Purification, Crystallization and Properties of NADP+-Specific Glutamate Dehydrogenase from Lactobacillus fermentum
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概要
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The distribution of amino acid dehydrogenases in lactic acid bacteria was investigated. Several lactic acid bacteria were found to have NADP+-specific glutamate dehydrogenase, but NAD+- specific glutamate dehydrogenase activity was not detected in the bacteria tested. No alanine, leucine or lysine dehydrogenase activity was detected either, though serine and proline dehydrogenases occur in some of the bacteria. NADP+-specific glutamate dehydrogenase was purified to homogeneity and crystallized from Lactobacillus fermentum IFO 3071. The enzyme had a molecular weight of about 300, 000 and consisted of six subunits identical in molecular weight (50, 000). The enzyme is highly specific for L-glutamate and α-ketoglutarate, and the activity of the reductive amination is much higher than that of the oxidative deamination. The pH optima for the deamination and the amination were about 9.0 and 8.0, respectively. The apparent Km values were determined to be 79 mM for L-glutamate, 44 μM for NADP+, 5.6mM for α-ketoglutarate, 6.76mM for NH3, and 77.5 μM for NADPH.
著者
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Misono Haruo
Laboratory Of Applied Microbiology Department Of Agricultural Chemistry Kochi University
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Nagasaki Susumu
Laboratory of Applied Microbiology, Department of Bioresources Science, Kochi University
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MISONO Haruo
Laboratory of Applied Microbiology, Department of Agricultural Chemistry, Kochi University
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GOTO Norihiko
Laboratory of Applied Microbiology, Department of Agricultural Chemistry, Kochi University
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