ライフサイエンスコーパス: multicopper oxidase

1 the O-O bond is coupled to rapid IET in the multicopper oxidases.

2 for the evolution of nitrite reductases and multicopper oxidases.

3 ation more closely resemble the three-domain multicopper oxidases.

4 termediates in the evolution of three-domain multicopper oxidases.

5 Iron remains bound to Fpn in the absence of multicopper oxidases.

6 utative protein possessing two signatures of multicopper oxidases.

7 e different ceruloplasmins relative to other multicopper oxidases.

8 ows high sequence and functional homology to multicopper oxidases.

9 resent evidence that Drosophila melanogaster multicopper oxidase-1 (MCO1) is a functional ferroxidase

10 no acid sequence similarity to the family of multicopper oxidases, a diverse group of proteins that u

11 n by an enzyme or enzyme complex involving a multicopper oxidase, although the biochemical mechanism

12 This copper atom is not present in any other multicopper oxidase, and its presence appears to stabili

13 The multicopper oxidases are a family of enzymes that couple

14 The two-domain multicopper oxidases are proposed to be key intermediate

15 er in an enzymatic fuel cell together with a multicopper oxidase at the cathode, or in a proton excha

16 The multicopper oxidases catalyze the 4e- reduction of O2 to

17 Multicopper oxidases catalyze the 4e- reduction of O2 to

18 The multicopper oxidases contain at least four copper atoms

19 that support a hypothesis that the putative multicopper oxidase CueO and the transenvelope transport

20 The multicopper oxidase CueO had previously been demonstrate

21 The multicopper oxidase CueO oxidizes toxic Cu(I) and is req

22 We further show that the multicopper oxidase encoded by LOW PHOSPHATE ROOT 1 (LPR

23 proteins in the plasma membrane of yeast--a multicopper oxidase, encoded by the FET3 gene, and a per

24 ntiserum was generated against hephaestin, a multicopper oxidase essential for enteric iron absorptio

25 Human ceruloplasmin (CP) is a multicopper oxidase essential for normal iron homeostasi

26 Ceruloplasmin is a multicopper oxidase essential for normal iron homeostasi

27 Based on FET3 sequence homology to the multicopper oxidase family and iron oxidation studies in

28 This protein is a member of the multicopper oxidase family, an evolutionarily conserved

29 Bilirubin oxidases, a sub class of the Multicopper oxidases family, were discovered in 1981 by

30 The multicopper oxidase Fet3p catalyzes the four-electron re

31 The multicopper oxidase Fet3p couples four 1e(-) oxidations

32 The multicopper oxidase Fet3p is thought to convert extracel

33 isiae restored copper incorporation into the multicopper oxidase Fet3p, providing direct evidence of

34 tant abrogated copper incorporation into the multicopper oxidase Fet3p.

35 restoration of copper incorporation into the multicopper oxidase Fet3p.

36 ort system, which relies on the cell surface multicopper oxidase Fet3p.

37 visiae, Fe(II) is oxidized to Fe(III) by the multicopper oxidase, Fet3p, and the Fe(III) produced is

38 These are a multicopper oxidase, Fet3p, with specificity towards Fe(

39 of blue copper oxidase, a type C two-domain multicopper oxidase from Nitrosomonas europaea, has been

40 nducible oxidase activity, attributed to the multicopper oxidase function of PcoA.

41 A number of two-domain multicopper oxidases have been identified from genome se

42 of the metal transporter IREG1/MTP1 and the multicopper oxidase, hephaestin.

43 s fatty acid desaturase homolog (Ole2) and a multicopper oxidase homolog (Fet3) play roles in prostag

44 his is consistent with a possible role for a multicopper oxidase in Arabidopsis Fe homeostasis, as pr

45 Fet3p is a multicopper oxidase in this membrane essential for high

46 Ceruloplasmin is unique among the multicopper oxidases in that in addition to the usual co

47 ) process supports a molecular mechanism for multicopper oxidases in which O(2) is reduced to H(2)O i

48 xide-responsive transcriptional regulator, a multicopper oxidase involved in denitrification, and an

49 zation of Ctr1p (copper transporter), Fet3p (multicopper oxidase involved in high-affinity iron uptak

50 tion of O2 at the trinuclear active sites of multicopper oxidases is discussed.

51 CueO (YacK), a multicopper oxidase, is part of the copper-regulatory cu

52 cs model for catalytic dioxygen reduction on multicopper oxidase (MCO) cathodes.

53 A CotA multicopper oxidase (MCO) from Bacillus pumilus, previou

54 hyrin (ZnTMPyP(4+)) photosensitizer with the multicopper oxidase (MCO) laccase allows to link the oxi

55 A multicopper oxidase (MCO) MnxG protein from marine Bacil

56 The bacterial protein complex Mnx contains a multicopper oxidase (MCO) MnxG that, unusually, catalyze

57 The enzyme mechanism of the multicopper oxidase (MCO) SLAC from Streptomyces coelico

58 Fet3p from Saccharomyces cerevisiae is a multicopper oxidase (MCO) that contains 3 cupredoxin-lik

59 Fet3p is a multicopper oxidase (MCO) that functions together with t

60 A gene (yacK) encoding a putative multicopper oxidase (MCO) was cloned from Escherichia co

61 ) genes, including mnxG, encoding a putative multicopper oxidase (MCO), as responsible for this two-e

62 s sp. PL-12, Mnx, is a complex composed of a multicopper oxidase (MCO), MnxG, and two accessory prote

63 f manganese solid formation (as MnOx) by the multicopper oxidase (MCO)-containing Mnx protein complex

64 The multicopper oxidases (MCOs) are the family of enzymes th

65 Multicopper oxidases (MCOs) catalyze the 4e(-) reduction

66 e of expensive and inefficient Pt catalysts, multicopper oxidases (MCOs) have been envisioned because

67 G of the Mnx protein complex is unique among multicopper oxidases (MCOs) in carrying out a two-electr

68 The multicopper oxidases (MCOs) utilize a blue type 1 (T1) c

69 Multicopper oxidases (MCOs) utilize an electron shuttlin

70 n hemocyanin (Hc), tyrosinase (Tyr), and the multicopper oxidases (MCOs), such as laccase (Lc), and p

71 road agreement on the catalytic mechanism of multicopper oxidases (MCOs), the geometric and electroni

72 (NiRs) and the trinuclear Cu cluster in the multicopper oxidases (MCOs).

73 . tuberculosis and was renamed mycobacterial multicopper oxidase (MmcO).

74 nsfer processes, both requiring the putative multicopper oxidase, MnxG, in which Mn(III) is a transie

75 Hence, Rv0846c is a multicopper oxidase of M. tuberculosis and was renamed m

76 The multicopper oxidase phenoxazinone synthase (PHS) catalyz

77 Fet3p is a multicopper oxidase recently isolated from the yeast, Sa

78 This is the highest resolution multicopper oxidase structure yet determined and provide

79 SufI is structurally related to the multicopper oxidase superfamily but lacks metal cofactor

80 ing that the reaction might involve a unique multicopper oxidase system capable of a two-electron oxi

81 dation of Mn(II) appears to involve a unique multicopper oxidase system capable of the overall two-el

82 Laccase is a multicopper oxidase that contains four Cu ions, one type

83 Laccase is a multicopper oxidase that contains four Cu ions, one type

84 Fet3p is a multicopper oxidase that contains four Cu ions: one type

85 CueO itself is a multicopper oxidase that requires copper for activity.

86 Fet3p is a multicopper oxidase that uses four copper ions (one type

87 t with that of human ceruloplasmin and other multicopper oxidases that are devoid of ferroxidase acti

88 Laccases are blue multicopper oxidases that catalyse the four-electron red

89 the unique reactivity of this and homologous multicopper oxidases that support the essential traffick

90 t ectoine and an unprecedented enrichment of multicopper oxidases, thioredoxin-like proteins, and tra

91 ne of the predicted gene products encoding a multicopper oxidase to validate the screen.

92 energies of the type 1 (T1) Cu site in four multicopper oxidases were calculated by combining first

93 3 protein from Saccharomyces cerevisiae is a multicopper oxidase with specificity toward Fe(II) and C

94 ion of the type 1 Cu sites of four different multicopper oxidases with two different substrates were