Purification and Characterization of the Clostridium josui Porphobilinogen Deaminase Encoded by the hemC Gene from a Recombinant Escherichia coil

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概要

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• The porphobilinogen deaminase encoded by the Clostridium josui hemC gene was purified from a recombinant Escherichia coli strain and its properties were characterized. The optimal temperature and pH of the purified enzyme were 65°C and 7.0, respectively. This enzyme was quite thermostable : it retained 86% of the original activity after incubation at 70°C for 1h. The K_m and V_max values of the enzyme were 65μM and 3.3μmol/h/mg for porphobilinogen, respectively.

• 公益社団法人日本生物工学会の論文
• 1999-04-25

著者

• Ohmiya Kunio

  Faculty Of Bioresources Mie University

• KIMURA Tetsuya

  Faculty of Bioresources, Mie University

• Kajino T

  Special Research Laboratory Ii Toyota Central R&d Laboratories Inc.

• Kimura Tetsuya

  National Center For Seeds And Seedlings

• KARITA Shuichi

  Center for Molecular Biology and Genetics Mie University

• Sakka Kazuo

  Faculty Of Bioresources Mie University

• FUJINO Emi

  Graduate School of Bioresources, Mie University

• Fujino Emi

  Graduate School Of Bioresources Mie University

• FUJINO Emi

  Faculty of Bioresources Mie University

• Fujino Tsuchiyoshi

  Biodevelopment Division Central Institute Nagoya Seiraku Co. Ltd.

• Kimura Tetsuya

  Faculty Of Bioresources Mie University

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