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Results 1 - 10 of 11 > >>
EC Number General Information Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.36evolution in many luminous species (i.e. Aliivibrio fischeri, Photorhabdus luminescens, and others) not only LuxG, but also Fre-like oxidoreductases are found. Probably, they are not involved in the regulation of bioluminescence in vivo except for in Photorhabdus species which lack luxG gene and apparently compensate oxidoreductase activity by Fre. Phylogenetic analysis, sequence comparisons, and reconstruction of phylogenetic tree. The enzyme belongs to the FNR superfamily. The determined specific residues can play a significant role in the division of oxidoreductases into Fre and LuxG subfamily and the mechanisms of their functioning 765735
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.36evolution SMOB-ADP1 belongs to the flavin reductases of the HpaC-like subfamily. NAD(P)H:flavin oxidoreductase structure comparisons, overview 741794
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.36malfunction deletion of the encoding genes genes nfr1 and nfr2 in Lactobacillus johnsonii leads to a 40fold reduction of hydrogen peroxide formation. H2O2 production in this mutant can only be restored by in trans complementation of both genes -, 741680
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.36malfunction inhibition of Nox causes a noticeable decrease in the microsclerotium yields. Silencing of Nox decreases the microsclerotium yield by 98.5%, H2O2 and virulence decrease it by 38% and 21.5%, respectively -, 743891
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.36metabolism in many luminous species (i.e. Aliivibrio fischeri, Photorhabdus luminescens, and others) not only LuxG, but also Fre-like oxidoreductases are found. LuxG enzymes are able to reduce FMN, FAD, and riboflavin with comparable efficiency, whereas for Fre oxidoreductases FAD is a preferred substrate 765735
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.36more enzyme structure modelling and structure comparisons. The difference in affinity to flavins could be partly attributed to the absence of the Arg46 in the structure of LuxG. This residue forms a conserved Arg46-Pro47-Phe48-Ser49 segment characteristic to all Fre oxidoreductases as well as to the members of FNR family, but not to LuxG oxidoreductases 765735
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.36more His160 and Arg38 contribute to the catalytic activity and the pH dependence 764038
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.36more stabilizing effect of another Paracoccus denitrificans protein, the NAD(P)H:acceptor oxidoreducase FerB, against spontaneous oxidation of the FerA-produced dihydroflavin. The turnover rate for NADH oxidation initiated by the addition of FMN is comparable to that for the native, untagged FerA, indicating that the His tag does not interfere with catalysis. Enzyme active ite structure analysis, overview -, 743241
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.36physiological function the 4-hydroxyphenylacetate 3-monooxygenase from Escherichia coli W is a two-component enzyme encoded by the hpaB and hpaC genes and catalyzes the initial reaction in the degradation of 4-hydroxyphenylacetate, i.e., the introduction of a second hydroxyl group into the benzene nucleus at a position ortho to the existing hydroxyl group, giving rise to 3,4-dihydroxyphenylacetate 438899
Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.36physiological function the conserved NADH-dependent flavin reductase is prominently involved in H2O2 production in Lactobacillus johnsonii, overview -, 741680
Results 1 - 10 of 11 > >>