ライフサイエンスコーパス: flavin-adenine dinucleotide

1 nicotinamide adenine dinucleotide), and FAD (flavin adenine dinucleotide).

2 e and has stoichiometric amounts of heme and flavin adenine dinucleotide.

3 active oxygen species (ROS) formation at the flavin adenine dinucleotide.

4 adenylate cofactors NAD(P), coenzyme A, and flavin adenine dinucleotide.

5 with potential binding sites for NAD(P)H and flavin adenine dinucleotide.

6 d a molecular weight of 22,000 and contained flavin adenine dinucleotide.

7 e dehydrogenase with a bicovalently attached flavin adenine dinucleotide.

8 e flavin coenzymes flavin mononucleotide and flavin adenine dinucleotide.

9 spectra of ALR bound to oxidized and reduced flavin adenine dinucleotide.

10 rescent metabolic coenzymes reduced NADH and flavin adenine dinucleotide.

11 to coenzyme forms flavin mononucleotide and flavin adenine dinucleotide.

12 th stoichiometric amounts of the chromophore flavin-adenine dinucleotide.

13 The protein contained flavin adenine dinucleotide and exhibited NADPH quinone

14 Both enzymes use flavin adenine dinucleotide and folate in their reaction

15 ers also formed in mutants that did not bind flavin adenine dinucleotide and in truncated peptides wi

16 nent, was found to contain approximately one flavin adenine dinucleotide and one ferredoxin-type [2Fe

17 ites across the two molecules, involving the flavin adenine dinucleotide and substrate-binding pocket

18 li, was shown to possess noncovalently bound flavin adenine dinucleotide and to exhibit L-2-hydroxygl

19 n glucose oxidase, electron transfer between flavin-adenine-dinucleotide and tryptophan(s)/tyrosine(s

20 llular NADPH, across a chain comprising FAD (flavin adenine dinucleotide) and two haems, to reduce ex

21 The NADH, flavin adenine dinucleotide, and Fe-S center binding sit

22 factor in addition to a molybdenum cofactor, flavin adenine dinucleotide, and FeS centers, were purif

23 educed nicotinamide adenine dinucleotide and flavin adenine dinucleotide, and the absorption of cytoc

24 BLUF domains (sensors of blue light using flavin adenine dinucleotide) are a group of flavin-conta

25 ated WC-1 and WC-2 confirmed that WC-1, with flavin adenine dinucleotide as a cofactor, is the blue l

26 the oxidation of d-lactate to pyruvate using flavin adenine dinucleotide as a cofactor; knowledge of

27 However, NAD(P)H and flavin adenine dinucleotide binding motifs are conserved

28 teine-to-serine substitution remote from the flavin adenine dinucleotide binding site decouples confo

29 ce of DWF1 shows significant similarity to a flavin adenine dinucleotide-binding domain conserved in

30 this family is that the sequence of the key flavin adenine dinucleotide-binding domain is split into

31 7 of 10 dwf1 mutations directly affected the flavin adenine dinucleotide-binding domain.

32 se-methanol-choline oxidoreductase family of flavin adenine dinucleotide-binding enzymes catalyzing h

33 The input sensor in Aer is a flavin adenine dinucleotide-binding PAS domain, which is

34 This gene is predicted to encode a conserved flavin adenine dinucleotide-binding protein involved in

35 hey had open reading frames that predicted a flavin adenine dinucleotide-binding site, multiple N-gly

36 ial N-glycosylation sites, and a presumptive flavin adenine dinucleotide-binding site.

37 utative redox active site CAVC as well as an flavin-adenine dinucleotide-binding domain are highly co

38 that the amino terminus domain of IrtA is a flavin-adenine dinucleotide-binding domain essential for

39 Blue light using flavin adenine dinucleotide (BLUF) proteins are essentia

40 t MHPCO is a homotetrameric protein with one flavin adenine dinucleotide bound per subunit.

41 s a flavoprotein containing covalently bound flavin adenine dinucleotide, but no detectable heavy met

42 th the flavoprotein SdhA, directly bound the flavin adenine dinucleotide co-factor, and was required

43 hotoinduced electron transfer from a reduced flavin adenine dinucleotide cofactor (FADH(-)) to the bo

44 rified NDH-2 contains a non-covalently bound flavin adenine dinucleotide cofactor and oxidizes NADH w

45 clic electron transfer between the catalytic flavin adenine dinucleotide cofactor and the damaged DNA

46 ht activation, electron transfer between the flavin adenine dinucleotide cofactor and tryptophan resi

47 tate of the electron transport system via an flavin adenine dinucleotide cofactor bound to a PAS doma

48 The flavin adenine dinucleotide cofactor has an unusual bent

49 the entire pH range under investigation, the flavin adenine dinucleotide cofactor of GOx changed dire

50 d for Sdh1 flavination (incorporation of the flavin adenine dinucleotide cofactor).

51 tors but unique in having a PAS domain and a flavin-adenine dinucleotide cofactor that is postulated

52 ws in vitro responsiveness to high cofactor (flavin adenine dinucleotide) concentrations.

53 The acyl-CoA dehydrogenases are a family of flavin adenine dinucleotide-containing enzymes that cata

54 ACAD9 is a flavin adenine dinucleotide-containing flavoprotein, and

55 In Neurospora, the flavin adenine dinucleotide-containing protein WHITE COL

56 generates an inactive enzyme unable to bind flavin adenine dinucleotide covalently.

57 Here we report the identification of a novel flavin adenine dinucleotide-dependent amine oxidase (ren

58 ression of whiE ORFVIII, encoding a putative flavin adenine dinucleotide-dependent hydroxylase that c

59 e cytochrome P450 monooxygenase (TamI) and a flavin adenine dinucleotide-dependent oxidase (TamL), wh

60 midine/spermine N1-acetyltransferase and the flavin adenine dinucleotide-dependent polyamine oxidase

61 talyses removal of H3K4me2/H3K4me1 through a flavin-adenine-dinucleotide-dependent oxidation reaction

62 , such as LOV and BLUF (blue-light-utilizing flavin adenine dinucleotide) domains, cryptochromes, and

63 n addition, NADH ED-FRAP was correlated with flavin adenine dinucleotide (FAD(+)) fluorescence.

64 .1 atom/mol), Fe (21 +/- 1.6 atoms/mol), and flavin adenine dinucleotide (FAD) (0.83 +/- 0.1 mol/mol)

65 ltage sensing (LOV) and Blue-Light-Utilizing flavin adenine dinucleotide (FAD) (BLUF) domains represe

66 ced nicotine adenine dinucleotide (NADH) and flavin adenine dinucleotide (FAD) - is demonstrated.

67 tion of the histone tail lysine (H3K4), with flavin adenine dinucleotide (FAD) acting as cofactor.

68 at contain noncovalently or covalently bound flavin adenine dinucleotide (FAD) analogues were studied

69 ophilum at 1.6 A resolution, in complex with flavin adenine dinucleotide (FAD) and a bacterial lipid.

70 se is a homodimeric flavoenzyme containing a flavin adenine dinucleotide (FAD) and a redox-active dis

71 ve a common structural fold, a dependence on flavin adenine dinucleotide (FAD) and an internal photoa

72 nt HlmI was purified from E. coli with bound flavin adenine dinucleotide (FAD) and converts reduced h

73 vin as the direct precursor of the cofactors flavin adenine dinucleotide (FAD) and flavin mononucleot

74 s soluble and contains an equimolar ratio of flavin adenine dinucleotide (FAD) and flavin mononucleot

75 The riboflavin (RF) cofactors, flavin adenine dinucleotide (FAD) and flavin mononucleot

76 The adsorption of flavin adenine dinucleotide (FAD) and glucose oxidase (G

77 PvdA requires both flavin adenine dinucleotide (FAD) and nicotinamide adeni

78 the formation of the essential flavocoenzyme flavin adenine dinucleotide (FAD) and plays an important

79 interactions on the stabilization of reduced flavin adenine dinucleotide (FAD) and substrate/product

80 flux between flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD) and/or the electron ac

81 yglutamate (MTHF) and the catalytic cofactor flavin adenine dinucleotide (FAD) are noncovalently boun

82 Tryptophan and flavin adenine dinucleotide (FAD) are separated by a 10

83 The endogenous fluorophores NADH and flavin adenine dinucleotide (FAD) are two of the princip

84 hyltetrahydrofolate (CH(3)-H(4)folate) using flavin adenine dinucleotide (FAD) as a cofactor.

85 al to the molecular clock using a pterin and flavin adenine dinucleotide (FAD) as chromophore/cofacto

86 hyltetrahydrofolate (CH(3)-H(4)folate) using flavin adenine dinucleotide (FAD) as cofactor.

87 nstead methylenetetrahydrofolate and reduced flavin adenine dinucleotide (FAD) as essential cofactors

88 heir interactions and the functional role of flavin adenine dinucleotide (FAD) binding in CRYs remain

89 t DntB contains the highly conserved ADP and flavin adenine dinucleotide (FAD) binding motifs charact

90 rs of electrons requiring photoactivation of flavin adenine dinucleotide (FAD) bound near a triad of

91 oS contains a flavin cofactor, identified as flavin adenine dinucleotide (FAD) by fluorescence spectr

92 purified PrnF protein catalyzes reduction of flavin adenine dinucleotide (FAD) by NADH with a k(cat)

93 AidB was recently shown to possess a flavin adenine dinucleotide (FAD) cofactor and to bind t

94 produce type II symptoms occur close to the flavin adenine dinucleotide (FAD) cofactor binding site.

95 , cycles of reduction and reoxidation of the flavin adenine dinucleotide (FAD) cofactor depend on rat

96 ichia coli photolyase, photoreduction of the flavin adenine dinucleotide (FAD) cofactor in its neutra

97 en a spin label and an enzymatically reduced flavin adenine dinucleotide (FAD) cofactor in P. denitri

98 Adenosine is a structural part of the flavin adenine dinucleotide (FAD) cofactor of the dehydr

99 , which lacks the covalent attachment to the flavin adenine dinucleotide (FAD) cofactor present in th

100 r, has a HAMP domain and a PAS domain with a flavin adenine dinucleotide (FAD) cofactor that senses t

101 homology region (PHR) carrying the oxidized flavin adenine dinucleotide (FAD) cofactor, and a crypto

102 ion of two key glutamic acids as well as the flavin adenine dinucleotide (FAD) cofactor.

103 the spectral properties of its tightly bound flavin adenine dinucleotide (FAD) cofactor.

104 formation of flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD) cofactors, is internal

105 The enzyme contains 1 mol of flavin adenine dinucleotide (FAD) covalently linked to C

106 hF) of p-cresol methylhydroxylase (PCMH) has flavin adenine dinucleotide (FAD) covalently tethered to

107 the cytoplasm, where the PAS (Per-ARNT-Sim)-flavin adenine dinucleotide (FAD) domain senses redox ch

108 on of the NAD(P)H domain with respect to the flavin adenine dinucleotide (FAD) domain that precludes

109 responses were matched by inverted biphasic flavin adenine dinucleotide (FAD) fluorescence transient

110 5'-nucleotidase, resulted in accumulation of flavin adenine dinucleotide (FAD) in culture supernatant

111 d ultrafast photoreduction of oxidized state flavin adenine dinucleotide (FAD) in subpicosecond and o

112 es a reaction in two parts: reduction of the flavin adenine dinucleotide (FAD) in the enzyme by reduc

113 reduction of FMN by electrons from NADPH and flavin adenine dinucleotide (FAD) in the reductase domai

114 Flavin adenine dinucleotide (FAD) is involved in importa

115 Flavin adenine dinucleotide (FAD) is one of the primary

116 The cofactor flavin adenine dinucleotide (FAD) is required for the ca

117 tive folding was shown to depend on cellular flavin adenine dinucleotide (FAD) levels but not on ubiq

118 The flavin adenine dinucleotide (FAD) moiety of Frd is unusu

119 t in addition to having a tightly associated flavin adenine dinucleotide (FAD) moiety, yeast Ero1p is

120 PA) capture probes prebound to electroactive flavin adenine dinucleotide (FAD) molecules, and a signa

121 TftC was an NADH:flavin adenine dinucleotide (FAD) oxidoreductase.

122 studies of Aer suggested that it might use a flavin adenine dinucleotide (FAD) prosthetic group to mo

123 eductase (MMOR), which contains [2Fe-2S] and flavin adenine dinucleotide (FAD) prosthetic groups.

124 he active site, where a non-covalently bound flavin adenine dinucleotide (FAD) sits at the base of an

125 5 is required for the covalent attachment of flavin adenine dinucleotide (FAD) to protein Sdh1, a sub

126 ic dehydrogenase domain (DH(CDH)) containing flavin adenine dinucleotide (FAD), a cytochrome domain (

127 ia, with a decrease in the cellular level of flavin adenine dinucleotide (FAD), a metabolic cofactor

128 , shown to possess stoichiometric amounts of flavin adenine dinucleotide (FAD), and confirmed to have

129 asured the 2P-excitation spectra of NAD(P)H, flavin adenine dinucleotide (FAD), and lipoamide dehydro

130 P450-type heme, flavin mononucleotide (FMN), flavin adenine dinucleotide (FAD), and tetrahydrobiopter

131 but not by the addition of L-arginine, heme, flavin adenine dinucleotide (FAD), flavin mononucleotide

132 contains an N-terminal PAS domain that binds flavin adenine dinucleotide (FAD), senses aerotactic sti

133 They usually bind two chromophores: flavin adenine dinucleotide (FAD), which forms the activ

134 ith isotopically labeled riboflavin (Rf) and flavin adenine dinucleotide (FAD), which permit the firs

135 aks were due to the redox of enzyme cofactor flavin adenine dinucleotide (FAD), which was not the par

136 e atomic crystal structures of the catalytic flavin adenine dinucleotide (FAD)- and heme-binding doma

137 previously characterized BdlA homolog is the flavin adenine dinucleotide (FAD)-binding Aer, the redox

138 rochemical analysis of this and the isolated flavin adenine dinucleotide (FAD)-binding domain in the

139 oach yielded a polypeptide that included the flavin adenine dinucleotide (FAD)-binding domain of nNOS

140 esolution of the three domains of d-LDH: the flavin adenine dinucleotide (FAD)-binding domain, the ca

141 These proteins comprise two modules: a flavin adenine dinucleotide (FAD)-binding module and a t

142 Because LSD1 belongs to the family of flavin adenine dinucleotide (FAD)-dependent amine oxidas

143 ient composite for electron transfer between flavin adenine dinucleotide (FAD)-dependent glucose dehy

144 A new extracellular flavin adenine dinucleotide (FAD)-dependent glucose dehy

145 SgcC3 unveiled the following: (i) SgcC3 is a flavin adenine dinucleotide (FAD)-dependent halogenase;

146 KMO is a flavin adenine dinucleotide (FAD)-dependent monooxygenas

147 w revealed that (i) SgcC is a two-component, flavin adenine dinucleotide (FAD)-dependent monooxygenas

148 line dehydrogenase domain that catalyzes the flavin adenine dinucleotide (FAD)-dependent oxidation of

149 Here, we show that the mitochondrial flavin adenine dinucleotide (FAD)-linked sulfhydryl oxid

150 recognizes the flavin moiety of both FMN and flavin adenine dinucleotide (FAD).

151 methylglycine) and contains covalently bound flavin adenine dinucleotide (FAD).

152 h contains a molecule of noncovalently bound flavin adenine dinucleotide (FAD).

153 n from the enzyme's fluorescent active site, flavin adenine dinucleotide (FAD).

154 ined high levels of noncovalently associated flavin adenine dinucleotide (FAD).

155 terodimers containing a single equivalent of flavin adenine dinucleotide (FAD).

156 enine dinucleotide (phosphate) (NAD(P)H) and flavin adenine dinucleotide (FAD).

157 mutant that has greatly reduced affinity for flavin adenine dinucleotide (FAD).

158 In PdR, the flavin adenine dinucleotide (FAD/FADH2) redox center act

159 Flavin-adenine dinucleotide (FAD) dependent glucose dehy

160 rm this role: 5'-phosphoriboflavin (FMN) and flavin-adenine dinucleotide (FAD).

161 ced flavins (flavin mononucleotide [FMN] and flavin adenine dinucleotide [FAD]) and cob(III)alamin to

162 between VVD residue Cys108 and its cofactor flavin adenine dinucleotide(FAD), and prompts VVD switch

163 four, bis-His-ligated, c-type hemes and one flavin adenine dinucleotide, FAD.

164 steady-state kinetic mechanism of the active flavin adenine dinucleotide-(FAD-) containing form of th

165 or of a photolyase is a two-electron-reduced flavin adenine dinucleotide (FADH(-)).

166 e (4HPA) 3-monooxygenase (HpaB) is a reduced flavin adenine dinucleotide (FADH(2)) utilizing monooxyg

167 TcpA is a reduced flavin adenine dinucleotide (FADH2)-dependent monooxygen

168 ation of the enzyme indicated that a reduced flavin adenine dinucleotide (FADH2)-utilizing monooxygen

169 apparent molecular mass of 47 kDa, requires flavin adenine dinucleotide for activity, has NADH-speci

170 The dynamics of electron transfer to excited flavin adenine dinucleotide from a neighboring tyrosine

171 ERO1alpha followed by displacement of bound flavin adenine dinucleotide from the active site of the

172 icotinamide adenine dinucleotide phosphate , flavin adenine dinucleotide , glutathione disulfide/glut

173 tes bind in close proximity to the catalytic flavin adenine dinucleotide group, substantial flexibili

174 he distance and orientation between MTHF and flavin adenine dinucleotide in At-Cry3 is similar to tha

175 s between the flavin and adenine moieties of flavin adenine dinucleotide in four redox forms of the o

176 TcuB transfers electrons from reduced flavin adenine dinucleotide in the Tcb dehydrogenase (Tc

177 to FMN (K(D) approximately 4 microM) than to flavin adenine dinucleotide (K(D) approximately 12 micro

178 Ac92 has homology to the family of flavin adenine dinucleotide-linked sulfhydryl oxidases a

179 a molecular mass of 45 kDa and contains one flavin adenine dinucleotide molecule per mole but lacks

180 a protein complex composed of oxidoreductase flavin adenine dinucleotide/NAD(P)-binding subunit (Dred

181 degradation, likely due to the imbalance of flavin adenine dinucleotide/nicotinamide adenine dinucle

182 .4 mol of acid-labile sulfur, and 0.7 mol of flavin adenine dinucleotide per mol of protein.

183 n a reduction of the binding affinity of the flavin-adenine dinucleotide prosthetic group.

184 recognition coincided with the loss of FAD (flavin-adenine dinucleotide) recognition in all isolates

185 ne, which encodes a 399-amino-acid NAD+- and flavin adenine dinucleotide-requiring enzyme responsible

186 anaerobic levels, and binding of NADH to the flavin-adenine dinucleotide site seemed to prevent oxyge

187 However, with flavin-adenine dinucleotide site-binding substrate NADH

188 After reconstitution with flavin adenine dinucleotide, the resulting protein was i

189 ur subunits that contain a covalently linked flavin adenine dinucleotide, three different iron-sulfur

190 at m5U54 is added by the enzyme TrmFO using flavin adenine dinucleotide together with N5,N10-methyle

191 ed in the literature for flavodoxin and free flavin adenine dinucleotide were simulated based on sele

192 precursor of flavin mononucleotide (FMN) and flavin adenine dinucleotide, which are essential coenzym