ライフサイエンスコーパス: isoalloxazine ring

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

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

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

4 otates to become almost perpendicular to the isoalloxazine ring.

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

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

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

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

9 apoflavodoxin that is capable of binding the isoalloxazine ring.

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

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

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

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

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

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

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

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

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

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

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

21 Two stacked isoalloxazine rings and nicotinamide/isoalloxazine rings

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

48 The flavin isoalloxazine ring is sandwiched between two tryptophan

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

68 1 forms pi-pi stacking interactions with the isoalloxazine ring of FAD.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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