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Literature summary for 1.7.1.6 extracted from
- Novel biochemical properties and physiological role of the flavin mononucleotide oxidoreductase YhdA from Bacillus subtilis (2020), Appl. Environ. Microbiol., 86, e1688-20 .
Application
| Application | Comment | Organism |
|---|---|---|
| environmental protection | anthropogenic activity has converted chromium (Cr), an element found in rocks, soils, plants, and animals, into a dangerous environmental pollutant. The activity of the pure oxidoreductase YhdA can be used for efficient bioremediation of Cr(VI) | Bacillus subtilis |
| additional information | health protection, the activity of the pure oxidoreductase YhdA can be used for efficient bioremediation of Cr(VI), it counteracts the cytotoxic and genotoxic effects of oxygen radicals induced by intracellular factors and those generated during reduction of hexavalent chromium. Oxidoreductases that possess the ability to reduce Cr(VI) to Cr(III), avoiding the intermediates Cr(V) and Cr(IV), are of significant biotechnological value | Bacillus subtilis |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene yhdA, recombinant overexpression of His10-tagged enzyme in Escherichia coli strain Rosetta (DE3) | Bacillus subtilis |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 7.26 | - |
Cr(VI) | pH 7.5, 30°C, recombinant His10-tagged enzyme | Bacillus subtilis |  |
| 37.3 | - |
NADPH | pH 7.5, 30°C, recombinant His10-tagged enzyme | Bacillus subtilis | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Cibacron Marine dye + NADPH + H+ | Bacillus subtilis | reductive degradation | ? + NADP+ | - |
r | |
| Cr(VI) + NADPH + H+ | Bacillus subtilis | - |
Cr(III) + NADP+ | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus subtilis | O07529 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Cibacron Marine dye + NADPH + H+ | reductive degradation | Bacillus subtilis | ? + NADP+ | - |
r | |
| Cr(VI) + NADPH + H+ | - |
Bacillus subtilis | Cr(III) + NADP+ | - |
r | |
| additional information | YhdA is characterized as an enzyme with azoreductase activity. The pure recombinant His10-YhdA protein efficiently catalyzes the reduction of Cr(VI) employing NADPH as a cofactor. The oxidoreductase possess the ability to reduce Cr(VI) to Cr(III), avoiding the intermediates Cr(V) and Cr(IV). The purified recombinant His10-YhdA protein displays a strong NADP(H)-dependent chromate reductase activity, overview | Bacillus subtilis | ? | - |
- |
|
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 20000, about, recombinant His10-tagged enzyme, SDS-PAGE | Bacillus subtilis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| azo-reductase | - |
Bacillus subtilis |
| BsuYhdA | - |
Bacillus subtilis |
| flavin mononucleotide oxidoreductase | - |
Bacillus subtilis |
| More | see also EC 1.6.5.2 | Bacillus subtilis |
| NADPH-dependent flavin mononucleotide oxide reductase | - |
Bacillus subtilis |
| YhdA | - |
Bacillus subtilis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
recombinant enzyme | Bacillus subtilis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
recombinant enzyme | Bacillus subtilis |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FMN | YhdA uses NADPH as the electron donor to reduce the active-site FMN | Bacillus subtilis | |
| additional information | YhdA uses NADPH as the electron donor to reduce the active-site FMN. No activity with NADH | Bacillus subtilis | |
| NADP+ | - |
Bacillus subtilis | |
| NADPH | - |
Bacillus subtilis | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the Bacillus subtilis YhdA enzyme belongs to the family of NADPH-dependent flavin mononucleotide oxide reductases and possesses azo-reductase activity. YhdA possesses structural homology with chromate reductases (cf. EC 1.6.5.2), amino acid homology to the two bona fide chromate reductases YieF and ChrR from Escherichia coli and Pseudomonas putida, respectively, with the signature sequence LFVTPEYNXXXXXXLKNAIDXXS, sequence comparisons, overview | Bacillus subtilis |
| physiological function | the bacterial flavin mononucleotide/NADPH-dependent oxidoreductase YhdA, widely distributed among Gram-positive bacilli, confers protection to cells from the cytotoxic effects of Cr(VI) and prevents the hypermutagenesis exhibited by a MutT/MutM/MutY-deficient strain. Additionally, a purified recombinant His10-YhdA protein displays a strong NADPH-dependent chromate reductase activity. In bacterial cells, YhdA counteracts the cytotoxic and genotoxic effects of intracellular and extracellular inducers of oxygen radicals, including those caused by hexavalent chromium. The enzyme upon overexpression confers protection on Bacillus subtilis from the cytotoxic effects promoted by Cr(VI) and counteracts the mutagenic effects of the reactive oxygen species (ROS)-promoted lesion 8-oxoguanine (8-OxoG). YhdA prevents the formation of mutations in Bacillus subtilis, mainly those that are increased in the absence of systems that repair 8-OxoG lesions | Bacillus subtilis |
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