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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 gen assimilation like cobalamin, riboflavin, molybdopterin and nicotinamide were negatively affected
14  formate dehydrogenase activities as well as molybdopterin and selenocysteine biosynthetic pathways.
15 paralogues may explain the formation of both molybdopterin and tungstopterin in this bacterium.
16 this hypothesis for other putatively ancient molybdopterin-based enzymes.
17  reactions from CO(2) to methane involve one molybdopterin-based two-electron reduction, two coenzyme
18 ntified biallelic frameshift variants in the molybdopterin binding (MPTb) domain, located upstream of
19 o it, SCO1134-1132, which encodes a putative molybdopterin binding complex.
20 ts that the SE293 gene product may control a molybdopterin binding protein located immediately adjace
21 t, a 974-amino-acid polypeptide containing a molybdopterin-binding domain.
22 ed similarity to an uncharacterized putative molybdopterin-binding oxidoreductase-like protein sharin
23 idase (aoxAB), a c-type cytochrome (cytc2and molybdopterin biosynthesis (chlE) were downstream of aox
24 ure of Escherichia coli strains deficient in molybdopterin biosynthesis (moa) to the purine base N-6-
25 dicted molybdopterin cofactor chaperon clrD, molybdopterin biosynthesis and two genes of unknown func
26 lved in lipid synthesis and secretion and in molybdopterin biosynthesis, as well as in genes with unk
27       To determine the exact role of MoeB in molybdopterin biosynthesis, the protein was purified aft
28 e-5'-triphosphate (GTP) in the first step of molybdopterin biosynthesis.
29 pathways associated with tRNA thiolation and molybdopterin biosynthesis.
30 thionine enzyme, catalyzes the first step in molybdopterin biosynthesis.
31 hat structurally resembles ubiquitin and the molybdopterin biosynthetic protein MoaD.
32 o the ubiquitin activating enzyme E1 and the molybdopterin biosynthetic protein MoeB.
33 (-) and mogA(-) cells are able to synthesize molybdopterin, but both are deficient in molybdenum inco
34 in the biosynthesis of thiamin, menaquinone, molybdopterin, coenzyme F420, and heme.
35 bacterium tuberculosis is able to synthesize molybdopterin cofactor (MoCo), which is utilized by nume
36 to enzymatic domains known to coordinate the molybdopterin cofactor (MoCo).
37             The Culex AO sequence contains a molybdopterin cofactor binding domain and two iron-sulfu
38 ing the chlorate reductase clrABC, predicted molybdopterin cofactor chaperon clrD, molybdopterin bios
39                         An ancillary role in molybdopterin cofactor metabolism, hypothesized from phy
40 ron, and moaA, involved in biosynthesis of a molybdopterin cofactor of nitrate reductase.
41 es that are responsible for synthesizing the molybdopterin cofactor, an essential cofactor for aldehy
42 coli, which is required for the synthesis of molybdopterin cofactor.
43               Both catalytic enzymes contain molybdopterin cofactors and form distinct phylogenetic c
44 site through relative orientation of the two molybdopterin cofactors, in a variant of the Ray-Dutt tw
45 oxime reducing component (mARC) proteins are molybdopterin-containing enzymes of unclear physiologica
46 f the dimethyl sulfoxide reductase family of molybdopterin-containing enzymes.
47 der aerobic conditions showed an overall low molybdopterin content and an accumulation of cyclic pyra
48                                          The molybdopterin content of Escherichia coli mod and mog mu
49                           The molybdenum and molybdopterin contents of the two samples were comparabl
50 acid hydrolysis, indicated the presence of a molybdopterin cytosine dinucleotide cofactor.
51 iated with a terminal oxo ligand and the two molybdopterin dithiolene ligands have been assigned.
52 xo-Mo(VI) and des-oxo-Mo(IV) forms with both molybdopterin dithiolene ligands remaining coordinated i
53 ernative function, possibly as a carrier for molybdopterin during molybdenum incorporation.
54  the guanine nucleotide which is attached to molybdopterin during the biosynthesis of the molybdenum
55                                      The bis-molybdopterin enzyme dimethylsulfoxide reductase (DMSOR)
56                 Spectral analogy with a mono-molybdopterin enzyme supports the conclusion that in the
57 ons in relation to the existence of separate molybdopterin enzymes catalyzing DMSO reduction and DMS
58 um is part of the catalytic mechanism of bis-molybdopterin enzymes of the dimethyl sulfoxide reductas
59 s makes it a member of a multigene family of molybdopterin enzymes that includes genes for anaerobic
60 f the dimethyl sulfoxide reductase family of molybdopterin enzymes that utilizes NADPH as the direct
61 he role of thiolate ligands of molybdenum in molybdopterin enzymes.
62 ically, those catalyzing lipopolysaccharide, molybdopterin, FAD, and phylloquinol biosynthesis).
63 ransferase, MobA, which converts MoCo to bis-molybdopterin guanine dinucleotide (bis-MGD), a form of
64 ains selenocysteine (SeCys), molybdenum, two molybdopterin guanine dinucleotide (MGD) cofactors, and
65 cription factor FNR, in molybdenum cofactor (molybdopterin guanine dinucleotide [MGD]) synthesis, or
66 e S-transferase fusion protein, contains the molybdopterin guanine dinucleotide cofactor (MGD) as its
67 H, FDH(Se), from Escherichia coli contains a molybdopterin guanine dinucleotide cofactor and a seleno
68  Mo atom, four S atoms associated with a bis-molybdopterin guanine dinucleotide cofactor, and four to
69 haeroides apo-DMSOR, an enzyme that requires molybdopterin guanine dinucleotide for activity.
70 MobA-mediated conversion of molybdopterin to molybdopterin guanine dinucleotide has been demonstrated
71 mily of bacterial oxotransferases containing molybdopterin guanine dinucleotide indicate a similar po
72 se, which integrates Mo(MGD)2 complex (MGD = molybdopterin guanine dinucleotide) for oxygen atom tran
73  sulfoxide reductase (BSOR) contains the bis(molybdopterin guanine dinucleotide)molybdenum cofactor a
74 tudying the mechanism of assembly of the bis(molybdopterin guanine dinucleotide)molybdenum cofactor i
75 cterial oxotransferases that contain the bis(molybdopterin guanine dinucleotide)molybdenum cofactor.
76   The enzyme contained the prosthetic group, molybdopterin guanine dinucleotide, and did not require
77 hey are unable to catalyse the conversion of molybdopterin guanine dinucleotide, the active form of t
78 ression and characterization of a functional molybdopterin guanine dinucleotide-containing enzyme and
79 inks a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide.
80 a monooxo molybdenum cofactor containing two molybdopterin guanine dinucleotides that asymmetrically
81 insertion into molybdopterin is required for molybdopterin-guanine dinucleotide formation, and that M
82 nsequence, are deficient in the formation of molybdopterin-guanine dinucleotide.
83 ure demonstrates 11 redox centers, including molybdopterin-guanine dinucleotides, five [4Fe-4S] clust
84 involved in the conversion of precursor Z to molybdopterin in the molybdenum cofactor biosynthetic pa
85                                 XOR requires molybdopterin, iron-sulphur centres, and FAD as cofactor
86                      The dithiolene group of molybdopterin is generated by molybdopterin synthase, wh
87                                              Molybdopterin is required by various molybdoenzymes, suc
88 s demonstrate that molybdenum insertion into molybdopterin is required for molybdopterin-guanine dinu
89                 Although the function of the molybdopterin ligand has not yet been conclusively estab
90 41 in proton abstraction and the molybdenum, molybdopterin, Lys44, and the Fe4S4 cluster in electron
91  to the oxidation state, indicating that the molybdopterin may be directly involved in the enzymatic
92 The SNaR consists of the fragments of the Mo-molybdopterin (MO-MPT) binding site and nitrate reductio
93                       Escherichia coli MobA, molybdopterin-Mo, GTP, and MgCl(2) are required and suff
94 nalysis shows the enzyme to contain a single molybdopterin mononucleotide and one FAD per alpha beta
95 been shown that conversion of precursor Z to molybdopterin (MPT) by Escherichia coli MPT synthase ent
96                                          The molybdopterin (MPT) synthase complex in Escherichia coli
97 logous to human MOCS2A, the small subunit of molybdopterin (MPT) synthase.
98            Its basic form comprises a single molybdopterin (MPT) unit, which binds a molybdenum ion b
99 , molybdenum and tungsten are coordinated by molybdopterin (MPT), a tricyclic pyranopterin containing
100 ses a family of related molecules containing molybdopterin (MPT), a tricyclic pyranopterin with a cis
101 ed pterin derivative, usually referred to as molybdopterin (MPT), which coordinates the essential tra
102                 We were able to reconstitute molybdopterin (MPT)-free sulfite oxidase in vitro with t
103  sulfur atoms from a pyranopterindithiolate (molybdopterin, MPT) cofactor.
104 enum in Moco is the pyranopterin dithiolene (molybdopterin, MPT).
105 rome c(3) (cycA), Fe hydrogenase (hydB), and molybdopterin oxidoreductase (mopB).
106 oding a putative regulatory protein, DmsR, a molybdopterin oxidoreductase of the DMSO reductase famil
107 e transcripts for short-chain dehydrogenase, molybdopterin oxidoreductase, and polyketide cyclase.
108 xified by the previously identified putative molybdopterin oxidoreductase.
109 d to assess differences in reactivity of the molybdopterin site, as well as subsequent electron-trans
110 itionally, we were able to identify putative molybdopterin synthase association pathways and near-cry
111                             The structure of molybdopterin synthase in a novel crystal form revealed
112 minal thiocarboxylate on the MoaD subunit of molybdopterin synthase might resemble the ubiquitin-acti
113  thiocarboxylated MoaD, the mechanism of the molybdopterin synthase reaction was examined.
114                     The crystal structure of molybdopterin synthase revealed a heterotetrameric enzym
115 5 WW domain, and dimerization of the E. coli molybdopterin synthase subunits.
116 e sets of analyses revealed that paralemmin, molybdopterin synthase sulfurylase, Tel6 oncogene (ETV6)
117  and MoaE (a homolog of the large subunit of molybdopterin synthase) were essential for MoCo-dependen
118                             Escherichia coli molybdopterin synthase, the protein responsible for addi
119 olene group of molybdopterin is generated by molybdopterin synthase, which consists of a large (MoaE)
120 eric subunits (MOCO1-A and MOCO1-B) of human molybdopterin synthase, which is involved in the convers
121 n and plant Cnx1, which are also involved in molybdopterin synthesis.
122 or contains a tricyclic pyranopterin, termed molybdopterin, that bears the cis-dithiolene group respo
123 s in Moco biosynthesis, ligation of metal to molybdopterin (the organic component of the cofactor) to
124       The MogA protein exhibits affinity for molybdopterin, the organic component of Moco, and has be
125 binding pocket for the terminal phosphate of molybdopterin, the product of the enzyme, and suggested
126 olecules such as iron-sulfur (FeS) clusters, molybdopterin, thiamin, lipoic acid, biotin, and the thi
127 are involved in the biosynthesis of thiamin, molybdopterin, thioquinolobactin, and cysteine.
128  addition of molybdenum to the dithiolene of molybdopterin to form molybdenum cofactor.
129 st time that the MobA-mediated conversion of molybdopterin to molybdopterin guanine dinucleotide has
130  mutation resulted in the loss of a specific molybdopterin transferase (moeA), allowing for Fdh2-depe
131 d molybdenum ligation to de novo synthesized molybdopterin using only purified components and monitor
132 mophilic organisms, could also be ligated to molybdopterin using this system, though not as efficient
133 nversion of a single precursor Z molecule to molybdopterin was observed.
134 onsible for mediating molybdenum ligation to molybdopterin, whereas MogA stimulates this activity in
135 nding sites for ferredoxin, nickel-iron, and molybdopterin, whereas the more recent advent of oxygen
136  the MoeA protein mediates ligation of Mo to molybdopterin while the MogA protein enhances this proce
137 ar polypeptide fold and active site with two molybdopterins within this family.

 
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