Purification and Properties of Extremely Thermostable Glutamate Dehydrogenases from Two Hyperthermophilic Archaebacteria, Pyrococcus woesei and Pyrococcus furiosus

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概要

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• Glutamate dehydrogenase (L-glutamate: NADP oxidoreductase, deaminating, EC 1.4.1.4) from the hyperthermophilic archaebacteria Pyrococcus woesei and P. furiosus were purified to homogeneity from crude extracts. The enzymes had similar enzymological properties: molecular mass, subunit structure, optimum pHs for the oxidative deamination and reductive amination, substrate specificity and coenzyme specificity as well as thermostability; the activity was not lost after incubation at 105℃ for 30 min. However, some differences were detected in resistance to urea denaturation and effects of salts on their activity and stability. The N-terminal 20 amino acid sequences of the two enzymes were identical.

• 社団法人日本農芸化学会の論文
• 1993-06-23

著者

• OHSHIMA TOSHIHISA

  Department of Chemistry, Kyoto University of Education

• Nishida Naoshi

  Department Of Medicine And Clinical Science Graduate School Of Medicine Kyoto University

• Nishida Norikazu

  Department Of Medicine And Clinical Science Graduate School Of Medicine Kyoto University

• Ohshima T

  Microbial Genetics Division Institute Of Genetic Resources Faculty Of Agriculture Kyushu University

• Ohshima Toshihisa

  Department Of Biological Science And Technology Faculty Of Engineering The University Of Tokushima

• Ohshima Toshihisa

  Microbial Genetics Division, Institute of Genetic Resources, Faculty of Agriculture, Kyushu University

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