Guerrillot L, Vandecasteele J P
Eur J Biochem. 1977 Nov 15;81(1):185-92. doi: 10.1111/j.1432-1033.1977.tb11940.x.
Two soluble aldehyde dehydrogenases isoenzymes have been purified and separated from extracts of a paraffin-assimilating bacterium, Pseudomonas aeruginosa. The first one, obtained at an estimated purity of 20% (spec. act. with butanal 0.33 kat/kg) was NAD-dependent. It was rapidly inactivated at pH 8.6 but was efficiently protected by NAD. It had a molecular weight of 225000 and presented a high affinity for aldehydes of short and middle chain lengths. The second enzyme, obtained in a nearly homogenous state (spec. act. with pentanal 0.62 kat/kg) was NADP-dependent. It was activated by ions, in particular potassium ions, and had a good affinity for aldehydes of higher chain lengths. Both enzymes were stabilized by thiols and glycerol and were inactivated by reagents of sulfhydryl groups. These enzymes are 'constitutive' and their physiological function is uncertain. When the bacteria were grown on n-paraffin a new membrane-bound NAD-dependent aldehyde dehydrogenase activity was produced.
已从同化石蜡的铜绿假单胞菌提取物中纯化并分离出两种可溶性醛脱氢酶同工酶。第一种酶，估计纯度为20%（对丁醛的比活性为0.33 kat/kg），依赖于NAD。它在pH 8.6时迅速失活，但能被NAD有效保护。其分子量为225000，对短链和中链长度的醛具有高亲和力。第二种酶，以近乎同质的状态获得（对戊醛的比活性为0.62 kat/kg），依赖于NADP。它被离子激活，特别是钾离子，对较长链长度的醛具有良好的亲和力。两种酶都通过硫醇和甘油得以稳定，并且被巯基试剂灭活。这些酶是“组成型”的，其生理功能尚不确定。当细菌在正构石蜡上生长时，会产生一种新的膜结合的依赖于NAD的醛脱氢酶活性。
