A locus of Pseudomonas pickettii DTP0602, had, that encodes 2,4,6-trichlorophenol-4-dechlorinase with hydroxylase activity, and hydroxylation of various chlorophenols by the enzyme

Functional Analysis of the Small Component of the 4-Hydroxyphenylacetate 3-Monooxygenase of Escherichia coli W: a Prototype of a New Flavin:NAD(P)H Reductase Subfamily

“…In fact, HadB shows significant similarity only with the H 2 O 2 -forming NADH oxidase from Thermus thermophilus HB8 (28). Interestingly, we have identified just at the 5Ј end of the hadAB operon of B. pickettii (36), a partially sequenced ORF that might form part of the same operon and that encodes a protein showing 23% amino acid identity with the HpaC reductase (data not shown). Whether the protein encoded by this ORF could be the real reductase component of the chlorophenol 4-hydroxylase from B. pickettii instead of the proposed HadB protein (Table 2) requires further research.…”

“…In this regard, a coupling protein enhancing the activity of an aromatic monooxygenase had been also described for the 4-HPA hydroxylase from Pseudomonas putida (2,3). However, in the past four years several TC-FDM enzymes whose amino acid sequences have revealed significant similarities with those of the HpaB and HpaC proteins have been reported in different bacteria, suggesting that HpaB and HpaC could be considered as the representative oxygenase and reductase components, respectively, of this new TC-FDM family (13,16,21,36,41).…”

Two‐Component Flavin‐dependent Pyrrole‐2‐carboxylate Monooxygenase from Rhodococcus Sp.

“…However, a high identity was observed with the single-component 2,4,6-trichlorophenol monooxygenase from Azotobacter sp. (Wieser et al, 1997) and the twocomponent monooxygenases chlorophenol-4-hydroxylase from Ralstonia pickettii (formerly Pseudomonas) and 4-hydroxyphenylacetate 3-hydroxylase from Escherichia coli (Prieto and Garcia, 1994;Takizawa et al, 1995). Interestingly, the sequences of both subunits of the R. pickettii enzyme contain the typical dinucleotide-binding motif (Takizawa et al, 1995), whereas none is present in the subunits of the Escherichia coli enzyme (Prieto and Garcia, 1994).…”

“…(Wieser et al, 1997) and the twocomponent monooxygenases chlorophenol-4-hydroxylase from Ralstonia pickettii (formerly Pseudomonas) and 4-hydroxyphenylacetate 3-hydroxylase from Escherichia coli (Prieto and Garcia, 1994;Takizawa et al, 1995). Interestingly, the sequences of both subunits of the R. pickettii enzyme contain the typical dinucleotide-binding motif (Takizawa et al, 1995), whereas none is present in the subunits of the Escherichia coli enzyme (Prieto and Garcia, 1994). It was suggested that the absence of this sequence might be correlated with the ability of enhanced NAD(P)H-dependent FAD reduction in the presence of a sub-strate (Prieto and Garcia, 1994).…”

“…In the cases of P. putidu, E. coli and R. pickettii, no redox-active cofactor was found within the second non-flavin-containing protein. It was suggested that this component has only a regulatory function and is not directly involved in the hydroxylation of the substrate (Arunachalam et al, 1992;Prieto and Garcia, 1994;Takizawa et al, 1995).…”