ライフサイエンスコーパス: isoalloxazine

1 ty of lumazine and ultimately the riboflavin isoalloxazine.

2 s a unique interaction between Lys53 and the isoalloxazine.

3 are adjacent to the quininoidal edge of the isoalloxazine.

4 alysis via a number of different mechanisms, isoalloxazine analogues are valuable for mechanistic stu

5 configuration of the FAD cofactor, where the isoalloxazine and adenine rings are nearly in vdW contac

6 that the unique relative orientation of the isoalloxazine and adenine rings may have resulted from t

7 nce of F397 in nicotinamide access to flavin isoalloxazine and confirm flavin binding contributions f

8 nalogue binds against the si face of the FAD isoalloxazine and is protected from bulk solvent by heli

9 s stacked parallel to the si face of the FAD isoalloxazine and positions the sulfenyl oxygen atom onl

10 P)H binds with the nicotinamide near the FAD isoalloxazine and the ADP moiety extending toward the mo

11 interactions between coplanar nicotinamide, isoalloxazine, and Phe309 rings; (ii) rearrangement of m

12 characterized by large rotations of the FAD isoalloxazine around the C1-'C2' and N10-C1' bonds, coup

13 in substrate binding is the movement of the isoalloxazine between an "in" conformation and a more ex

14 rs ordering of the peptide loops so only one isoalloxazine can fit.

15 , between coenzyme analog, NAD(P)H4, and the isoalloxazine center in the model flavoenzymes morphinon

16 on involves the secretion of flavins, yellow isoalloxazine compounds that serve important redox roles

17 in the pyrazine and pyrimidine rings of the isoalloxazine core of the cofactor from readily availabl

18 The isoalloxazine core was required for enzymatic inhibition

19 ncluding 20 degrees butterfly bending of the isoalloxazine, crankshaft rotation of the ribityl, shift

20 e pathway for molecular oxygen to access the isoalloxazine group for the oxidative half reaction.

21 dds a fourth non-aromatic ring to the flavin isoalloxazine group.

22 annealing step was necessary to perfect the isoalloxazine helix and expel the C60 moiety away from t

23 i-pi overlap between the graphene sidewalls, isoalloxazine helix, and the C60 cage that facilitates S

24 hat brings the C60 in pi-pi overlap with the isoalloxazine helix.

25 terface which enable specific binding of the isoalloxazine heterocycle of riboflavin and its two cofa

26 sulfate (SDS) overcomes this strong nanotube/isoalloxazine interaction and restores the FMN into exte

27 atural substrate is bound to the enzyme, the isoalloxazine is in the correct position (the "in" confo

28 The isoalloxazine is observed to move between these conforma

29 number of spectral features associated with isoalloxazine modes in this pH range are evidence for a

30 reactant, the rings of the nicotinamide and isoalloxazine moieties are stacked roughly parallel to e

31 onalized flavin (FC60), composed of PCBM and isoalloxazine moieties attached on either ends of a line

32 rs to be due to hydrogen bonding between the isoalloxazine moiety and the protein.

33 avodoxins catalyze redox reactions using the isoalloxazine moiety of the flavin mononucleotide (FMN)

34 otinamide moiety into close contact with the isoalloxazine moiety of the flavin.

35 OH) is described that contains the tricyclic isoalloxazine moiety, the C-4a-hydroperoxide functionali

36 es belonging to certain carbons of the FMN's isoalloxazine moiety.

37 It is therefore concluded that isoalloxazine movement is required for pyridine nucleoti

38 likely reflects the interaction between the isoalloxazine N1 of the orotate-reducing flavin and Lys

39 of the oxidized cofactor can be observed, an isoalloxazine N5-iminium adduct and a N5 secondary ketim

40 aptamers recognize with high specificity the isoalloxazine nucleus of FAD but do not distinguish FAD

41 droxybenzoate (2,4-diOHB) indicated that the isoalloxazine of the artificial flavin adopts the more s

42 -lived charge-transfer complex involving the isoalloxazine of the FAD cofactor.

43 showed that reduction of FAD occurs when the isoalloxazine of the FAD moves to the surface of the pro

44 s of reduction of the enzyme require (a) the isoalloxazine of the flavin be held by the protein in a

45 n of a narrow tunnel leading directly to the isoalloxazine portion of the FAD prosthetic group.

46 o arise from the ring current field from the isoalloxazine portion of the flavin cofactor.

47 Upon blue-light excitation, the isoalloxazine ring (ISO) may undergo an ultrafast reduct

48 cofactor, including a 22 degrees bend of the isoalloxazine ring along the N(5)-N(10) axis, crankshaft

49 ich makes van der Waals contact with the FAD isoalloxazine ring and also hydrogen-bonds to the ribity

50 n bonding and pi-pi interactions between the isoalloxazine ring and either the nicotinamide ring or T

51 The FMN is bound with hydrogen bonds to the isoalloxazine ring and electrostatic interactions with t

52 trix shield the reactive C4a position of the isoalloxazine ring and force the tricycle into an atypic

53 between the Arg115 side chain and N5 of the isoalloxazine ring and interactions of the flavin with t

54 significant overlap between the intercalated isoalloxazine ring and its adjacent base-triple platform

55 gen bond is formed between the N5 of the FAD isoalloxazine ring and the hydroxyl side chain of alpha

56 owing that the environments for the flavin's isoalloxazine ring are not identical in the two phases.

57 exes are consistent with modification of the isoalloxazine ring at position N5.

58 . vulgaris flavodoxin that are necessary for isoalloxazine ring binding.

59 owever, the FADH- structure reveals that the isoalloxazine ring buckles in the opposite sense, this a

60 y bound to RNA through interactions with the isoalloxazine ring chromophore and direct and Mg(2+)-med

61 tional rearrangements of the protein and the isoalloxazine ring during catalysis.

62 ormational rearrangements of the protein and isoalloxazine ring during catalysis.

63 elix and to the active-site entrance; an FAD isoalloxazine ring exposed to solvent; and a large and a

64 from solution is bound, the insertion of the isoalloxazine ring first.

65 r-401 and Phe-485 in phiLOV sandwich the FMN isoalloxazine ring from both sides, whereas Ser-390 anch

66 The isoalloxazine ring has a butterfly angle of 25 degrees ,

67 bstrate was bound at the re-side face of the isoalloxazine ring in a solvent-connected cavity.

68 Phe(1395) stacks parallel to the FAD isoalloxazine ring in neuronal nitric-oxide synthase (nN

69 ent and placement with respect to the flavin isoalloxazine ring in the active site of rhNQO1; a quali

70 alpha beta is due to solvent exposure of the isoalloxazine ring in the beta 2 active site.

71 , are achieved by moving the position of the isoalloxazine ring in the protein structure.

72 The isoalloxazine ring is coordinated by an unusual cis-Ala-

73 In this model, the binding of the flavin isoalloxazine ring is dependent on the presence of a pho

74 The Raman data show that the isoalloxazine ring is predominantly "out" for Tyr222Phe.

75 The flavin isoalloxazine ring is sandwiched between two tryptophan

76 Its His-289 residue in the re-side of the isoalloxazine ring is within hydrogen bonding distance w

77 ieties are required for folding: whereas the isoalloxazine ring linked to ribitol and one phosphate i

78 The spectra consist of a rich assortment of isoalloxazine ring modes whose normal mode origin can be

79 gen at C6 of DHO is transferred to N5 of the isoalloxazine ring of an enzyme-bound FMN prosthetic gro

80 isting of the substrate (cyclohexanone), the isoalloxazine ring of C4a-peroxyflavin, the side chain o

81 residue in the FNR module of NOS shields the isoalloxazine ring of FAD and is known to regulate NADPH

82 e at reaction distance to the N5 atom of the isoalloxazine ring of FAD and the hydroxyl group of Tyr(

83 droxyl group of serine or threonine with the isoalloxazine ring of FAD and with the amino acids in it

84 In the model, Pdx is docked above the isoalloxazine ring of FAD of Pdr with the distance betwe

85 de ring of NADPH, which is juxtaposed to the isoalloxazine ring of FAD to facilitate hydride transfer

86 t that is in contact with the re face of the isoalloxazine ring of FAD when the structure of PchF is

87 oned directly above and in parallel with the isoalloxazine ring of FAD, and mass spectrometry extende

88 zolyl ring of 3FMTDZ was positioned over the isoalloxazine ring of FAD, whereas that of HETDZ had the

89 charge and 4-5 masculine bend in the reduced isoalloxazine ring of FAD, which resulted in a new mode

90 at resveratrol molecule in parallel with the isoalloxazine ring of FAD.

91 1 forms pi-pi stacking interactions with the isoalloxazine ring of FAD.

92 n selected because of their proximity to the isoalloxazine ring of FAD.

93 n a conserved phenylalanine, Phe223, and the isoalloxazine ring of FAD.

94 difference in active site residues near the isoalloxazine ring of FAD: Val402 in EcPutA is substitut

95 active site and would appear to require the isoalloxazine ring of FADH- to buckle in a particular wa

96 stabilizes developing negative charge on the isoalloxazine ring of flavin mononucleotide during hydri

97 icantly reduced the electron density for the isoalloxazine ring of FMN and induced a conformational c

98 a base-triple on complex formation with the isoalloxazine ring of FMN intercalating into the helix b

99 rogen bonding of the uracil like edge of the isoalloxazine ring of FMN to the Hoogsteen edge of an ad

100 The isoalloxazine ring of FMN was shown buried within a narr

101 the peptide Gly57-Asp58, in a bend near the isoalloxazine ring of FMN, is correlated with the oxidat

102 face of AvLOx, and within 20 angstrom of the isoalloxazine ring of FMN.

103 The isoalloxazine ring of the bound FAD is more buried in th

104 Since the isoalloxazine ring of the chromophore is unable to under

105 th the structure of rat CPR, is close to the isoalloxazine ring of the enzyme-bound FAD.

106 irpin conformation and is wedged between the isoalloxazine ring of the FAD and the side chain of Phe2

107 beta bond of the thioester substrate and the isoalloxazine ring of the FAD are located, is larger in

108 utilizing a pi-stacking interaction with the isoalloxazine ring of the FAD cofactor.

109 tion of FADH(-) in photolyases, in which the isoalloxazine ring of the flavin and the adenine are in

110 gen at C6 of DHO is transferred to N5 of the isoalloxazine ring of the flavin as a hydride.

111 jority of the critical interactions with the isoalloxazine ring of the flavin mononucleotide (FMN) co

112 in favorable pi-sigma interactions with the isoalloxazine ring of the flavin to help stabilize forma

113 77), which stacks against the re-face of the isoalloxazine ring of the flavin.

114 at presents a CxxC disulfide proximal to the isoalloxazine ring of the flavin.

115 ect contact with the re or inner face of the isoalloxazine ring of the FMN cofactor.

116 relative position of a peptide loop and the isoalloxazine ring of the FMN is slightly different in t

117 matic substitution, diradical formation, and isoalloxazine ring opening have been proposed.

118 es flank the flavin, which is bound with its isoalloxazine ring perpendicular to a five-stranded beta

119 cated in the antigen-combining site with its isoalloxazine ring stacked between the parallel aromatic

120 hat the spin density distribution within the isoalloxazine ring system depends critically on the natu

121 te hydroxylase (PHBH) have revealed that the isoalloxazine ring system of FAD is capable of adopting

122 The isoalloxazine ring system of one conformation (the "out"

123 , Tyr-466, and Ser-468) in a pocket near the isoalloxazine ring system of the FAD co-factor.

124 the nicotinamide base stacks directly on the isoalloxazine ring system of the FAD.

125 the flavin prenyltransferase, extending the isoalloxazine ring system with a fourth non-aromatic rin

126 ble loop (loop III) above the si-face of the isoalloxazine ring that changes position depending on th

127 antiomer cannot approach close enough to the isoalloxazine ring to form a flavin adduct, but can be f

128 The binding of the flavin isoalloxazine ring to its subsite is dependent on the pr

129 either adduct formation or reduction of the isoalloxazine ring to the neutral semiquinone, both of w

130 The 8-position of the FAD isoalloxazine ring was chosen for modification because i

131 The 8-position of the FAD isoalloxazine ring was chosen for modifications, because

132 dithiol substrates of these oxidases to the isoalloxazine ring where the reaction with molecular oxy

133 amide moiety of NADP(+) lies against the FAD isoalloxazine ring with a tilt of approximately 30 degre

134 through conformational rearrangements of the isoalloxazine ring within the protein structure.

135 yl of the ribityl chain of FAD and N1 of the isoalloxazine ring, and between alpha H286 and the C2-ca

136 evere (35 degrees ) butterfly bending of the isoalloxazine ring, and disruption of an electrostatic n

137 hat stacks against the si-face of the flavin isoalloxazine ring, and P92, the second residue in the m

138 the methyl group of Thr-394 "crowds" the FMN isoalloxazine ring, Leu-470 triggers side chain "flippin

139 alpha H286 and the C2-carbonyl oxygen of the isoalloxazine ring, may play a role in the stabilization

140 the plane of the FMN via pi-overlap with the isoalloxazine ring, penetrating deep into the groove, wi

141 ension concurrent with a 5 A movement of the isoalloxazine ring, positioning the flavin ring adjacent

142 ing into the sulfur-reducing side of the FAD isoalloxazine ring, suggesting how this enzyme class may

143 d provides several interactions with the FMN isoalloxazine ring, was targeted in this study.

144 vement of the side chain of Trp60 out of the isoalloxazine ring-binding site and other associated con

145 ing subsite or the loops that constitute the isoalloxazine ring-binding site.

146 ate-induced conformational change within the isoalloxazine ring-binding subsite.

147 apoflavodoxin that is capable of binding the isoalloxazine ring.

148 re believed to bind to it mainly through the isoalloxazine ring.

149 ormational change in the vicinity of the FAD isoalloxazine ring.

150 epting a hydrogen bond from the H(N5) of the isoalloxazine ring.

151 degrees along the N5-N10 axis of the flavin isoalloxazine ring.

152 thyl group beta-protons at position 8 of the isoalloxazine ring.

153 ition to directly attack the C4a atom of the isoalloxazine ring.

154 ns the heme planar to the si-face of the FMN isoalloxazine ring.

155 e dynamics and the planarity of their flavin isoalloxazine ring.

156 otates to become almost perpendicular to the isoalloxazine ring.

157 in terms of the difference at C8alpha of the isoalloxazine ring.

158 and BrdUMP in a closed conformation near the isoalloxazine ring.

159 synthase, Phe1395 is positioned over the FAD isoalloxazine ring.

160 conformational changes are apparent for the isoalloxazine ring; the three-ring system exhibits more

161 -FPR place their respective nicotinamide and isoalloxazine rings 15 A apart and separated by residues

162 Two stacked isoalloxazine rings and nicotinamide/isoalloxazine rings

163 The two flavin isoalloxazine rings are juxtaposed, with the closest dis

164 The stacked nicotinamide:isoalloxazine rings in TftC and sequential reaction kine

165 The distance between the two isoalloxazine rings is 18 A.

166 d be necessary to place the nicotinamide and isoalloxazine rings parallel and adjacent to one another

167 based on the interaction of the adenine and isoalloxazine rings that can be tailored by the "solvati

168 Moreover, the known ability of isoalloxazine rings to act as metal chelators, along wit

169 stacked isoalloxazine rings and nicotinamide/isoalloxazine rings were at a proper distance for hydrid

170 ide (FMN) and apo-flavodoxin is dominated by isoalloxazine-stacking interactions and 5'-phosphate hyd

171 S-C1(=O)-C2 plane of the substrate with the isoalloxazine substantially alter rates of the reductive

172 te to provide multiple interactions with the isoalloxazine system of FMN that are usually provided by

173 ove into position to form a complex with the isoalloxazine that is competent for hydride transfer and

174 to the stretch of the 4C&dbd;O group of the isoalloxazine; the relatively narrow profile of this fea

175 actopyranose binds at the re face of the FAD isoalloxazine with the anomeric carbon atom poised for n

176 erivatives (5-deazaflavins, alloxazines, and isoalloxazines) with boronic acids or boronic acid ester

177 early parallel to the middle ring of the FAD isoalloxazine, with the inhibitor C5 atom 3.3 A from the