title: A novel phenol hydroxylase and catechol 2,3-dioxygenase from the thermophilic Bacillus thermoleovorans strain A2: nucleotide sequence and analysis of the genes.
abstract: The new thermophilic Bacillus thermoleovorans strain A2 degrades phenol and cresols via the meta cleavage pathway. The first two enzymes involved in this process, the phenol hydroxylase and catechol 2,3-dioxygenase, encoded by the pheA and pheB genes respectively, were cloned and sequenced. The deduced amino acid sequence of pheA contains 524 amino acids with a theoretical M(r) of 59,602 Da and displays less than 10% amino acid identity to known phenol hydroxylases. The greatest amino acid identity (54%) displayed by pheA is with the larger component of the two-component 4-hydroxyphenylacetic acid hydroxylase from Escherichia coli W encoded by hpaB. No second component was present on the 3.8-kb insert. The consensus sequence GXGXXG for FAD/NAD binding sites is not present in pheA. PheB encodes a new catechol 2,3-dioxygenase of 308 amino acids (M(r) 35,487 Da) which has greatest amino acid identity (43%) with the 3-methyl catechol 2,3-dioxygenase of Pseudomonas putida UCC2 encoded by tdnC. Both pheA and pheB encode new enzymes which display low sequence homology with those previously published.
authors.affiliation: Department of Technical Biochemistry, Technical University Hamburg-Harburg, Germany.
authors.forename: F M
authors.initials: FM
authors.lastname: Duffner
authors.forename: R
authors.initials: R
authors.lastname: Müller
mesh_terms: D001407:Bacillus / Q000201:enzymology / Q000235:genetics*; D050557:Catechol 2,3-Dioxygenase; D003001:Cloning, Molecular; D049308:Dioxygenases; D005798:Genes, Bacterial; D006899:Mixed Function Oxygenases / Q000737:chemistry / Q000235:genetics*; D010105:Oxygenases / Q000737:chemistry / Q000235:genetics*
chemical_list: D006899:Mixed Function Oxygenases; D010105:Oxygenases; D049308:Dioxygenases; D050557:Catechol 2,3-Dioxygenase; C022336:phenol 2-monooxygenase