Coleman J P, Perry J J
J Gen Microbiol. 1985 Nov;131(11):2901-7. doi: 10.1099/00221287-131-11-2901.
Mycobacterium vaccae strain JOB-5 cultured in the presence of propane contained an inducible secondary alcohol dehydrogenase. The enzyme was purified 198-fold using DEAE-cellulose, omega-aminopentyl agarose and NAD-agarose chromatography. The Mr of the enzyme was approximately 136000, with subunits of Mr 37000. The pH optimum for the reaction oxidizing propan-2-ol to propanone was 10-10.5 while the optimum for the reverse reaction was 7.5-8.5. The isoelectric point was 4.9. NAD but not NADP could serve as electron acceptor. The apparent Km values for propan-2-ol and NAD were 4.9 X 10(-5)M and 2.8 X 10(-4)M, respectively. The enzyme was inhibited by thiol reagents and metal chelators. It appears to play an essential role in the metabolism of propane by this bacterium.
在丙烷存在的情况下培养的母牛分枝杆菌菌株JOB-5含有一种可诱导的仲醇脱氢酶。使用DEAE-纤维素、ω-氨基戊基琼脂糖和NAD-琼脂糖色谱法将该酶纯化了198倍。该酶的Mr约为136000，亚基的Mr为37000。将丙-2-醇氧化为丙酮的反应的最适pH为10 - 10.5，而逆反应的最适pH为7.5 - 8.5。等电点为4.9。NAD而非NADP可作为电子受体。丙-2-醇和NAD的表观Km值分别为4.9×10(-5)M和2.8×10(-4)M。该酶受到硫醇试剂和金属螯合剂的抑制。它似乎在这种细菌的丙烷代谢中起重要作用。
