The enzyme had maximal activity at pH 7.5 to 8.0 and 50℃, and was stable at pH 8.0 and up to 45℃. N-Formyl (K_m=12.5mM), N-acetyl (K_m=2.52mM), N-propionyl (K_m=0.194mM), N-butyryl (K_m=0.033mM), and N-glycyl (K_m=1.11mM) derivatives of D-aspartate were hydrolyzed, but N-carbobenzoyl-D-aspartate, N-acetyl-L-aspartate, and N-acetyl-D-glutamate were not substrates. The enzyme was inhibited by both divalent cations (Hg^<2+>, Ni^<2+>, Cu^<2+>) and thiol reagents (N-ethylmaleimide, iodoacetic acid, dithiothreitol, and p-chloromercuribenzoic acid). The N-terminal amino acid sequence and amino acid composition were analyzed.
- 社団法人日本農芸化学会の論文
- 1993-07-23
著者
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酒井 謙二
九大院生資環
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Wakayama Mamoru
Department Of Bioscience And Biotechnology Faculty Of Science And Engineering Ritsumeikan University
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Moriguchi Mitsuaki
Department Of Food And Bioscience Beppu University
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Moriguchi Mitsuaki
Department Of Applied Chemistry Faculty Of Engineering Oita University
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Katsuno Yutaka
Department of Applied Chemistry, Faculty of Engineering, Oita University
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KATSUNO Yuko
School of Food and Nutritional Sciences, University of Shizuoka
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Sakai Kenji
Department Of Environmental Chemistry And Engineering Faculty Of Engineering Oita University
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Maki Tetsuyoshi
Department Of Applied Chemistry Faculty Of Engineering Oita University
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SAKAI Kenji
Research Institute for Theoretical Physics Hiroshima University
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Sakai Kenji
Department Of Applied Chemistry Faculty Of Engineering Oita University
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