Lee J, Oh J, Min K R, Kim Y
College of Pharmacy, Chungbuk National University, Cheongju, Korea.
Biochem Biophys Res Commun. 1996 Jan 17;218(2):544-8. doi: 10.1006/bbrc.1996.0097.
The salicylate hydroxylase, a flavoprotein monooxygenase, catalyzes the decarboxylative hydroxylation of salicylate to form catechol. Nucleotide sequence of a salicylate hydroxylase gene and its 5'-flanking region in chromosomal DNA of Pseudomonas putida KF715 was analyzed. The salicylate hydroxylase was encoded in an open reading frame with 1308 base pairs which can encode a polypeptide of molecular weight 48 kDa with 435 amino acids. The open reading frame was preceded by a putative ribosome-binding sequence. A predicted amino acid sequence of the salicylate hydroxylase exhibited 84% identity with corresponding enzyme encoded in NAH7 plasmid, and 20 to 30% homologies with other similar flavoprotein monooxygenases. A 5'-flanking sequence of the salicylate hydroxylase gene exhibited extensive homology with promoter and nahR-binding site of sal operon in NAH7 plasmid.
水杨酸羟化酶是一种黄素蛋白单加氧酶，催化水杨酸的脱羧羟基化反应形成儿茶酚。对恶臭假单胞菌KF715染色体DNA中的水杨酸羟化酶基因及其5′侧翼区域的核苷酸序列进行了分析。水杨酸羟化酶由一个1308个碱基对的开放阅读框编码，该开放阅读框可编码一个含有435个氨基酸、分子量为48 kDa的多肽。该开放阅读框之前有一个假定的核糖体结合序列。水杨酸羟化酶的预测氨基酸序列与NAH7质粒中编码的相应酶具有84%的同一性，与其他类似的黄素蛋白单加氧酶具有20%至30%的同源性。水杨酸羟化酶基因的5′侧翼序列与NAH7质粒中sal操纵子的启动子和nahR结合位点具有广泛的同源性。
