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Literature summary for 1.14.13.50 extracted from
- Classic pentachlorophenol hydroxylating phenylalanine 4-monooxygenase from indigenous Bacillus tropicus strain AOA-CPS1 cloning, overexpression, purification, characterization and structural homology modelling (2022), Appl. Biochem. Biotechnol., 194, 635-658 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| sequence comparisons and phylogenetic analysis, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Bacillus tropicus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | the enzyme-substrate reaction kinetic studies show the allosteric nature of the enzyme and follow pre-steady state using NADH as a co-substrate. Steady-state kinetics | Bacillus tropicus |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | activates | Bacillus tropicus |  |
| Fe2+ | activates by 63.3% | Bacillus tropicus | |
| Fe3+ | the catalytic active site of the enzyme has a Fe metal ion-binding centre in contact with residues His124, Glu125, His129 and Glu214. Fe3+ does not activate the enzyme activity | Bacillus tropicus | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| pentachlorophenol + NADH + H+ + O2 | Bacillus tropicus | - |
2,3,5,6-tetrachloro-1,4-benzoquinone + NADP+ + chloride + H2O | - |
? | |
| pentachlorophenol + NADH + H+ + O2 | Bacillus tropicus AOA-CPS1 | - |
2,3,5,6-tetrachloro-1,4-benzoquinone + NADP+ + chloride + H2O | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus tropicus | - |
- |
- |
| Bacillus tropicus AOA-CPS1 | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Bacillus tropicus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | enzyme CpsB from Bacillus tropicus reacts with PCP to trap 1,4-tetrachlorobenzoquinone (Tet-CBQ) formed as 2,3,5,6-tetrakis[(2-hydroxyethyl)thio]-1,4-hydroquinone (THTH) | Bacillus tropicus | ? | - |
? | |
| additional information | enzyme CpsB from Bacillus tropicus reacts with PCP to trap 1,4-tetrachlorobenzoquinone (Tet-CBQ) formed as 2,3,5,6-tetrakis[(2-hydroxyethyl)thio]-1,4-hydroquinone (THTH) | Bacillus tropicus AOA-CPS1 | ? | - |
? | |
| pentachlorophenol + NADH + H+ + O2 | - |
Bacillus tropicus | 2,3,5,6-tetrachloro-1,4-benzoquinone + NADP+ + chloride + H2O | - |
? | |
| pentachlorophenol + NADH + H+ + O2 | - |
Bacillus tropicus AOA-CPS1 | 2,3,5,6-tetrachloro-1,4-benzoquinone + NADP+ + chloride + H2O | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | 1 * 64000, SDS-PAGE | Bacillus tropicus |
| additional information | the predicted enzyme secondary structure comprises 290 residues of betaalphabeta motifs, 2 beta-sheets, 1 beta-hairpins, 6 strands, 15 alpha-helixes, 24 helix-helix interactions and 25 beta-turns | Bacillus tropicus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GM610_18120 | locus name | Bacillus tropicus |
| PCP 4-monooxygenase | - |
Bacillus tropicus |
| PCP-4-monooxygenase | - |
Bacillus tropicus |
| PcpB | - |
Bacillus tropicus |
| Phe4MO | - |
Bacillus tropicus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
- |
Bacillus tropicus |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 60 | optimum activity at 30°C, about 60% of maximal activity at 60°C | Bacillus tropicus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | 30 | purified enzyme, 180 min, 90% activity remaining | Bacillus tropicus |
| 40 | - |
purified enzyme, 180 min, 80% activity remaining | Bacillus tropicus |
| 50 | - |
purified enzyme, 180 min, 65% activity remaining | Bacillus tropicus |
| 60 | - |
purified enzyme, 180 min, 20% activity remaining | Bacillus tropicus |
| 70 | - |
purified enzyme, 180 min, no activity remaining | Bacillus tropicus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
- |
Bacillus tropicus |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 11.5 | 10% of maximal activity at pH 5.0, 25% of maximal activity at pH 6.0, about 10% of maximal activity at pH 11.5, inactive at at pH 12-13 | Bacillus tropicus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NADH | - |
Bacillus tropicus | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme belongs to the Bacillus cereus group in the Phe4MO superfamily, sequence comparisons and phylogenetic analysis | Bacillus tropicus |
| metabolism | the first step in the PCP degradation pathway is the rate-limiting step involving the hydroxylation of PCP to 1,4-tetrachlorobenzoquinone (Tet-CBQ). The reaction is catalysed by the enzyme PCP 4-monooxygenase (PcpB) in bacteria and cytochrome p450 monooxygenase in fungus. Phe4MO also plays a critical role in xenobiotic compound degradation and lipid metabolism | Bacillus tropicus |
| additional information | enzyme homology structure modeling using PDB IDs 4Q3W and 4JPY individually as templates, overview. The catalytic active site of the enzyme has a Fe3+ metal ion-binding centre in contact with residues His124, Glu125, His129 and Glu214 | Bacillus tropicus |
| physiological function | efficient degradation of pentachlorophenol (PCP) and involvement of different genes and enzymes in the degradation pathway in Bacillus tropicus strain AOA-CPS1 | Bacillus tropicus |
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