J. Lee et al., NUCLEOTIDE-SEQUENCE OF SALICYLATE HYDROXYLASE GENE AND ITS 5'-FLANKING REGION OF PSEUDOMONAS-PUTIDA KF715, Biochemical and biophysical research communications, 218(2), 1996, pp. 544-548
The salicylate hydroxylase, a flavoprotein monooxygenase, catalyzes th
e decarboxlative hydroxylation of salicylate to form catechol. Nucleot
ide sequence of a salicylate hydroxylase gene and its 5'-flanking regi
on in chromosomal DNA of Pseudomonas putida KF715 was analyzed. The sa
licylate hydroxylase was encoded in an open reading frame with 1308 ba
se pairs which can encode a polypeptide of molecular weight 48 kDa wit
h 435 amino acids. The open reading frame was preceded by a putative r
ibosome-binding sequence. A predicted amino acid sequence of the salic
ylate hydroxylase exhibited 84% identity with corresponding enzyme enc
oded in NAH7 plasmid, and 20 to 30% homologies with other similar flav
oprotein monooxygenases. A 5'-flanking sequence of the salicylate hydr
oxylase gene exhibited extensive homology with promoter and nahR-bindi
ng site of sal operon in NAH7 plasmid. (C) 1996 Academic Press, Inc.