恶臭假单胞菌顺式甲苯二氢二醇脱氢酶的纯化及性质
Purification and properties of cis-toluene dihydrodiol dehydrogenase from Pseudomonas putida.
作者信息
Rogers J E, Gibson D T
出版信息
J Bacteriol. 1977 Jun;130(3):1117-24. doi: 10.1128/jb.130.3.1117-1124.1977.
Abstract
The purification of (+)-cis-1(S),2(R)-dihydroxy-3-methylcyclohexa-3,5-diene dehydrogenase from cells of Pseudomonas putida grown with toluene as the sole source of carbon and energy is reported. The molecular weight of the enzyme is 104,000 at pH 9.7. The enzyme is composed of four apparently identical subunits with molecular weights of 27,000. The enzyme is specific for nicotinamide adenine dinucleotide and oxidizes a number of cis-dihydrodiols. Both enantiomers of a racemic mixture of cis-1,2-dihydroxyl-1,2-dihydronaphthalene dihydrodiol are oxidized by the enzyme. No enzymatic activity is observed with trans-1,2-dihydroxyl-1,2-dihydronaphthalene dihydrodiol.
摘要
报道了从以甲苯作为唯一碳源和能源生长的恶臭假单胞菌细胞中纯化(+)-顺式-1(S),2(R)-二羟基-3-甲基环己-3,5-二烯脱氢酶的方法。该酶在pH 9.7时分子量为104,000。该酶由四个分子量为27,000的明显相同的亚基组成。该酶对烟酰胺腺嘌呤二核苷酸具有特异性，并能氧化多种顺式二氢二醇。顺式-1,2-二羟基-1,2-二氢萘二氢二醇外消旋混合物的两种对映体均被该酶氧化。反式-1,2-二羟基-1,2-二氢萘二氢二醇未观察到酶活性。
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