Taira K, Hayase N, Arimura N, Yamashita S, Miyazaki T, Furukawa K
Fermentation Research Institute, MITI, Tsukuba Science City, Ibaraki, Japan.
Biochemistry. 1988 May 31;27(11):3990-6. doi: 10.1021/bi00411a015.
The bphC gene encoding 2,3-dihydroxybiphenyl dioxygenase was cloned from biphenyl-degrading and chlorinated biphenyl-degrading Pseudomonas paucimobilis Q1, and its complete nucleotide sequence was determined. The DNA-derived protein sequence provides the primary structure of 298 amino acids. Polyclonal antibodies raised against this protein from P. paucimobilis Q1 failed to cross-react with the previously isolated 2,3-dihydroxybiphenyl dioxygenase from Pseudomonas pseudoalcaligenes KF707 [Furukawa, K., & Arimura, N. (1987) J. Bacteriol. 169, 924-927. Furukawa, K., Arimura, N., & Miyazaki, T. (1987) J. Bacteriol. 169, 427-429], despite the close similarities of these proteins in terms of their native as well as subunit molecular weights, cofactor, and enzymatic activities. The sequence homology of the 2,3-dihydroxybiphenyl dioxygenase from the two different sources is examined.
从能降解联苯和氯化联苯的少动假单胞菌Q1中克隆出了编码2,3-二羟基联苯双加氧酶的bphC基因,并测定了其完整的核苷酸序列。由DNA推导的蛋白质序列显示该蛋白由298个氨基酸组成。用少动假单胞菌Q1的这种蛋白制备的多克隆抗体,无法与之前从产碱假单胞菌KF707中分离出的2,3-二羟基联苯双加氧酶发生交叉反应[古川,K.,&有村,N.(1987年)《细菌学杂志》169, 924 - 927页。古川,K.,有村,N.,&宫崎,T.(1987年)《细菌学杂志》169, 427 - 429页],尽管这两种蛋白质在天然状态以及亚基分子量、辅因子和酶活性方面都非常相似。对来自两种不同来源的2,3-二羟基联苯双加氧酶的序列同源性进行了检测。