Peterson J B, LaRue T A
J Bacteriol. 1982 Sep;151(3):1473-84. doi: 10.1128/jb.151.3.1473-1484.1982.
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.
从日本根瘤菌类菌体和自由生活的日本根瘤菌61A76中部分纯化出一种可溶性乙醛脱氢酶(EC 1.2.1.3)。该酶被NAD⁺、NADH和二硫苏糖醇激活,并能还原NAD(P)⁺。乙醛、丙醛、丁醛、苯甲醛和琥珀酸半醛是其底物。直链醛的米氏常数随碳链长度增加而降低。该乙醛脱氢酶受到6-氰基嘌呤的抑制,但不受甲硝唑的抑制。这些化合物抑制分离出的类菌体的乙炔还原,但不抑制其呼吸作用。