Effects of Bienzyme Complex Formation of Cysteine Synthetase from Escherichia coli on Some Properties and Kinetics

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概要

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• Some properties and kinetics of the free and bound serine acetyltransferases (SATs) and O-acetylserine sulfhydrylase-As (OASS-As) from Escherichia coli were investigated. In some cases, SAT⊿C20,deleting 20 amino acid residues from the C-terminus of the wild-type SAT (Biosci. Biotechnol. Biochem., 63,168-179 (1999)) was tested for comparison. The optimum pH and stability against some reagents for the free and bound wild-type SATs were similar except for the resistance to cold inactivation. The kinetics for the wild-type SAT and SAT⊿C20 followed a Ping-Pong Bi Bi mechanism with a mixed-type inhibition by L-cysteine. The kinetics and kinetic constants for the wild-type SAT were not changed by the complex formation with OASS-A. The optimum pH for OASS-A was shifted towards an alkaline pH by the complex formation. Thermal stability and stability against some reagents for the free and bound OASS-As were almost the same. On the other hand, the maximum velocity for OASS-A was lowered and dissociation constants for the substrates and products were increased by forming the complex with the wild-type SAT, although the kinetics for the free and bound enzymes followed the same Ping-Pong Bi Bi mechanism. From comparisons of computed courses of L-cysteine formation from L-serine using SAT (wild-type SAT and SAT⊿C20) and OASS-A with the experimental results and changes in the stability of the wild-type SAT by the complex formation, we discuss the role and significance of a complex formation for the cysteine synthetase.

• 社団法人日本農芸化学会の論文
• 2000-08-23

著者

• Nakanishi Kazuhiro

  Graduate School of Natural Science and Technology, Okayama University

• Sakiyama Takaharu

  Department of Bioscience and Biotechnology, Faculty of Engineering, Okayama University

• Nakanishi Kazuhiro

  Department of Bioscience and Biotechnology, Faculty of Engineering, Okayama University

• 崎山 高明

  Department Of Bioscience And Biotechnology Faculty Of Engineering Okayama University:(present Addres

• MATSUYAMA Asahi

  Research and Development Division, Kikkoman Corporation

• Kusubayashi Noriko

  Department Of Biochemical Engineering And Science Kyushu Institute Of Technology

• MINO Koshiki

  Department of Bioscience and Biotechnology, Faculty of Engineering, Okayama University

• EISAKI Naoki

  Research Institute of Innovative Technology for the Earth (RITE)

• YAMANOUE Tsuyoshi

  Department of Bioscience and Biotechnology, Faculty of Engineering, Okayama University

• Mino Koshiki

  Department Of Bioscience And Biotechnology Faculty Of Engineering Okayama University:japan

• Sakiyama Takaharu

  Department Of Agricultural Chemistry Faculty Of Agriculture The University Of Tokyo

• Nakanishi Kazuhiro

  Department Of Bioscience And Biotechnology Faculty Of Engineering Okayama University

• Nakanishi K

  Department Of Bioscience And Biotechnology Faculty Of Engineering Okayama University

• Nakanishi Kazuhiro

  Division Of Chemistry And Biochemistry Graduate School Of Natural Science And Technology Okayama Uni

• Nakanishi Kazuhiro

  Department Of Anesthesia Nippon Medical School

• MATSUYAMA Akinobu

  Corporate Development Center, Daicel Chemical Industries, Ltd., Tsukuba Research Center

• Matsuyama A

  Corporate Development Center Daicel Chemical Industries Ltd. Tsukuba Research Center

• Matsuyama Asahi

  Research And Development Division Kikkoman Corporation

• Nakanishi Kazuhiro

  Graduate School Of Natural Science And Technology Okayama University

• Yamanoue Tsuyoshi

  Department Of Bioscience And Biotechnology Faculty Of Engineering Okayama University

• Nakanishi Kazuhiro

  Deparment Of Food Science And Technology Faculty Of Agriculture Kyoto University

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