[PDF] Structure and function of YcnD from Bacillus subtilis, a flavin-containing oxidoreductase. | Semantic Scholar (2024)

The gene yhdA from Bacillus subtilis encoding a putative flavin mononucleotide (FMN)-dependent oxidoreductase was cloned and heterologously expressed in Escherichia coli, and it was demonstrated that the dye is a competitive inhibitor of NADPH and FMN.

It is demonstrated that a monofunctional chorismate synthase confers prototrophy in conjunction with a NADPH:  FMN oxidoreductase indicating that bifunctionality is required due to the lack of free reduced FMN in fungal and possibly protozoan species.

Characteristics suggest that the nitroreductase Gox0834 may be a possible candidate for catalyzing prodrug activation, bioremediation, or biocatalytic processes.

CinD is thus a nitroreductase which can protect L. lactis against oxidative stress that could be exerted by nitroaromatic compounds and copper.

CinD is thus a nitroreductase which can protect L. lactis from oxidative stress and is addressed here the function of one of these genes, ytjD, which is renamed cinD (copper-induced nit mirroreductase).

M mammalian quinone reductases emerge as central molecular switches that control the lifespan of transcription factors and hence participate in the development of apoptosis and cell transformation, suggesting a role beyond detoxication of quinones and involvement in the oxygen stress response.

It is demonstrated unambiguously that oleate hydratase from Lactobacillus rhamnosus ATCC 53103 is a FADH2-dependent enzyme by means of two different biochemical processes.

These enzymes (or their corresponding genes) could be used as biomarkers to predict the capacity of ecosystems to transform mesotrione and assess their contamination by both the parent molecule and/or the metabolites.

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Findings indicate that the rates of NADPH and NADP(+) dissociation in relation to the isotope-sensitive redox steps were both increased as a result of the mutation, and provide support to the critical role of the Arg203 in the specific recognition and binding of NAD PH.

The ipa-43d protein was found to be tightly associated with FMN and to be capable of reducing both nitrofurazone and FMN effectively and changed to the sequential mechanism upon coupling with the bioluminescent reaction.

NADPH-dependent flavin reductase (required for the activation of chorismate synthase) was purified to hom*ogeneity from cell-free extracts of Bacillus subtilis and the enzyme complex has the same catalytic properties as the dissociated enzyme except that it requires both a divalent metal ion and FMN for DCIP reduction.

It was shown that luciferase formed a complex at 1:1 molar ratio with the monomer of either the apoenzyme or the holoenzyme form of FRP with K(d) values of 7 and 11 microM, respectively.

Data indicate that the acpDgene product is not acyl carrier protein phosphodiesterase but an azoreductase, and that the gene product could not convert holo-acyl carrier protein into the apo form under either in vitro or in vivo conditions.

The structure of an NADPH:FMN oxidoreductase (flavin reductase P) that is involved in bioluminescence by providing reduced FMN to luciferase is reported and a model for how flavin reduct enzyme P might shuttle electrons between NADPH and luciferases is proposed.

This is the first report describing the sequencing and characterization of a gene encoding the azo dye-reducing enzyme, azoreductase, from aerobic bacteria and its expression in E. coli.

The crystal structure of FRase I, the major NAD(P)H:FMN oxidoreductase of Vibrio fischeri, is solved by the multiple isomorphous replacement method (MIR), which shows that most of the exposed re-face of the FMN cofactor is buried, which is consistent with the ping pong bi bi catalytic mechanism.

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