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Properties of gamma-aminobutyraldehyde dehydrogenase from Escherichia coli
M I Prieto1, J Martin, R Balaña-Fouce
1Departamento de Bioquímica, Facultad de Veterinaria, Universidad Complutense, Madrid, Spain.
Biochimie
|November 1, 1987
Abstract:
gamma-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 +/- 1,000 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 microM and 53.8 +/- 7.4 microM for delta-1-pyrroline and NAD+, respectively. An inhibitory capacity for NADH is also shown using the purified enzyme.