Soluble aldehyde dehydrogenase and metabolism of aldehydes by soybean bacteroids.
A soluble aldehyde dehydrogenase (EC 1.2.1.3) was partially purified from Rhizobium japonicum bacteroids and from free-living R. japonicum 61A76. The enzyme was activated by NAD+, NADH, and dithiothreitol, and it reduced NAD(P)+. Acetaldehyde, propionaldehyde, butyraldehyde, benzaldehyde, and succinic semialdehyde were substrates. The Km for straight-chain aldehydes decreased with increasing carbon chain length. The aldehyde dehydrogenase was inhibited by 6-cyanopurine, but not by metronidazole. These compounds inhibited acetylene reduction, but not respiration, by isolated bacteroids.
D000079:Acetaldehyde / Q000494:pharmacology; D000114:Acetylene / Q000378:metabolism; D000445:Aldehyde Oxidoreductases / Q000378:metabolism*; D000447:Aldehydes / Q000378:metabolism*; D004229:Dithiothreitol / Q000494:pharmacology; D004789:Enzyme Activation; D007700:Kinetics; D008795:Metronidazole / Q000494:pharmacology; D009243:NAD / Q000494:pharmacology; D010101:Oxygen Consumption / Q000187:drug effects; D011687:Purines / Q000494:pharmacology; D012231:Rhizobium / Q000201:enzymology* / Q000502:physiology; D013025:Glycine max / Q000382:microbiology
D000447:Aldehydes; D011687:Purines; D009243:NAD; D008795:Metronidazole; C018030:6-cyanopurine; D000445:Aldehyde Oxidoreductases; D000079:Acetaldehyde; D000114:Acetylene; D004229:Dithiothreitol