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Literature summary for 1.14.14.20 extracted from

  • Groening, J.; Eulberg, D.; Tischler, D.; Kaschabek, S.; Schloemann, M.
    Gene redundancy of two-component (chloro)phenol hydroxylases in Rhodococcus opacus 1CP (2014), FEMS Microbiol. Lett., 361, 68-75.
    View publication on PubMed
Search for more literature for 1.14.14.20

Cloned(Commentary)

Cloned (Comment) Organism
genes pheA1(1-3), phylogenetic analysis, typical for genes of the peripheral degradation of aromatic compounds, pheA1(1–3) and pheA2(1-3) are not located within gene clusters for central ortho- and meta-cleavage pathway. All three gene sets are nearby to genes with function in (chloro)aromatic degradation Rhodococcus opacus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
290000 310000 isozymes, gel filtration Rhodococcus opacus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2,4-dichlorophenol + FADH2 + O2 Rhodococcus opacus
-
 2,4-dichlorocatechol + FAD + H2O
-
 ?
2,4-dichlorophenol + FADH2 + O2 Rhodococcus opacus 1CP
-
 2,4-dichlorocatechol + FAD + H2O
-
 ?
2-chlorophenol + FADH2 + O2 Rhodococcus opacus poor substrate for isozyme PheA1(1) 2-chlorocatechol + FAD + H2O
-
 ?
2-chlorophenol + FADH2 + O2 Rhodococcus opacus 1CP poor substrate for isozyme PheA1(1) 2-chlorocatechol + FAD + H2O
-
 ?
4-chlorophenol + FADH2 + O2 Rhodococcus opacus
-
 4-chlorocatechol + FAD + H2O
-
 ?
4-chlorophenol + FADH2 + O2 Rhodococcus opacus 1CP
-
 4-chlorocatechol + FAD + H2O
-
 ?
4-methylphenol + FADH2 + O2 Rhodococcus opacus
-
 4-methylcatechol + FAD + H2O
-
 ?
additional information Rhodococcus opacus substrate speccificities of the three isozymes, overview ?
-
 ?
additional information Rhodococcus opacus 1CP substrate speccificities of the three isozymes, overview ?
-
 ?
phenol + FADH2 + O2 Rhodococcus opacus
-
 catechol + FAD + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Rhodococcus opacus A0A069AW73 gene pheA1(1); gene pheA1(1)
-
Rhodococcus opacus 1CP A0A069AW73 gene pheA1(1); gene pheA1(1)
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2,4-dichlorophenol + FADH2 + O2
-
 Rhodococcus opacus 2,4-dichlorocatechol + FAD + H2O
-
 ?
2,4-dichlorophenol + FADH2 + O2
-
 Rhodococcus opacus 1CP 2,4-dichlorocatechol + FAD + H2O
-
 ?
2-chlorophenol + FADH2 + O2
-
 Rhodococcus opacus 2-chlorocatechol + FAD + H2O
-
 ?
2-chlorophenol + FADH2 + O2 poor substrate for isozyme PheA1(1) Rhodococcus opacus 2-chlorocatechol + FAD + H2O
-
 ?
2-chlorophenol + FADH2 + O2
-
 Rhodococcus opacus 1CP 2-chlorocatechol + FAD + H2O
-
 ?
2-chlorophenol + FADH2 + O2 poor substrate for isozyme PheA1(1) Rhodococcus opacus 1CP 2-chlorocatechol + FAD + H2O
-
 ?
4-chlorophenol + FADH2 + O2
-
 Rhodococcus opacus 4-chlorocatechol + FAD + H2O
-
 ?
4-chlorophenol + FADH2 + O2
-
 Rhodococcus opacus 1CP 4-chlorocatechol + FAD + H2O
-
 ?
4-methylphenol + FADH2 + O2
-
 Rhodococcus opacus 4-methylcatechol + FAD + H2O
-
 ?
additional information substrate speccificities of the three isozymes, overview Rhodococcus opacus ?
-
 ?
additional information substrate speccificities of the three isozymes, overview Rhodococcus opacus 1CP ?
-
 ?
phenol + FADH2 + O2
-
 Rhodococcus opacus catechol + FAD + H2O
-
 ?

Subunits

Subunits Comment Organism
oligomer homotetrameric or homohexameric structure, all phenol hydroxylase isoenzymes, x * 59000-63000, SDS-PAGE Rhodococcus opacus

Synonyms

Synonyms Comment Organism
FAD reductase
-
 Rhodococcus opacus
PheA2
-
 Rhodococcus opacus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Rhodococcus opacus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
 assay at Rhodococcus opacus

Cofactor

Cofactor Comment Organism Structure
FADH2 FAD is again reduced at the expense of NADH and NADPH Rhodococcus opacus

General Information

General Information Comment Organism
evolution phylogenetic analysis shows exceptional high similarities of PheA1(1-3) and PheA2(1-3) to putative phenol hydroxylases in several Rhodococcus strains, overview Rhodococcus opacus