Characterization of meso-Diaminopimelate Dehydrogenase from Corynebacterium glutamicum and Its Distribution in Bacteria(Microbiology & Fermentaion Industry)

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概要

• 論文の詳細を見る

• meso-Diaminopimelate dehydrogenase (EC 1.4.1.16) was purified to homogeneity from Corynebacterium glutamicum ATCC 13032. The enzyme had a molecular weight of about 70,000 and consisted of two subunits identical in molecular weight. The enzyme was highly specific for meso-2,6-diaminopimelate. The pH optima for deamination and amination were about 9.8 and 7.9, respectively. The Michaelis constants were 3.1 mM for meso-2,6-diaminopimelate, 0.12 mM for NADP^+, 0.28 mM for L-2-amino-6-ketopimelate, 36 mM for ammonia, and 0.13 mM for NADPH. D and L isomers of 2,6-diaminopimelate competitively inhibited the oxidative deamination of meso-2,6-diaminopimelate. The enzyme was distributed in a wider range of bacterial species than reported previously [Misono et al, J. Bacteriol., 137, 22 (1979)] when assayed by a sensitive formazan formation method.

• 社団法人日本農芸化学会の論文
• 1986-11-23

著者

• Misono H

  Kochi Univ. Kochi Jpn

• Misono Haruo

  Department Of Bioresources Science Faculty Of Agriculture Kochi University

• Misono Haruo

  Department Of Bioresource Science Kochi University

• Misono Haruo

  Laboratory Of Applied Microbiology Department Of Agricultural Chemistry Kochi University

• Nagasaki S

  Department Of Bioresources Science Kochi University

• Nagasaki Susumu

  Laboratory of Applied Microbiology, Department of Bioresources Science, Kochi University

• OGASAWARA Masanobu

  Laboratory of Applied Microbiology, Department of Agricultural Chemistry, Kochi University

• Ogasawara Masanobu

  Weed Control Research Institute Faculty Of Agriculture Utsunomiya University

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