Ishizaki T, Hirayama N, Shinkawa H, Nimi O, Murooka Y
Department of Fermentation Technology, Faculty of Engineering, Hiroshima University, Japan.
J Bacteriol. 1989 Jan;171(1):596-601. doi: 10.1128/jb.171.1.596-601.1989.
The nucleotide sequence of a 2.1-kilobase-pair fragment containing the Streptomyces choA gene, which codes a secreted cholesterol oxidase, was determined. A single open reading frame encodes a mature cholesterol oxidase of 504 amino acids, with a calculated Mr of 54,913. The leader peptides extend over 42 amino acids and have the characteristics of a signal sequence, including basic amino acids near the amino terminus and a hydrophobic core near the signal cleavage site. Analyses of the total amino acid composition and amino acid sequencing of the first 21 amino acids from the N terminus of the purified extracellular enzyme agree with the values deduced from nucleotide sequencing data.
测定了一个包含编码分泌型胆固醇氧化酶的链霉菌choA基因的2.1千碱基对片段的核苷酸序列。一个单一的开放阅读框编码一个由504个氨基酸组成的成熟胆固醇氧化酶,计算的分子量为54,913。前导肽延伸超过42个氨基酸,并具有信号序列的特征,包括氨基末端附近的碱性氨基酸和信号切割位点附近的疏水核心。对纯化的细胞外酶N末端前21个氨基酸的总氨基酸组成和氨基酸测序分析与从核苷酸测序数据推导的值一致。