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Literature summary extracted from

  • Valenzuela-Garcia, L.I.; Zapata, B.L.; Ramirez-Ramirez, N.; Huchin-Mian, J.P.; Robleto, E.A.; Ayala-Garcia, V.M.; Pedraza-Reyes, M.
    Novel biochemical properties and physiological role of the flavin mononucleotide oxidoreductase YhdA from Bacillus subtilis (2020), Appl. Environ. Microbiol., 86, e1688-20 .
    View publication on PubMed

Application

EC Number Application Comment Organism
1.7.1.6 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
1.7.1.6 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)

EC Number Cloned (Comment) Organism
1.7.1.6 gene yhdA, recombinant overexpression of His10-tagged enzyme in Escherichia coli strain Rosetta (DE3) Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.7.1.6 7.26
-
 Cr(VI) pH 7.5, 30°C, recombinant His10-tagged enzyme Bacillus subtilis
1.7.1.6 37.3
-
 NADPH pH 7.5, 30°C, recombinant His10-tagged enzyme Bacillus subtilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.7.1.6 Cibacron Marine dye + NADPH + H+ Bacillus subtilis reductive degradation ? + NADP+
-
 r
1.7.1.6 Cr(VI) + NADPH + H+ Bacillus subtilis
-
 Cr(III) + NADP+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.7.1.6 Bacillus subtilis O07529
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.1.6 Cibacron Marine dye + NADPH + H+ reductive degradation Bacillus subtilis ? + NADP+
-
 r
1.7.1.6 Cr(VI) + NADPH + H+
-
 Bacillus subtilis Cr(III) + NADP+
-
 r
1.7.1.6 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

EC Number Subunits Comment Organism
1.7.1.6 ? x * 20000, about, recombinant His10-tagged enzyme, SDS-PAGE Bacillus subtilis

Synonyms

EC Number Synonyms Comment Organism
1.7.1.6 azo-reductase
-
 Bacillus subtilis
1.7.1.6 BsuYhdA
-
 Bacillus subtilis
1.7.1.6 flavin mononucleotide oxidoreductase
-
 Bacillus subtilis
1.7.1.6 More see also EC 1.6.5.2 Bacillus subtilis
1.7.1.6 NADPH-dependent flavin mononucleotide oxide reductase
-
 Bacillus subtilis
1.7.1.6 YhdA
-
 Bacillus subtilis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.7.1.6 30
-
 recombinant enzyme Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.7.1.6 7.5
-
 recombinant enzyme Bacillus subtilis

Cofactor

EC Number Cofactor Comment Organism Structure
1.7.1.6 FMN YhdA uses NADPH as the electron donor to reduce the active-site FMN Bacillus subtilis
1.7.1.6 additional information YhdA uses NADPH as the electron donor to reduce the active-site FMN. No activity with NADH Bacillus subtilis
1.7.1.6 NADP+
-
 Bacillus subtilis
1.7.1.6 NADPH
-
 Bacillus subtilis

General Information

EC Number General Information Comment Organism
1.7.1.6 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
1.7.1.6 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