Moon J, Chang H, Min K R, Kim Y
College of Pharmacy, Chungbuk National University Cheongju, Korea.
Biochem Biophys Res Commun. 1995 Mar 28;208(3):943-9. doi: 10.1006/bbrc.1995.1425.
The catechol 2,3-dioxygenase is an aromatic ring-fission enzyme catalyzing the conversion of catechol to 2-hydroxymuconic semialdehyde. A catechol 2,3-dioxygenase gene has been cloned from chromosomal DNA of Alcaligenes sp. KF711, and its sequence was determined. The catechol 2,3-dioxygenase gene was consisted of 927 nucleotides with ATG initiation codon and TGA termination codon, which can encode a polypeptide of molecular weight 35 kDa containing 308 amino acid residues. G+C content of the gene was 58 mol%, and a putative ribosome-binding sequence was identified at about 10 nucleotides upstream from the ATG initiation codon. The sequence of catechol 2,3-dioxygenase from Alcaligenes sp. KF711 exhibited 81-92% homology at nucleotide level and 84-92% homology at amino acid level with those of corresponding enzymes encoded in xylE of TOL plasmid, nahH of NAH7 plasmid, and dmpB of Pseudomonas CF600.
儿茶酚2,3-双加氧酶是一种芳香环裂解酶,催化儿茶酚转化为2-羟基粘康酸半醛。已从产碱杆菌属菌株KF711的染色体DNA中克隆出儿茶酚2,3-双加氧酶基因,并测定了其序列。儿茶酚2,3-双加氧酶基因由927个核苷酸组成,具有ATG起始密码子和TGA终止密码子,可编码一个分子量为35 kDa、含有308个氨基酸残基的多肽。该基因的G+C含量为58 mol%,在ATG起始密码子上游约10个核苷酸处鉴定出一个假定的核糖体结合序列。产碱杆菌属菌株KF711的儿茶酚2,3-双加氧酶序列在核苷酸水平上与TOL质粒的xylE、NAH7质粒的nahH和假单胞菌CF600的dmpB中编码的相应酶具有81-92%的同源性,在氨基酸水平上具有84-92%的同源性。