Mostrando 17,101 - 17,120 Resultados de 20,270 Para Buscar 'Flavina~', tiempo de consulta: 2.96s Limitar resultados
  1. 17101
    “…Riboflavin (vitamin B2) is the precursor of flavin mononucleotide (FMN) and flavin adenine dinucleotide, which are essential coenzymes in all free-living organisms. …”
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  2. 17102
  3. 17103
    “…The concentrations of ferulic acid and hydroxysafflor flavin A in Taohongsiwu decoction were 0.12 and 0.57 mg/ml, respectively. …”
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  4. 17104
    “…Enzymes known as bifunctional and bimodular prokaryotic type-I FAD synthetase (FADS) exhibit ATP:riboflavin kinase (RFK) and FMN:ATP adenylyltransferase (FMNAT) activities in their C-terminal and N-terminal modules, respectively, and produce flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD). …”
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  5. 17105
  6. 17106
    “…Human flavin-containing monooxygenase 3 (hFMO3) catalyses the oxygenation of a wide variety of compounds including drugs as well as dietary compounds. …”
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  7. 17107
    “…Dihydroorotate dehydrogenase (DHODH) is a flavin‐binding enzyme essential for pyrimidine biosynthesis, which converts dihydroorotate to orotate. …”
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  8. 17108
    “…Two amino acid sequence motifs, a flavin adenine dinucleotide-binding domain and a flavin-containing amine oxidoreductase, were highly conserved in SpAMO. …”
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  9. 17109
    “…Structural and enzymatic analyses indicate that Osm1 has a specific binding pocket for flavin molecules, including FAD, FMN, and riboflavin, catalyzing their oxidation while reducing fumarate to succinate. …”
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  10. 17110
  11. 17111
    “…Human triokinase/flavin mononucleotide (FMN) cyclase (hTKFC) catalyzes the adenosine triphosphate (ATP)-dependent phosphorylation of D-glyceraldehyde and dihydroxyacetone (DHA), and the cyclizing splitting of flavin adenine dinucleotide (FAD). hTKFC structural models are dimers of identical subunits, each with two domains, K and L, with an L2-K1-K2-L1 arrangement. …”
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  12. 17112
    “…[Image: see text] Algae, plants, bacteria, and fungi contain flavin-binding light-oxygen-voltage (LOV) domains that function as blue light sensors to control cellular responses to light. …”
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  13. 17113
    “…Surprisingly, dCRY appears to mediate red-light–evoked depolarization in wild-type flies, absent in both cry-null flies, and following acute treatment with the flavin-specific inhibitor diphenyleneiodonium in wild-type flies. …”
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  14. 17114
    “…The typical and conservative motifs, including the flavin adenine dinucleotide (FAD)-binding motif and flavin-containing monooxygenases (FMO)-identifying sequence, existed in the gene structures. …”
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  15. 17115
    “…RESULTS: In order to test the performance of the proposed deep-based system, eight different plant datasets were used: Flavia, Swedish, ICL, Foliage, Folio, Flower17, Flower102, and LeafSnap. …”
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  16. 17116
    “…Here, we uncovered that the bacterial thymidylate synthase ThyX, which relies on both folate and flavin for activity, can also use a formaldehyde-shunt to directly synthesize thymidylate. …”
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  17. 17117
    por Willetts, Andrew
    Publicado 2021
    “…However, following that auspicious beginning, the biochemistry of EC 1.14.14.108, and its isoenzymic partner 3,6-diketocamphane 1,6-monooxygenase (EC 1.14.14.155) was dogged for many years by the mistaken belief that the enzymes were true flavoproteins that function with a tightly-bound flavin cofactor in the active site. This misconception led to a number of erroneous interpretations of relevant experimental data. …”
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  18. 17118
    “…The cellular spatial distribution of de novo lipogenesis, new protein synthesis, NADH, Flavin, unsaturated lipids, and saturated lipids were all imaged and quantified in this experiment. …”
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  19. 17119
    “…The computational analysis results allowed us to rationalize some of the available spectroscopic data regarding ligand-induced conformational changes leading to an increase in the flavin adenine dinucleotide (FAD) solvent-exposed surface, which has been previously correlated with the formation of complexes with electron acceptors.…”
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  20. 17120
    “…A sulfoquinovosidase hydrolyzes the SQ glycoside and the liberated SQ is acted on by a flavin mononucleotide-dependent sulfoquinovose monooxygenase, in concert with an NADH-dependent flavin reductase, to release sulfite and 6-oxo-glucose. …”
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