Properties of gamma-aminobutyraldehyde dehydrogenase from Escherichia coli.

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Prieto MI, Martin J, Balana-Fouce R, Garrido-Pertierra A

Properties of gamma-aminobutyraldehyde dehydrogenase from Escherichia coli.

Biochimie. 1987 Nov-Dec;69(11-12):1161-8.

PubMed ID
3129020 [ View in PubMed
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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.

DrugBank Data that Cites this Article

Drug Targets
DrugTargetKindOrganismPharmacological ActionActions
NADH4-trimethylaminobutyraldehyde dehydrogenaseProteinHumans
Unknown
Not AvailableDetails