Properties of γ-aminobutyraldehyde dehydrogenase from Escherichia coli |
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Authors: | María I Prieto Jesus Martin Rafael Balaa-Fouce Amando Garrido-Pertierra |
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Institution: | María I. Prieto, Jesus Martin, Rafael Balaña-Fouce,Amando Garrido-Pertierra |
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Abstract: | γ-Aminobutyraldehyde dehydrogenase from Escherichia coli K-12 has been purified and characterized from cell mutants able to grow in putrescine as the sole carbon and nitrogen source. The enzyme has an Mr of 195 000±10 000 in its dimeric form with an Mr of 95 000±1000 for each subunit, a pH optimum at 5.4 in sodium citrate buffer, and does not require bivalent cations for its activity. Km values are 31.3±6.8 μM and 53.8±7.4 μM for Δ-1-pyrroline and NAD+, respectively. An inhibitory capacity for NADH is also shown using the purified enzyme. |
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Keywords: | γ -aminobutyraldehyde dehydrogenase E coli γ -aminobutyraldé hyde dé shydrogé nase E coli |
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