Chemical Modification of Histidine Residue of N-Acyl-D-Glutamate Amidohydrolase from Pseudomonas sp. 5f-1
スポンサーリンク
概要
- 論文の詳細を見る
N-Acyl-D-glutamate amidohydrolase (D-AGase) from Pseudomonas sp. 5f-1 was inactivated by diethyl pyrocarbonate (DEP). The chemical modification by DEP showed a difference spectrum at 246nm due to the N-carbethoxyhistidine residue. Removal of the carbethoxy group from inactivated enzyme with hydroxylamine restored enzyme activity. The inactivation by DEP proceeded with pseudo-first-order kinetics, and was protected in the presence of the substrate N-acetyl-D-glutamate (Glu), or the competitive inhibitor sodium α-ketoglutarate (α-KGA). These results suggest the presence of an essential histidine residue at or near of the active site of the enzyme.
- 社団法人日本農芸化学会の論文
- 1996-04-23
著者
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酒井 謙二
九大院生資環
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Sakai Kenji
Department of Plant Resources, Kyushu University
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WAKAYAMA Mamoru
Department of Biotechnology, Faculty of Life Sciences, Ritsumeikan University
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MORIGUCHI Mitsuaki
Department of Applied Chemistry, Faculty of Engineering, Oita University
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YADA Harutaka
Department of Applied Chemistry, Faculty of Engineering, Oita University
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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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Yada Harutaka
Department Of Applied Chemistry Faculty Of Engineering Oita University
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Mori Masatsugu
Department Of Applied Chemistry Faculty Of Engineering Oita University
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Sakai Kenji
Department Of Environmental Chemistry And Engineering Faculty Of Engineering Oita University
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TSUTSUMI Tetsuo
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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Tsutsumi Tetsuo
Department Of Applied Chemistry Faculty Of Engineering Oita University
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Sakai Kenji
Department Of Applied Chemistry Faculty Of Engineering Oita University
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