Contains FMN. The enzyme can utilize NADH and NADPH with similar reaction rates. Different from EC 1.5.1.42, FMN reductase (NADH) and EC 1.5.1.38, FMN reductase (NADPH). The luminescent bacterium Vibrio harveyi possesses all three enzymes . Also reduces riboflavin and FAD, but more slowly.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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SYSTEMATIC NAME
IUBMB Comments
FMNH2:NAD(P)+ oxidoreductase
Contains FMN. The enzyme can utilize NADH and NADPH with similar reaction rates. Different from EC 1.5.1.42, FMN reductase (NADH) and EC 1.5.1.38, FMN reductase (NADPH). The luminescent bacterium Vibrio harveyi possesses all three enzymes [1]. Also reduces riboflavin and FAD, but more slowly.
the enzyme has a hemin binding activity, pronbably in the hydrophobic pocket near loops beta4-alpha5 and beta8-beta9, docking of biliverdin IXalpha and FMN , overview
ChuY has flavin mononucleotide (FMN) reductase activity, using NAD(P)H as a cofactor, and shows porphyrin ring binding affinity. ChuY acts as a reductase in heme homeostasis to maintain the virulence potential of Escherichia coli strain CFT073
ChuY has flavin mononucleotide (FMN) reductase activity, using NAD(P)H as a cofactor, and shows porphyrin ring binding affinity. ChuY acts as a reductase in heme homeostasis to maintain the virulence potential of Escherichia coli strain CFT073
the two molecules in the asymmetric unit are related by pseudo 2fold rotation symmetry. ChuY contains six alpha-helices and ten beta-strands. A central beta-sheet, consisting of seven parallel beta-strands, beta1, beta2, beta3, beta4, beta5, beta6, and beta10, is flanked by six alpha-helices, forming alternating beta-strand and alpha-helix repeats, which is a representative feature of Rossmann folds. Three other beta-strands (beta7-beta9) are located on the top of the beta-sheet
the two molecules in the asymmetric unit are related by pseudo 2fold rotation symmetry. ChuY contains six alpha-helices and ten beta-strands. A central beta-sheet, consisting of seven parallel beta-strands, beta1, beta2, beta3, beta4, beta5, beta6, and beta10, is flanked by six alpha-helices, forming alternating beta-strand and alpha-helix repeats, which is a representative feature of Rossmann folds. Three other beta-strands (beta7-beta9) are located on the top of the beta-sheet
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged enzyme, using 0.1 M Bis-Tris, pH 6.5, 50 mM CaCl2, and 30% PEG MME 550 as precipitants, ChuY crystals belong to the primitive monoclinic space group P21 with two molecules forming an asymmetric unit, multi-wavelength anomalous dispersion, using a SeMet-labeled crystal at a resolution of 2.4 A
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene chuY, encoded in the chu gene cluster of strain CFT073, recombinant expression as His-tagged enzyme in Escherichia coli, complementation of an Escherichia coli chuY-knockout strain with expression of the wild-type gene
enzyme ChuY is a potential target for the development of antibacterial or antivirulence drugs to combat not only UPEC but a broad range of pathogenic bacteria that contain chuY system or its orthologue, ranging from Vibrio to staphylococcal species
enzyme ChuY is a potential target for the development of antibacterial or antivirulence drugs to combat not only UPEC but a broad range of pathogenic bacteria that contain chuY system or its orthologue, ranging from Vibrio to staphylococcal species