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FEMS Microbiol Lett. 1998 Apr 1;161(1):37-45.

A novel phenol hydroxylase and catechol 2,3-dioxygenase from the thermophilic Bacillus thermoleovorans strain A2: nucleotide sequence and analysis of the genes.

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Department of Technical Biochemistry, Technical University Hamburg-Harburg, Germany.


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.

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