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Literature summary for 1.14.13.2 extracted from
- Pyridine nucleotide coenzyme specificity of p-hydroxybenzoate hydroxylase and related flavoprotein monooxygenases (2018), Front. Microbiol., 9, 3050 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene Reut_B4006, sequence comparisons and phylogenetic analysis and tree, recombinant expression of the codon-optimized gene in Acinetobacter sp. ADP1 | Cupriavidus pinatubonensis |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0264 | - |
4-hydroxybenzoate | pH 7.5, 30°C, recombinant enzyme PHBHCn2, via UV/VIS-NAD(P)H consumption determination, with NADPH | Cupriavidus pinatubonensis |  |
| 0.0306 | - |
4-hydroxybenzoate | pH 7.5, 30°C, recombinant enzyme PHBHCn2, via product determination per HPLC, with NADPH | Cupriavidus pinatubonensis | |
| 0.146 | - |
NADPH | pH 7.5, 30°C, recombinant enzyme PHBHCn2, via UV/VIS-NAD(P)H consumption determination | Cupriavidus pinatubonensis | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-hydroxybenzoate + NADPH + H+ + O2 | Cupriavidus pinatubonensis | - |
3,4-dihydroxybenzoate + NADP+ + H2O | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Cupriavidus pinatubonensis | Q46U22 | Cupriavidus necator or Ralstonia eutropha | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-hydroxybenzoate + NADPH + H+ + O2 | - |
Cupriavidus pinatubonensis | 3,4-dihydroxybenzoate + NADP+ + H2O | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | PHBH and related enzymes lack a canonical NAD(P)H-binding domain | Cupriavidus pinatubonensis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| p-hydroxybenzoate hydroxylase | - |
Cupriavidus pinatubonensis |
| PHBH | - |
Cupriavidus pinatubonensis |
| PHBHCn2 | - |
Cupriavidus pinatubonensis |
| Reut_B4006 | - |
Cupriavidus pinatubonensis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Cupriavidus pinatubonensis |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 18 | - |
4-hydroxybenzoate | pH 7.5, 30°C, recombinant enzyme PHBHCn2, via UV/VIS-NAD(P)H consumption determination, with NADPH | Cupriavidus pinatubonensis | |
| 30.4 | - |
4-hydroxybenzoate | pH 7.5, 30°C, recombinant enzyme PHBHCn2, via product determination per HPLC, with NADPH | Cupriavidus pinatubonensis | |
| 37 | - |
NADPH | pH 7.5, 30°C, recombinant enzyme PHBHCn2, via UV/VIS-NAD(P)H consumption determination | Cupriavidus pinatubonensis | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Cupriavidus pinatubonensis |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | the enzyme is a flavoprotein | Cupriavidus pinatubonensis | |
| additional information | no activity with NADH | Cupriavidus pinatubonensis | |
| NADPH | PHBH and related enzymes lack a canonical NAD(P)H-binding domain. The enzyme PHBHCn2 is strictly dependent on NADPH and contains the NADPH-preferring sequence motif 32-EQRSPEYVLGR | Cupriavidus pinatubonensis | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | amino acid sequences of NADH-preferring PHBHs of putative PHBHs identified in currently available bacterial genomes, phylogenetic analysis, overview. The pyridine nucleotide coenzyme specificity of PHBH emerged through adaptive evolution, and the NADH-preferring enzymes are the older versions of PHBH. Structural comparison and distance tree analysis of group A flavoprotein monooxygenases indicates that a similar protein segment as being responsible for the pyridine nucleotide coenzyme specificity of PHBH is involved in determining the pyridine nucleotide coenzyme specificity of the other group A members. Evolutionary rate calculation. Among the actinobacterial sequences presently available, most comprise the NADH-preferring fingerprint. However, Mycobacteria have a mixed type motif, often the first or both arginine(s) of the NADH-fingerprint are present but the remaining part is lacking. In addition, many mycobacterial sequences have parts of the NADPH-preferring fingerprint, especially, x(D/E)YVL(G/S)R | Cupriavidus pinatubonensis |
| additional information | energy profiling from enzyme protein structure is realized by means of a coarse-grained residue-level pair potential function modeling, overview | Cupriavidus pinatubonensis |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 253.4 | - |
NADPH | pH 7.5, 30°C, recombinant enzyme PHBHCn2, via UV/VIS-NAD(P)H consumption determination | Cupriavidus pinatubonensis | |
| 681.8 | - |
4-hydroxybenzoate | pH 7.5, 30°C, recombinant enzyme PHBHCn2, via UV/VIS-NAD(P)H consumption determination, with NADPH | Cupriavidus pinatubonensis | |
| 993.5 | - |
4-hydroxybenzoate | pH 7.5, 30°C, recombinant enzyme PHBHCn2, via product determination per HPLC, with NADPH | Cupriavidus pinatubonensis | |
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