ライフサイエンスコーパス: molybdopterin

1 ynthesis of molybdenum cofactor from Mo-free molybdopterin.

2 he sulfur atoms of a pterin derivative named molybdopterin.

3 th a pyranopterin-dithiolene cofactor termed molybdopterin.

4 of the molybdenum atom to the dithiolene of molybdopterin.

5 l phosphate group similar to that present in molybdopterin.

6 thiolene moiety located on the pyran ring of molybdopterin.

7 the pterin moiety present in precursor Z and molybdopterin.

8 ight thiol-containing compounds cysteine and molybdopterin.

9 ) have been localized to the vicinity of the molybdopterin active site in the X-ray structure of chic

10 gene encodes DMSO reductase, containing the molybdopterin active site.

11 he enzyme is bound to a dinucleotide form of molybdopterin and is coordinated with selenium.

12 d in a mobA(-) Escherichia coli strain lacks molybdopterin and molybdenum but contains a full complem

13 paralogues may explain the formation of both molybdopterin and tungstopterin in this bacterium.

14 this hypothesis for other putatively ancient molybdopterin-based enzymes.

15 ntified biallelic frameshift variants in the molybdopterin binding (MPTb) domain, located upstream of

16 o it, SCO1134-1132, which encodes a putative molybdopterin binding complex.

17 ts that the SE293 gene product may control a molybdopterin binding protein located immediately adjace

18 t, a 974-amino-acid polypeptide containing a molybdopterin-binding domain.

19 ed similarity to an uncharacterized putative molybdopterin-binding oxidoreductase-like protein sharin

20 idase (aoxAB), a c-type cytochrome (cytc2and molybdopterin biosynthesis (chlE) were downstream of aox

21 ure of Escherichia coli strains deficient in molybdopterin biosynthesis (moa) to the purine base N-6-

22 dicted molybdopterin cofactor chaperon clrD, molybdopterin biosynthesis and two genes of unknown func

23 lved in lipid synthesis and secretion and in molybdopterin biosynthesis, as well as in genes with unk

24 To determine the exact role of MoeB in molybdopterin biosynthesis, the protein was purified aft

25 e-5'-triphosphate (GTP) in the first step of molybdopterin biosynthesis.

26 pathways associated with tRNA thiolation and molybdopterin biosynthesis.

27 thionine enzyme, catalyzes the first step in molybdopterin biosynthesis.

28 hat structurally resembles ubiquitin and the molybdopterin biosynthetic protein MoaD.

29 o the ubiquitin activating enzyme E1 and the molybdopterin biosynthetic protein MoeB.

30 (-) and mogA(-) cells are able to synthesize molybdopterin, but both are deficient in molybdenum inco

31 in the biosynthesis of thiamin, menaquinone, molybdopterin, coenzyme F420, and heme.

32 bacterium tuberculosis is able to synthesize molybdopterin cofactor (MoCo), which is utilized by nume

33 The Culex AO sequence contains a molybdopterin cofactor binding domain and two iron-sulfu

34 ing the chlorate reductase clrABC, predicted molybdopterin cofactor chaperon clrD, molybdopterin bios

35 An ancillary role in molybdopterin cofactor metabolism, hypothesized from phy

36 ron, and moaA, involved in biosynthesis of a molybdopterin cofactor of nitrate reductase.

37 es that are responsible for synthesizing the molybdopterin cofactor, an essential cofactor for aldehy

38 coli, which is required for the synthesis of molybdopterin cofactor.

39 Both catalytic enzymes contain molybdopterin cofactors and form distinct phylogenetic c

40 site through relative orientation of the two molybdopterin cofactors, in a variant of the Ray-Dutt tw

41 oxime reducing component (mARC) proteins are molybdopterin-containing enzymes of unclear physiologica

42 f the dimethyl sulfoxide reductase family of molybdopterin-containing enzymes.

43 der aerobic conditions showed an overall low molybdopterin content and an accumulation of cyclic pyra

44 The molybdopterin content of Escherichia coli mod and mog mu

45 The molybdenum and molybdopterin contents of the two samples were comparabl

46 acid hydrolysis, indicated the presence of a molybdopterin cytosine dinucleotide cofactor.

47 iated with a terminal oxo ligand and the two molybdopterin dithiolene ligands have been assigned.

48 xo-Mo(VI) and des-oxo-Mo(IV) forms with both molybdopterin dithiolene ligands remaining coordinated i

49 ernative function, possibly as a carrier for molybdopterin during molybdenum incorporation.

50 the guanine nucleotide which is attached to molybdopterin during the biosynthesis of the molybdenum

51 The bis-molybdopterin enzyme dimethylsulfoxide reductase (DMSOR)

52 Spectral analogy with a mono-molybdopterin enzyme supports the conclusion that in the

53 ons in relation to the existence of separate molybdopterin enzymes catalyzing DMSO reduction and DMS

54 um is part of the catalytic mechanism of bis-molybdopterin enzymes of the dimethyl sulfoxide reductas

55 s makes it a member of a multigene family of molybdopterin enzymes that includes genes for anaerobic

56 f the dimethyl sulfoxide reductase family of molybdopterin enzymes that utilizes NADPH as the direct

57 he role of thiolate ligands of molybdenum in molybdopterin enzymes.

58 ransferase, MobA, which converts MoCo to bis-molybdopterin guanine dinucleotide (bis-MGD), a form of

59 ains selenocysteine (SeCys), molybdenum, two molybdopterin guanine dinucleotide (MGD) cofactors, and

60 cription factor FNR, in molybdenum cofactor (molybdopterin guanine dinucleotide [MGD]) synthesis, or

61 e S-transferase fusion protein, contains the molybdopterin guanine dinucleotide cofactor (MGD) as its

62 H, FDH(Se), from Escherichia coli contains a molybdopterin guanine dinucleotide cofactor and a seleno

63 Mo atom, four S atoms associated with a bis-molybdopterin guanine dinucleotide cofactor, and four to

64 haeroides apo-DMSOR, an enzyme that requires molybdopterin guanine dinucleotide for activity.

65 MobA-mediated conversion of molybdopterin to molybdopterin guanine dinucleotide has been demonstrated

66 mily of bacterial oxotransferases containing molybdopterin guanine dinucleotide indicate a similar po

67 se, which integrates Mo(MGD)2 complex (MGD = molybdopterin guanine dinucleotide) for oxygen atom tran

68 sulfoxide reductase (BSOR) contains the bis(molybdopterin guanine dinucleotide)molybdenum cofactor a

69 tudying the mechanism of assembly of the bis(molybdopterin guanine dinucleotide)molybdenum cofactor i

70 cterial oxotransferases that contain the bis(molybdopterin guanine dinucleotide)molybdenum cofactor.

71 The enzyme contained the prosthetic group, molybdopterin guanine dinucleotide, and did not require

72 hey are unable to catalyse the conversion of molybdopterin guanine dinucleotide, the active form of t

73 ression and characterization of a functional molybdopterin guanine dinucleotide-containing enzyme and

74 inks a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide.

75 a monooxo molybdenum cofactor containing two molybdopterin guanine dinucleotides that asymmetrically

76 insertion into molybdopterin is required for molybdopterin-guanine dinucleotide formation, and that M

77 nsequence, are deficient in the formation of molybdopterin-guanine dinucleotide.

78 ure demonstrates 11 redox centers, including molybdopterin-guanine dinucleotides, five [4Fe-4S] clust

79 involved in the conversion of precursor Z to molybdopterin in the molybdenum cofactor biosynthetic pa

80 XOR requires molybdopterin, iron-sulphur centres, and FAD as cofactor

81 The dithiolene group of molybdopterin is generated by molybdopterin synthase, wh

82 Molybdopterin is required by various molybdoenzymes, suc

83 s demonstrate that molybdenum insertion into molybdopterin is required for molybdopterin-guanine dinu

84 Although the function of the molybdopterin ligand has not yet been conclusively estab

85 41 in proton abstraction and the molybdenum, molybdopterin, Lys44, and the Fe4S4 cluster in electron

86 to the oxidation state, indicating that the molybdopterin may be directly involved in the enzymatic

87 The SNaR consists of the fragments of the Mo-molybdopterin (MO-MPT) binding site and nitrate reductio

88 Escherichia coli MobA, molybdopterin-Mo, GTP, and MgCl(2) are required and suff

89 nalysis shows the enzyme to contain a single molybdopterin mononucleotide and one FAD per alpha beta

90 been shown that conversion of precursor Z to molybdopterin (MPT) by Escherichia coli MPT synthase ent

91 The molybdopterin (MPT) synthase complex in Escherichia coli

92 logous to human MOCS2A, the small subunit of molybdopterin (MPT) synthase.

93 Its basic form comprises a single molybdopterin (MPT) unit, which binds a molybdenum ion b

94 , molybdenum and tungsten are coordinated by molybdopterin (MPT), a tricyclic pyranopterin containing

95 ses a family of related molecules containing molybdopterin (MPT), a tricyclic pyranopterin with a cis

96 ed pterin derivative, usually referred to as molybdopterin (MPT), which coordinates the essential tra

97 We were able to reconstitute molybdopterin (MPT)-free sulfite oxidase in vitro with t

98 sulfur atoms from a pyranopterindithiolate (molybdopterin, MPT) cofactor.

99 rome c(3) (cycA), Fe hydrogenase (hydB), and molybdopterin oxidoreductase (mopB).

100 oding a putative regulatory protein, DmsR, a molybdopterin oxidoreductase of the DMSO reductase famil

101 xified by the previously identified putative molybdopterin oxidoreductase.

102 d to assess differences in reactivity of the molybdopterin site, as well as subsequent electron-trans

103 itionally, we were able to identify putative molybdopterin synthase association pathways and near-cry

104 The structure of molybdopterin synthase in a novel crystal form revealed

105 minal thiocarboxylate on the MoaD subunit of molybdopterin synthase might resemble the ubiquitin-acti

106 thiocarboxylated MoaD, the mechanism of the molybdopterin synthase reaction was examined.

107 The crystal structure of molybdopterin synthase revealed a heterotetrameric enzym

108 5 WW domain, and dimerization of the E. coli molybdopterin synthase subunits.

109 e sets of analyses revealed that paralemmin, molybdopterin synthase sulfurylase, Tel6 oncogene (ETV6)

110 and MoaE (a homolog of the large subunit of molybdopterin synthase) were essential for MoCo-dependen

111 Escherichia coli molybdopterin synthase, the protein responsible for addi

112 olene group of molybdopterin is generated by molybdopterin synthase, which consists of a large (MoaE)

113 eric subunits (MOCO1-A and MOCO1-B) of human molybdopterin synthase, which is involved in the convers

114 n and plant Cnx1, which are also involved in molybdopterin synthesis.

115 or contains a tricyclic pyranopterin, termed molybdopterin, that bears the cis-dithiolene group respo

116 s in Moco biosynthesis, ligation of metal to molybdopterin (the organic component of the cofactor) to

117 The MogA protein exhibits affinity for molybdopterin, the organic component of Moco, and has be

118 binding pocket for the terminal phosphate of molybdopterin, the product of the enzyme, and suggested

119 olecules such as iron-sulfur (FeS) clusters, molybdopterin, thiamin, lipoic acid, biotin, and the thi

120 are involved in the biosynthesis of thiamin, molybdopterin, thioquinolobactin, and cysteine.

121 addition of molybdenum to the dithiolene of molybdopterin to form molybdenum cofactor.

122 st time that the MobA-mediated conversion of molybdopterin to molybdopterin guanine dinucleotide has

123 d molybdenum ligation to de novo synthesized molybdopterin using only purified components and monitor

124 mophilic organisms, could also be ligated to molybdopterin using this system, though not as efficient

125 nversion of a single precursor Z molecule to molybdopterin was observed.

126 onsible for mediating molybdenum ligation to molybdopterin, whereas MogA stimulates this activity in

127 the MoeA protein mediates ligation of Mo to molybdopterin while the MogA protein enhances this proce

128 ar polypeptide fold and active site with two molybdopterins within this family.