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 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 | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-hydroxybenzoate + NADPH + H+ + O2 | Cupriavidus pinatubonensis | - |
3,4-dihydroxybenzoate + NADP+ + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Cupriavidus pinatubonensis | Q46U22 | Cupriavidus necator or Ralstonia eutropha | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-hydroxybenzoate + NADPH + H+ + O2 | - |
Cupriavidus pinatubonensis | 3,4-dihydroxybenzoate + NADP+ + H2O | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | PHBH and related enzymes lack a canonical NAD(P)H-binding domain | Cupriavidus pinatubonensis |
Synonyms | Comment | Organism |
---|---|---|
p-hydroxybenzoate hydroxylase | - |
Cupriavidus pinatubonensis |
PHBH | - |
Cupriavidus pinatubonensis |
PHBHCn2 | - |
Cupriavidus pinatubonensis |
Reut_B4006 | - |
Cupriavidus pinatubonensis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Cupriavidus pinatubonensis |
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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Cupriavidus pinatubonensis |
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 | 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 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 |