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Query: KEGG:D02011 (FAD)
 5,530 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Quinones constituting the electron transfer systems in a marine unicellular diatom, Phaeodactylum tricornutum, were isolated and identified chromatographically. The alga contained five quinones, i.e., plastoquinone A, plastoquinone C, plastoquinone D, alpha-tocopherylquinone, and ubiquinone-9. Other types of quinones, such as vitamin K1, were not detected. The contents of plastoquinone A, plastoquinone C, plastoquinone D, ubiquinone-9, and alpha-tocopherylquinone were 25.5, 4.95, 1.99, 4.78, and 0.28 mmol per mol of chlorophyll, respectively. The contents of the soluble C-type cytochromes, cytochrome c-550 and cytochrome c-553, were 2.15 and 4.34 mmol (heme basis) per mol of chlorophyll, respectively. The amount of B-type cytochrome in the bound form was estimated to be 3.24 mmol (heme basis) per mol of chlorophyll. The acid-soluble flavins, FAD and FMN, were present in amounts of 0.68 and 0.41 mmol per mol of chlorophyll, respectively.
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PMID:Studies on electron transfer systems in the marine diatom Phaeodactylum tricornutum. II. Identification and determination of quinones, cytochromes, and flavins. 67 Jan 58

The metabolism of flavins in mouse was studied with [F-(2)-14C, A-(2,8)-14C]FAD and [F-(2)-14C, 32P]FMN. Ninety minutes after injection, radioactive isoalloxazine nucleus of double-labeled FAD was markedly incorporated into FAD, FMN and riboflavin in the liver, whereas a small amount of radioactive adenine nucleus of double-labeled FAD was found in FAD in the liver. In the case of FMN, radioactive isoalloxazine nucleus of double-labeled FMN was markedly incorporated into FAD, FMN and riboflavin in the liver, whereas only a minute amount of radioactive phosphorus was incorporated into FMN and FAD in the same organ. These results indicate that FMN and FAD injected are rapidly hydrolyzed and resynthesized in animal body.
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PMID:Metabolism of injected flavins studied by using double-labeled [14C]flavin adenine dinucleotide and [14C, 32P]flavin mononucleotide. 73 34

The kinetic properties and regulation of activity of GTP-cyclohydrolase, the enzyme of the first step of flavinogenesis in the Pichia guilliermondii yests, partially purified by gel-filtration were studied. It was found that the curve of the dependence of reaction rate on substrate concentration is non-hyperbolic. FAD inhibited the enzyme activity, while riboflavin and FMN had no such effect. In addition to FAD, 5'-AMP, 3',5'-AMP, ADP, ATP, NAD and NADP inhibited the enzyme activity. Under combined action of FAD and AMP on GTP-cyclohydrolase no synergetic or antagonistic effects of the inhibitors on the enzyme activity were observed. The enzyme appreciably lost its sensitivity to FAD and AMP after thermal treatment. The data obtained suggest that GTP-cyclohydrolase from P. guilliermondii is an allosteric enzyme, which is inhibited by the end product of flavinogenesis FAD, as well as by other 5'-AMP-containing nucleotides.
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PMID:[Regulation of the activity of GTP-cyclohydrolase, the enzyme of the first step of flavinogenesis in yeasts]. 73 22

The process, by which FAD is attached covalently to the 6-hydroxy-D-nicotine oxidase apoprotein in D-nicotine-induced cells of Arthrobacter oxidans was studied in vitro. [3H]Adenine-labelled FAD prepared biosynthetically in Clostridium kluyveri was incorporated into the 6-hydroxy-D-nicotine oxidase molecule during cell-free translation. FAD rather than FMN or riboflavin was thus shown to be the flavin derivative transferred to the polypeptide chain. After short-term protein synthesis on ribosomes from induced A. oxidans cells in the presence of an Escherichia coli MRE 600 supernatant fraction and [adenine-2-3H]FAD, THE PEPTIDYL-TRNA fraction was separated from completed polypeptides. Labelled FAD was found to be covalently attached to the tRNA-bound polypeptides. Cleavage of the tRNA-peptide bond released labelled polypeptides the largest of which migrated as authentic 6-hydroxy-D-nicotine oxidase during dodecylsulfate/polyacrylamide gel electrophoresis. These results strongly suggest that FAD is incorporated into the nascent polypeptide chains of 6-hydroxy-D-nicotine oxidase during ribosomal translation.
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PMID:FAD is covalently attached to peptidyl-tRNA during cell-free synthesis of 6-hydroxy-D-nicotine oxidase. 73 74

Lumiflavin and lumichrome both inhibit the growth of different strains of Bacillus subtilis including riboflavin-constitutive mutant. Lumiflavin has no regulating effect, but lumichrome is an effector and it participates in the repression of riboflavin precursors synthesis and the synthesis of riboflavinsynthetase. Mutants resistant to lumiflavin or lumichrome accumulate a mixture of riboflavin, FMN and FAD. Their regulatory characteristics are substantially altered. They are repressed by higher concentrations of all effectors comparing with the wild type. The mapping of resistant mutants showed that the most of them are located near to ribC gene, probably inside of it. The simultaneous presence of all three flavins in the cultural medium shows that the regulatory protein is universal to the biosynthesis of all flavins.
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PMID:[Operon of riboflavin synthesis in Bacillus subtilis. IX. Preparation and properties of lumiflavin- or lumichrome-resistant mutants]. 81 36

Microorganisms formed readily ethylenethiourea (ETU) from 5,6-dihydro-3H-imidazo[2,1-c]-1,2,4-dithiazole-3-thione (DIDT), a spontaneous decomposition product of ethylenebisdithiocarbamates. This conversion also takes place after addition of reducing compounds like cysteine, glutathione or ascorbic acid. It consists of two steps: reduction of the S-S bond of DIDT with subsequent release of CS2 to form ETU. DIDT was reduced by NADH in the presence of enzyme extracts from Pseudomonas fluorescens or Asperigillus niger, or by commercial glutathione reductase or lipoamide dehydrogenase. ETU was formed as a result of this enzymatic reduction. The flavin compounds FMN and FAD were also able to promote the reduction of DIDT by NADH.
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PMID:Formation of ethylenethiourea from 5,6-dihydro-3H-imidazo[2,1-c]-1,2,4-dithiazole-3-thione by microorganisms and reducing agents. 81 82

NADPH-cytochrome c (cytochrome P-450) reductase (EC 1.6.2.4) has been purified to homogeneity, as judged by sodium dodecyl sulfate disc gel electrophoresis, from detergent-solubilized rat and pig liver microsomes using an affinity chromatography procedure. Treatment of microsomes with a polyethoxynonylphenyl ether plus either cholate or deoxycholate and subsequent batch-wise DEAE-cellulose chromatography followed by biospecific affinity chromatography on Sepharose 4B-bound N6-(6-aminohexyl)-adenosine 2',5'-bisphosphate (2'5'-ADP-Sepharose 4B) result in a greater than 30% yield of purified reductase from microsomes. The enzyme contains 1 mol each of FAD and FMN and exhibits a molecular weight of 78,000 g mol-1 estimated by comparison with protein standards on sodium dodecyl sulfate polyacrylamide gel electrophoresis. The turnover numbers calculated on the basis of flavin are 1360 min-1 and 1490 min-1 at 25 degrees for the pig and rat liver enzymes, respectively. Titration of these purified preparations aerobically with both NADPH and potassium ferricyanide demonstrated unequivocally that the air-stable, reduced form of NADPH-cytochrome c (P-450) reductase contains 2 electron equivalents, confirming recent results obtained by Masters et al. (Masters, B. S. S., Prough, R. A., and Kamin, H. (1975) Biochemistry 14, 607-613) for the proteolytically solubilized enzyme. In addition, these preparations are capable of reconstituting benzphetamine N-demethylation activity in the presence of partially purified cytochrome P-450 and dilauroylphosphatidylcholine, as measured by formaldehyde formation from benzphetamine.
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PMID:Some properties of a detergent-solubilized NADPH-cytochrome c(cytochrome P-450) reductase purified by biospecific affinity chromatography. 82 51

The incorporation of radioactivity derived from [2-14C] riboflavin into the flavins of rat liver mitochondrial outer membranes was studied. These membranes were found to contain about 0.6 nmol of non-covalently bound flavins per mg protein; the majority is in the form of FAD (73%) and FMN (24%). The membranes also contain about 1.5 nmol per mg of covalently bound flavins. After labeling, radioactive flavins appeared in the non-covalently bound flavins for about 4 h. Most of this radioactivity was in FAC (77%). Neither the rate nor extent of this labeling was affected by cycloheximide (1 mg/kg) administered 30 min prior to the radioactive riboflavin. With the covalently bound flavins, radioactivity was incorporated into the coenzymes for at least 18 h, but the rate of incorporation was much slower. After cycloheximide, radioactive flavins continued to appear in covalently bound flavins for about 2 h, but then stopped. Labeling of both types of flavins after [14C] riboflavin was considerably slower than the incorporation of [3H] leucine into outer membrane proteins. These results suggest that with flavoproteins from the mitochondrial outer membranes, the incorporation of flavins occurs after synthesis of the various apoenzymes is complete.
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PMID:Studies on the flavins in rat liver mitochondrial outer membranes. 87 72

Changes in glucose levels in blood, excretion of riboflavine in urine, FAD and FMN flavinic nucleotides and a total riboflavine content in liver homogenates were determined in rats. Both riboflavine deficiency and atebrine do not effect the glucose, blood levels. Atebrine (ATB) significantly inhibits the urinary excretion of riboflavine both in deficiency state and in satisfied demand of this vitamin. The lack of riboflavine in food results in a decrease of total riboflavine and FA- in liver, while during the first period of deficiency the amount of FMN increases. When the riboflavine demand is satisfied, low doses of ATP do not influence the total riboflavine and flavinic nucleotides content in the liver, while at high doses, the total riboflavine increases and the amount of FMN initially significantly exceeds the amount of FAD. ATB markedly inhibits the growth of rats both in the deficiency state and in the satisfied demand of riboflavine.
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PMID:Effect of atebrine on glucose blood levels and on flavinic nucleotides content in rat liver in deficiency state and in satisfied demand of riboflavine. 87 Aug 88

The quantity of FAD and FMN in mitochondria isolated from the liver of albino rats was determined before and after application of ultrasonic energy with the intensities 0,2,0,6 and 1,0 w/cm2 in a short-term test, and the intensity 0,2 w/cm2 applied at ten successive days in a long-term test. The total amount of the two coenzymes as well as their percentages were ascertained. The following results derive from our experiments: 1. A quantitative increase of FAD in liver mitochondria. This suggests that the capacity of the shortened respiratory chain has increased, since redox systems represent a factor determining its stage. 2. The flavine-mononucleotide responds to ultrasonics as a relatively instable biological macromolecule. 3. The total amount of flavine coenzymes is influenced especially by the quantity of FAD, and, correspondingly, by changes of the latter.
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PMID:[The influence of biophysical factors on biological oxidation and redox processes. 16. The possibility of influencing flavine coenzymes in liver mitochondria by means of ultrasonic treatment (author's transl)]. 89 14


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