FAD

出典: meddic

フラビンアデニンジヌクレオチド flavin adenine dinucleotide

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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2015/06/22 13:57:38」(JST)

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英文文献

  • Insight into the redox partner interaction mechanism in cytochrome P450BM-3 using molecular dynamics simulations.
  • Verma R, Schwaneberg U, Roccatano D.Author information School of Engineering and Science, Jacobs University Bremen, Campus Ring 1, Bremen, 28759, Germany; Department of Biotechnology, RWTH Aachen University, Worringer Weg 1, Aachen, 52074, Germany.AbstractFlavocytochrome P450BM-3 is a soluble bacterial reductase composed of two flavin (FAD/FMN) and one HEME domains. In this article, we have performed molecular dynamics simulations on both the isolated FMN and HEME domains and their crystallographic complex, with the aim to study their binding modes and to garner insight into the interdomain electron transfer (ET) mechanism. The results evidenced an interdomain conformational rearrangement that reduces the average distance between the FMN and HEME cofactors from 1.81 nm, in the crystal structure, to an average value of 1.41 ± 0.09 nm along the simulation. This modification is in agreement with previously proposed hypotheses suggesting that the crystallographic FMN/HEME complex is not in the optimal arrangement for favorable ET rate under physiological conditions. The calculation of the transfer rate along the simulation, using the Pathways Path method, demonstrated the occurrence of seven ET pathways between the two redox centers, with three of them providing ET rates (KET ) comparable with the experimental one. The sampled ET pathways comprise the amino acids N319, L322, F390, K391, P392, F393, A399, C400, and Q403 of the HEME domain and M490 of the FMN domain. The values of KET closer to the experiment were found along the pathways FMN(C7) → F390 → K391 → P392 → HEME(Fe) and FMN(C8) → M490 → F393 → HEME(Fe). Finally, the analysis of the collective modes of the protein complex evidences a clear correlation of the first two essential modes with the activation of the most effective ET pathways along the trajectory. © 2013 Wiley Periodicals, Inc. Biopolymers 101: 197-209, 2014.
  • Biopolymers.Biopolymers.2014 Mar;101(3):197-209. doi: 10.1002/bip.22301.
  • Flavocytochrome P450BM-3 is a soluble bacterial reductase composed of two flavin (FAD/FMN) and one HEME domains. In this article, we have performed molecular dynamics simulations on both the isolated FMN and HEME domains and their crystallographic complex, with the aim to study their binding modes a
  • PMID 23754593
  • Determination of free and bound riboflavin in cow's milk using a novel flavin-binding protein.
  • Koop J, Monschein S, Pauline Macheroux E, Knaus T, Macheroux P.Author information Institute of Biochemistry, Graz University of Technology, A-8010 Graz, Austria.AbstractA recently described putative protease from the gut bacterium Bacteroides thetaiotaomicron (termed ppBat) exhibits two tryptophan residues in the interface which enable specific binding of the isoalloxazine heterocycle of riboflavin and its two cofactor forms, FMN and FAD. Recombinant ppBat was used to capture riboflavin from bovine milk directly without any prior preparation steps. The flavin-loaded protein was then re-isolated by means of affinity chromatography to identify and quantify the captured flavins. Free riboflavin concentrations were determined to 197 and 151μg/l for milk with 3.5% and 0.5% fat content, respectively. Total riboflavin concentrations were also determined after acid-treatment of milk and were 4-5 times higher than for free riboflavin. Free FMN and FAD were not detectable and only trace amounts of FMN were found in milk following acid treatment. The method appears to be amenable to develop a direct assay for free riboflavin in milk and other foods.
  • Food chemistry.Food Chem.2014 Mar 1;146:94-7. doi: 10.1016/j.foodchem.2013.09.026. Epub 2013 Sep 12.
  • A recently described putative protease from the gut bacterium Bacteroides thetaiotaomicron (termed ppBat) exhibits two tryptophan residues in the interface which enable specific binding of the isoalloxazine heterocycle of riboflavin and its two cofactor forms, FMN and FAD. Recombinant ppBat was used
  • PMID 24176318
  • Characterization of Elements Involved in Allosteric Light Regulation of Phosphodiesterase Activity by Comparison of Different Functional BlrP1 States.
  • Winkler A1, Udvarhelyi A2, Hartmann E3, Reinstein J4, Menzel A5, Shoeman RL6, Schlichting I7.Author information 1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany. Electronic address: Andreas.Winkler@mpimf-heidelberg.mpg.de.2Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany. Electronic address: Aniko.Udvarhelyi@mpimf-heidelberg.mpg.de.3Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany. Electronic address: Elisabeth.Hartmann@mpimf-heidelberg.mpg.de.4Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany. Electronic address: Jochen.Reinstein@mpimf-heidelberg.mpg.de.5Paul Scherrer Institut, 5232 Villigen PSI, Switzerland. Electronic address: Andreas.Menzel@psi.ch.6Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany. Electronic address: Robert.Shoeman@mpimf-heidelberg.mpg.de.7Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany. Electronic address: Ilme.Schlichting@mpimf-heidelberg.mpg.de.AbstractBacteria have evolved dedicated signaling mechanisms that enable the integration of a range of environmental stimuli and the accordant modulation of metabolic pathways. One central signaling molecule in bacteria is the second messenger cyclic dimeric GMP (c-di-GMP). Complex regulatory mechanisms for modulating c-di-GMP concentrations have evolved, in line with its importance for maintaining bacterial fitness under changing environmental conditions. One interesting example in this context is the blue-light-regulated phosphodiesterase 1 (BlrP1) of Klebsiella pneumoniae. This covalently linked system of a sensor of blue light using FAD (BLUF) and an EAL phosphodiesterase domain orchestrates the light-dependent down-regulation of c-di-GMP levels. To reveal details of light-induced structural changes involved in EAL activity regulation, we extended previous crystallographic studies with hydrogen-deuterium exchange experiments and small-angle X-ray scattering analysis of different functional BlrP1 states. The combination of hydrogen-deuterium exchange and small-angle X-ray scattering allows the integration of local and global structural changes and provides an improved understanding of light signaling via an allosteric communication pathway between the BLUF and EAL domains. This model is supported by results from a mutational analysis of the EAL dimerization region and the analysis of metal-coordination effects of the EAL active site on the dark-state recovery kinetics of the BLUF domain. In combination with structural information from other EAL domains, the observed bidirectional communication points to a general mechanism of EAL activity regulation and suggests that a similar allosteric coupling is maintained in catalytically inactive EAL domains that retain a regulatory function.
  • Journal of molecular biology.J Mol Biol.2014 Feb 20;426(4):853-68. doi: 10.1016/j.jmb.2013.11.018. Epub 2013 Nov 27.
  • Bacteria have evolved dedicated signaling mechanisms that enable the integration of a range of environmental stimuli and the accordant modulation of metabolic pathways. One central signaling molecule in bacteria is the second messenger cyclic dimeric GMP (c-di-GMP). Complex regulatory mechanisms for
  • PMID 24291457

和文文献

  • 1584 破壊評価線図によるコラム角部溶接初層部の許容欠陥高さと必要破壊靱性 : 鉄骨造建築物の安全性向上に資する新自動溶接技術の開発 (その21)(溶接ロボット・工事現場接合,材料施工,2013年度日本建築学会大会(北海道)学術講演会・建築デザイン発表会)
  • 宗川 陽祐,中野 達也,有田 政樹,渡邉 一夫
  • 学術講演梗概集 2013(材料施工), 1168-1169, 2013-08-30
  • NAID 110009684188
  • 1P-044 担子菌酵母Cryptococcus sp. S-2による麹菌Aspergillus oryzae由来FAD結合型Glucose dehydrogenaseの組換え発現(酵素学,酵素工学,一般講演)
  • 歌島 悠,相場 洋志,岸本 高英,正木 和夫,家藤 治幸
  • 日本生物工学会大会講演要旨集 65, 28, 2013-08-25
  • NAID 110009737424
  • Improvement of Closed Crack Selectivity in Nonlinear Ultrasonic Imaging Using Fundamental Wave Amplitude Difference
  • Ikeuchi Masako,Jinno Kentaro,Ohara Yoshikazu,Yamanaka Kazushi
  • Jpn J Appl Phys 52(7), 07HC08-07HC08-5, 2013-07-25
  • … To realize the high selectivity of closed cracks, we propose a fundamental wave amplitude difference (FAD) method based on the threshold behavior of fundamental waves caused by the contact vibration of closed cracks. … The formulation clarified that FAD can selectively image closed cracks while eliminating other linear scatterers, which cannot be completely eliminated by the subharmonic wave amplitude difference (SAD) method. …
  • NAID 150000107379

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関連画像

FAD Facts, information, pictures fadFad.jpgFAD assault rifle FAD / SIMA Electronica FAD 【突撃銃CallofDutySeries.de - Eure Community rund


★リンクテーブル★
リンク元ピルビン酸デヒドロゲナーゼ」「フラビンアデニンジヌクレオチド」「β酸化」「ビタミンB2」「flavin adenine dinucleotide
関連記事F」「FA

ピルビン酸デヒドロゲナーゼ」

  [★]

pyruvate dehydrogenase
ピルビン酸脱水素酵素ピルビン酸ピルビン酸デヒドロゲナーゼ複合体


概要

  • ピルビン酸からアセチルCoAを生成し、クエン酸回路に投入するための酵素
  • 逆反応を触媒する酵素はない

反応

ピルビン酸+NAD++SH-CoA → アセチルCoA+NADH+CO2 

補酵素

臨床関連

不足

アルコール中毒によるビタミンB1不足によっても生じる


フラビンアデニンジヌクレオチド」

  [★]

flavin adenine dinucleotide, FAD
フラビンアデニンジヌクレオチドナトリウム flavin-adenine dinucleotide sodium
FADアスルダムアセラートアデフラビンアデラビン9号エフエーミックヒシデニンビタストファデミンフラジレンフラッドフラビタンベマカストムコティアムコファジンライボミンSリバレスレバサルトワカデニン
フラビンリボフラビン = ビタミンB2臓器製剤


  • 酸化還元反応に関わる補酵素。
  • 栄養ドリンクを飲んで尿が黄色に着色するのはフラビンのせい。
  • H+をe-を受け取って還元力のキャリアーとなる。



β酸化」

  [★]

β-oxidation, beta-oxidation
脂肪酸酸化 fatty acid oxidation
脂肪酸


  • 図:FB.384
  • 脂肪酸がミトコンドリアで酸化的に分解される
アシルCoA + FAD + NAD+ H2O + CoASH → アシルCoA + FADH2 + NADH + H+ + CoAS-COCH3


ビタミンB2」

  [★]

vitamin B2
リボフラビンriboflavin
ビタミン




flavin adenine dinucleotide」

  [★] フラビンアデニンジヌクレオチド FAD


F」

  [★] フェニルアラニン phenylalanine

WordNet   license wordnet

「the 6th letter of the Roman alphabet」
f


FA」

  [★]



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