EC Number   |
General Information |
Reference |
|---|
   1.14.14.20 | evolution |
phylogenetic analysis shows exceptional high similarities of PheA1(1-3) and PheA2(1-3) to putative phenol hydroxylases in several Rhodococcus strains, overview |
-, 736121 |
| 1.14.14.20 | metabolism |
the gene cluster comprising genes catA, catB, catC, catR, pheR, pheA2, pheA1, is involved in the ortho-cleavage pathway of phenol, the key enzyme of the phenol degradation pathway is the two-component phenol hydroxylase. Regulation analysis, the type of carbon catabolite repression and the temporal transcriptional pattern during cultivation are different in each of the analyzed phe clusters from Rhodococcus erythropolis and Rhodococcus jostii |
-, 735546 |
| 1.14.14.20 | more |
PheA2 homology modeling using the structure of ferric reductase (FeR) from Archaeoglobus fulgidus with NADP+ bound, PDB ID 1IOS, as template, overview |
-, 659279 |
| 1.14.14.20 | more |
structure analysis and modeling |
-, 736400 |
| 1.14.14.20 | physiological function |
Geobacillus thermoglucosidasius strain A7 degrades phenol at 65°C via the meta cleavage pathway |
-, 736171 |
| 1.14.14.20 | physiological function |
phenol hydroxylase (PheA) catalyzes the first step in the degradation of phenol in Geobacillus thermoglucosidasius strain A7 is described. The two-protein system, encoded by the pheA1 and pheA2 genes, consists of an oxygenase (PheA1) and a flavin reductase (PheA2) |
-, 659279 |
| 1.14.14.20 | physiological function |
phenol hydroxylase is a two-component enzyme encoded by pheA1 and pheA2 genes and strictly dependent on NADH and FAD. The intracellular enzyme is a clear example of a two-component tetrameric flavoprotein hydroxylase, in which flavin reduction and substrate oxygenation take place in the same protein |
-, 736132 |
| 1.14.14.20 | physiological function |
phenol-degrading aerobic bacteria are able to convert phenol into nontoxic intermediates of the tricarboxylic acid cycle via an ortho or meta pathway. The monooxygenation of the aromatic ring constitutes the first step in the biodegradation of many phenolic compounds. The two-component flavin-dependent monooxygenase phenol hydroxylase catalyzes the conversion of phenol to catechol in Rhodococcus erythropolis UPV-1. Recombinant PheA1 has no phenol hydroxylase activity on its own. Recombinant PheA2 is a flavin reductase that uses NAD(P)H in order to reduce flavin adenine dinucleotide (FAD), according to a random sequential kinetic mechanism. The hydroxylation of phenol in vitro requires the presence of both PheA1 and PheA2 components, in addition to NADH and FAD, but the physical interaction between the proteins is not necessary for the reaction. The enzymic activity catalyzed in vitro by His6PheA2 is essential to carry out the hydroxylation of phenol by His6PheA1 |
-, 701875 |
| 1.14.14.20 | physiological function |
the catabolism of toxic phenols in the thermophilic organism Bacillus thermoglucosidasius A7 is initiated by a two-component enzyme system. The smaller flavin reductase PheA2 component catalyzes the NADH-dependent reduction of free FAD according to a pingpong bisubstrate-biproduct mechanism. The reduced FAD is then used by the larger oxygenase component PheA1 to hydroxylate phenols to the corresponding catechols |
-, 736400 |
