ライフサイエンスコーパス: MgATP

1 The equilibrium constants K(1) (MgATP affinity) and K(2) (=k(2)/k(-2), ATP isomerization

2 impact upon many of the cell's more than 600 MgATP-dependent enzymes and every cellular system where

3 eotide conformation occurs transiently after MgATP binds to both NBDs with associated dimerization, a

4 verts 5-aminoimidazole ribonucleotide (AIR), MgATP, and bicarbonate into N(5)-CAIR, MgADP, and P(i).

5 bioassay, we show that equimolar MgCl(2) and MgATP solutions contain similar amounts of free Mg(2+),

6 g the fact that numeric values of Mg(2+) and MgATP concentrations necessary for complete inhibition a

7 tion and allosterically regulates Mg(2+) and MgATP(2-) binding.

8 ystals were grown in the presence of AIR and MgATP.

9 In contrast, both free ATP and MgATP(2-) robustly open the rapidly desensitizing P2X3 s

10 ndent enzyme, catalyzes the bicarbonate- and MgATP-dependent carboxylation of pyruvate to oxaloacetat

11 d MgADP regulation of the K(ATP) current and MgATP regulation of the L-type Ca(2+) current in an ioni

12 catalyzes the coenzyme A (CoA)-dependent and MgATP-dependent cleavage of citrate into oxaloacetate an

13 ar solution accelerated desensitization, and MgATP reactivated TRPM8 channels in excised patches in a

14 ate the inhibition of both electron flux and MgATP hydrolysis by CN-, but not that caused by azide.

15 Mo-nitrogenase, both total electron flux and MgATP hydrolysis with V-nitrogenase were inhibited.

16 Upon the addition of gp41 and MgATP, gp59 dissociates from the complex, and the DNA-bo

17 e with factor Xa and treatment with KNO3 and MgATP did not, however, lead to an increase in passive p

18 finity of the enzyme for ATP, magnesium, and MgATP.

19 west affinity from titrations with MgADP and MgATP are 25 and 37 microM, respectively.

20 gments, numerous reactions utilize MgGTP and MgATP, and Mg2+ also regulates several of the phototrans

21 tudies of RT in the presence of both NVP and MgATP indicate a strong negative cooperativity.

22 ubstrates fructose-6-phosphate (Fru-6-P) and MgATP.

23 Binding of pentulose and MgATP to form the reactive ternary complex is strongly s

24 usoidal analysis while varying phosphate and MgATP concentrations in skinned Drosophila IFM fibers.

25 a summary of the roles of the Fe protein and MgATP hydrolysis, information on the roles of the two me

26 he concerted action of NifZ, Fe protein, and MgATP and that the action of NifZ is required before tha

27 nce of the HscA/HscB co-chaperone system and MgATP.

28 n), a catalytically inactive E2 (Ubc12), and MgATP.

29 .5 and 2.0 mum sarcomere lengths as pCa and [MgATP] varied.

30 ic regulators of K(ATP) channel activity are MgATP and MgADP.

31 flexural rigidity of the actin filaments at [MgATP] </= 0.1 mM and local bending of the filament fron

32 in, and minimally requires 16 magnesium ATP (MgATP), eight protons, and eight electrons.

33 quilibrium-ordered addition of Mg(2+) before MgATP.

34 s preferred in which D-xylulose binds before MgATP.

35 HPPK*MgAMPCPP, because MgAMPCPP is a better MgATP analogue for HPPK with respect to both binding aff

36 istent with an allosteric antagonism between MgATP in one active site and Fru-6-P in a second active

37 We investigated the interactions between MgATP, MgADP, and the sulphonylurea gliclazide with KATP

38 show that the microtubule-Eg5 complex binds MgATP tightly, followed by rapid ATP hydrolysis with a s

39 iation indicating that the myosin head binds MgATP more tightly in the order IIA (8.7 mM(-1)), IID (4

40 ucleotide-binding domains (NBDs), that binds MgATP tightly at stoichiometry of 1 mol/mol Pgp.

41 Mutant E552A/E1197A bound MgATP and MgADP (1 mol/mol) with K(d) 9.2 and 92 microm,

42 ccluded conformation, with one tightly bound MgATP committed to hydrolysis.

43 thway progresses such that the tightly bound MgATP enters the transition state and is hydrolyzed.

44 The Fe protein, with two bound MgATP molecules, transfers one electron to the MoFe prot

45 2 receptor can be activated by free ATP, but MgATP(2-) promotes opening with very low efficacy.

46 that K(B) channels are strongly activated by MgATP (but not ATP(4)(-)) within the physiological range

47 ive to MgATP inhibition and not activated by MgATP.

48 Channel activation by MgATP was not antagonized by either 1 mm AMP or 500 micr

49 otype, characterized by robust activation by MgATP(2-) and weak regulation by Mg(2+).

50 K(ATP) channel unitary conductance, block by MgATP and activation by MgADP, did not differ between th

51 the apparent substrate inhibition caused by MgATP binding is not seen in hybrid tetramers with only

52 block of wild-type channels was increased by MgATP, but this effect was smaller for ND channels; chan

53 n was found to be similar to that induced by MgATP in Escherichia coli F(1)-ATPase molecules.

54 nhances the allosteric inhibition induced by MgATP.

55 Channel activity was inhibited by MgATP (>50 microM) and activated by MgADP (200 microM).

56 ivity of the K(ATP) channel to inhibition by MgATP and this increases the whole-cell K(ATP) current.

57 KATP channel inhibition by MgATP was enhanced in both homozygous (homE1506K) and he

58 ue to a reduced sensitivity to inhibition by MgATP.

59 l currents by reducing channel inhibition by MgATP.

60 In all cases, MgATP is required.

61 d vesicles purified from the mutant catalyze MgATP-dependent [(3)H]MTX uptake at only 40% of the capa

62 assembly of the catalytically active ChlHID-MgATP complex.

63 AAA(+) proteins ChlI and ChlD, form a ChlID-MgATP complex.

64 d facing ATP-binding cassette configuration; MgATP reduces binding affinity via a shift to the outwar

65 Cytoplasmic MgATP, supplied by dialysis at millimolar concentrations

66 astolic quasi-cell-like solutions (cytosolic MgATP, pCa 7) with an EC(50) of 9.0 +/- 0.4 mM.

67 th load-independent than with load-dependent MgATP-induced detachment rate.

68 g and other vital cells via the differential MgATP/ADP-dependent stimulatory actions of their tissue-

69 Isotope partitioning of the dPFK:MgATP complex indicates a random addition of MgATP and F

70 ough which each catalytic site cycles during MgATP hydrolysis as low --> high --> medium --> low.

71 anism, for which both E-MgADP-FAK-tide and E-MgATP-P-FAK-tide dead-end complexes form.

72 teps following the formation of the binary E.MgATP and E.SO4(2-) complexes and preceding the release

73 xyanion dissociation constants of dead end E.MgATP.oxyanion complexes were all increased.

74 n.) Chlorate and perchlorate form dead-end E.MgATP.oxyanion complexes.

75 rate of release of MgATP from the central E:MgATP:F6P complex 4-fold faster than the net rate consta

76 e in the rate of release of MgATP from the E:MgATP:F6P complex, independent of the concentration of F

77 resence of two endogenous channel effectors, MgATP and reduced glutathione, using the planar lipid bi

78 synthetase from Escherichia coli with either MgATP or MgADP/P(i) bound in the active site cleft.

79 unliganded and binary complexes with either MgATP or pyridoxal to 2.1-, 2.6-, and 3.2-A resolutions,

80 ence stoichiometric HscA and HscB and excess MgATP.

81 ed in the presence of up to 60 muM of excess MgATP without nonspecific binding of MgATP to the myosin

82 gor myosin heads to thin filaments following MgATP depletion in the absence of Ca(2+) also changed th

83 ubunit, with widely differing affinities for MgATP or MgADP.

84 ied ABCB6 showed a high binding affinity for MgATP (Kd = 0.18 muM) and an ATPase activity with a Km o

85 tants showed a severely reduced affinity for MgATP at the high affinity site.

86 site of Pfk-2 by increasing its affinity for MgATP with no alteration in the conformation of residues

87 ed in detail, demonstrating low affinity for MgATP, a preference for Mg as a metal cofactor and ATP a

88 Additionally, the Michaelis constants for MgATP and sulfate (or molybdate), the dissociation const

89 a more than 2-fold increase in the kcat for MgATP hydrolysis.

90 r APS (at saturating MgATP) and the K(m) for MgATP (at [APS](opt)) were 4.2 microM and 0.14 mM, respe

91 viscosity effect observed on k(cat)/K(m) for MgATP but not on k(cat)/K(m) for FAK-tide.

92 enerating state by substitution of MgADP for MgATP in maximum contracting solutions resulted in the s

93 tif were removed showed a normal pattern for MgATP binding to the catalytic sites, with a clearly pre

94 ATP binding and equal dissociation rates for MgATP and MgADP.

95 e quite dynamic, many important residues for MgATP binding and phosphoryl transfer in the active site

96 f the actin filament paths suggest that for [MgATP] >/= 0.25 mM, the flexural rigidity of heavy merom

97 m oxaloacetate, the reverse reaction to form MgATP, the oxamate-induced decarboxylation of oxaloaceta

98 e accumulation of the metabolite Mg(2+) from MgATP hydrolysis is required to make dantrolene administ

99 r the formation of profilin-MgATP-actin from MgATP-actin.

100 yosin cross-bridges use chemical energy from MgATP hydrolysis to generate force and shortening in str

101 the biosynthesis of carbamoyl phosphate from MgATP, bicarbonate, and glutamine.

102 yeast guanylate kinase in the complexes GKy.MgATP, GKy.MgADP, and GKy.MgADP.[u-(13)C]GMP were determ

103 At high MgATP concentrations (>0.1 mM), the oligomer forms E(2)P

104 Conversely, high MgATP concentrations reduced the gliclazide concentratio

105 establish that only molybdate, homocitrate, MgATP, and Fe protein are essential for FeMoco maturatio

106 perties of the binary substrate complex HPPK*MgATP be represented by those of HPPK*MgAMPCPP, because

107 g simulations of the apo-enzyme and the HPPK.MgATP complex.

108 rometry to monitor the effect of HscA, HscB, MgATP, and MgADP on the time course of cluster transfer

109 that at least three SUR1 must bind/hydrolyse MgATP to open the mutant K(ATP) channel.

110 Binding of non-hydrolyzable MgATP analogs or ATP in the absence of Mg is sufficient

111 n vitro motility, and only slowly hydrolyzed MgATP.

112 basis, we present evidence for a hyperbolic [MgATP]-velocity relationship of heavy-meromyosin-propell

113 As the hyperbolic [MgATP]-velocity relationship was not consistent with int

114 f protein)(-1), K(mA(MgATP)) = 0.15 mM, K(ia(MgATP)) = 1 mM, K(mB(sulfate)) = 0.16 mM, V(max,r) = 18.

115 imers can all cross-link MTs into bundles in MgATP.

116 n of Ca(2+) current during rapid increase in MgATP, and 4), demonstrates that decreased ATP/ADP ratio

117 r residues are not involved significantly in MgATP- or MgADP-binding or in interdomain communication

118 orylation were consistent with a decline in [MgATP](i) playing a prominent role in mediating inhibiti

119 s K(ATP) channels in two ways: by increasing MgATP activation and by decreasing ATP inhibition.

120 eal that XK has a weak substrate-independent MgATP-hydrolyzing activity, and phosphorylates several s

121 Neither domain significantly influenced MgATP affinity.

122 AlFx and BeFx inhibited MgATP hydrolysis by specific trapping of nucleotides in

123 is actin, M is myosin, D is MgADP, and S is MgATP.

124 tic values k(cat) (0.052 +/- 0.001 s(-1)), K(MgATP) (1.2 +/- 0.1 microM), K(iMgATP) (1.3 +/- 0.2 micr

125 (cat)/K(FAK-tide), while k(cat) and k(cat)/K(MgATP) were both decreased linearly at increasing solven

126 The effect of Mg(2+) is limited to V/K(MgATP), and initial rate studies indicate an equilibrium

127 ktr by 51% despite the presence of 5 mmol/L MgATP.

128 esence--versus in the absence--of the ligand MgATP or the RNA poly(C).

129 ease in the initial rate was observed at low MgATP.

130 This effect of lowered [MgATP] was qualitatively different from that seen when H

131 =10 mM MgATP and had a relatively high K(M) (MgATP) of approximately 1 mM.

132 +/- 5 nmol min(-1) (mg of protein)(-1), K(M)(MgATP) of 0.15 mM].

133 7 micromol min(-1) (mg of protein)(-1), K(mA(MgATP)) = 0.15 mM, K(ia(MgATP)) = 1 mM, K(mB(sulfate)) =

134 n with adenosine triphosphate and magnesium (MgATP) and trap both products in the crystal lattice, we

135 At <10 microM MgATP, E(1)[ATP].Mg.(H(+)):E(2) is formed at a high-affi

136 that under hydrolysis conditions (millimolar MgATP), not only the dimer dissociation rate increases,

137 s was maximal at concentrations of >or=10 mM MgATP and had a relatively high K(M) (MgATP) of approxim

138 es as in inside-out patches exposed to 10 mm MgATP.

139 g ATP hydrolysis, even in the presence of mm MgATP, and that the dissociation occurs following each h

140 finity for [ATP](i) (67% reduction with 6 mm[MgATP](i)).

141 ngth, 2.5 microm) from rabbit psoas muscle; [MgATP] was 4.6 mM, pH 7.1 and ionic strength was 200 mM.

142 ength 2.5 microm) from rabbit psoas muscle; [MgATP] was 4.6 mm, pH 7.1, ionic strength 200 mm and tem

143 n hybrid tetramers with only a single native MgATP binding site, the proposed kinetic mechanism is no

144 g pure mouse MDR3 P-glycoprotein and natural MgATP and MgADP.

145 se), but unlike the case for Mo-nitrogenase, MgATP hydrolysis was also inhibited by CN-.

146 on to previous data showing a nonhyperbolic [MgATP]-velocity relationship when actin filaments are pr

147 Neither MgADP nor MgATP-gamma-S could replace MgATP.

148 Remarkably, MgAMP and MgADP but not MgATP protected PFK-1 against inhibition by palmitoyl-Co

149 ATP inhibition, by enhancing the ability of MgATP to stimulate channel activity.

150 tituted with these mutants in the absence of MgATP(2-), the condition conducive to rigor cross-bridge

151 In the absence of MgATP, gliclazide block was similar for wild-type channe

152 cs simulations in the presence or absence of MgATP.

153 y MgADP in either the presence or absence of MgATP.

154 d with CuCl(2) in the presence or absence of MgATP.

155 ve forms of ATP and found that the action of MgATP(2-) and ATP(4-) differs between subtypes of P2X re

156 ulted from an enhanced stimulatory action of MgATP.

157 MgATP complex indicates a random addition of MgATP and F6P at low Mg(2+), with the rate of release of

158 n be contrasted with the ordered addition of MgATP prior to F6P at high Mg(2+).

159 With addition of MgATP, differences were significant at high levels of ac

160 98 s(-1)), an exceptionally weak affinity of MgATP for myosin (association constant, 0.2 mM(-1)), and

161 +) (but not Na(+)) increases the affinity of MgATP in a saturable fashion.

162 We observed synergistic binding of MgATP and kinase to the sensor, which was used to develo

163 e propose that upon initial loose binding of MgATP at two nucleotide-binding domains (NBDs), together

164 e, and R92 is dispensable for the binding of MgATP but plays a role in facilitating the binding of HP

165 lanine increases the K(d) for the binding of MgATP by a factor of 3, whereas the K(d) for HP increase

166 Binding of MgATP reduces the fraction of RT bound to NVP, as indica

167 excess MgATP without nonspecific binding of MgATP to the myosin.

168 protein and indicates that, upon binding of MgATP, the Fe protein undergoes a dramatic conformationa

169 dly accelerated the rate of tight binding of MgATP, whereas it did not effect the rate of dissociatio

170 The association constant of MgATP to cross-bridges (K(1)) after reconstitution of Tm

171 actions, enhancing the stimulatory effect of MgATP (which is mediated via SUR1).

172 microm eosin, indicating that the effect of MgATP is due to interactions within the nucleotide-bindi

173 The stimulatory effect of MgATP mediated by the regulatory sulphonylurea receptor

174 iclazide abolished the stimulatory effect of MgATP on all channels.

175 her reconstituted with Tn, and the effect of MgATP on the rate constants (K(1), K(2)) was studied.

176 The effect of MgATP was inhibited by 3 structurally different compound

177 hosphatidylinositol abolished this effect of MgATP, suggesting that it activated TRPV1 by generating

178 activated at 20 degrees C and the effects of MgATP, phosphate (P, P(i)), and MgADP were studied on th

179 the Fe protein likely involves hydrolysis of MgATP and protein-protein interaction between the Fe pro

180 the Fe protein coupled to the hydrolysis of MgATP.

181 The model, implemented with inclusion of MgATP-independent detachment from the rigor state, as su

182 bition upon both [Mg(2+)](i), as an index of MgATP depletion, and channel activity in cell-attached p

183 P to Kir6.2 inhibits, whereas interaction of MgATP with SUR1 activates, K(ATP) channels.

184 in the binding energy or binding kinetics of MgATP.

185 We also speculate that a lack of MgATP due to damaged mitochondria accounts for the decre

186 At likely cellular levels of MgATP (2.5 mM) and sulfate (0.4 mM), the overall endogen

187 cond order rate constant for methanolysis of MgATP) ranged between 10(12)- and 10(14)-fold.

188 Modelling of MgATP binding to XK and the accompanying conformational

189 Omission of MgATP from the intracellular solution accelerated desens

190 in in promoting the effective orientation of MgATP and sulfate at the active site.

191 is significantly reduced in the presence of MgATP and biotin.

192 site (aa 206-218) slowed in the presence of MgATP and increased in the presence of RNA.

193 rom ArsD to ArsA occurred in the presence of MgATP at 23 degrees C but not at 4 degrees C.

194 and the native Fe protein in the presence of MgATP can reversibly cycle between a regular cubane-type

195 Channel activity in the presence of MgATP reflects the balance between the stimulatory (at S

196 able states were apparent in the presence of MgATP revealing new insights into alternating access.

197 ructure of Pfk-2 obtained in the presence of MgATP shows a cation-binding site at the conserved posit

198 parations, were performed in the presence of MgATP using Cs+ as the charge carrier.

199 Crystallization of A-CAT in the presence of MgATP yielded structures with AMP or adenosine in the ca

200 INT bound was 2.6 nmol/mg in the presence of MgATP, Mg(2+), Mg-P(i), or Mg-vanadate with complete inh

201 se polypeptides associate in the presence of MgATP.

202 of interaction with actin in the presence of MgATP.

203 P at low Mg(2+), with the rate of release of MgATP from the central E:MgATP:F6P complex 4-fold faster

204 (2+) is a decrease in the rate of release of MgATP from the E:MgATP:F6P complex, independent of the c

205 rotein conformations that define the role of MgATP in nitrogenase catalysis.

206 om, showed strong temperature sensitivity of MgATP binding and equal dissociation rates for MgATP and

207 other mutants showed lower stoichiometry of MgATP and MgADP binding, in the order Ala > Gln > Asp >

208 ortant role in orienting the triphosphate of MgATP for catalysis.

209 sized that the profilin-induced weakening of MgATP binding by actin reduces the negative free energy

210 timulatory effect of the oxyanion sulfite on MgATP hydrolysis.

211 ed in the presence of MnAMPPNP and GalNAc or MgATP and GalNAc (which resulted in bound products in th

212 as observed in the absence of either HscB or MgATP, and cluster transfer was found to be an ATP-depen

213 SUR1 mutant that is insensitive to MgADP or MgATP activation.

214 of the introduced tryptophans with MgADP or MgATP revealed that both Mg-nucleotide complexes bind to

215 channel and provide evidence that MgADP (or MgATP hydrolysis), acting at the regulatory subunit of t

216 e kcat nor the KM values for fructose-6-P or MgATP.

217 l change upon binding of either pyridoxal or MgATP.

218 hat decrease affinity for Fru-6-P (R243E) or MgATP (F76A/R77D/R82A) allowing us to systematically sim

219 e presence of low concentrations of Fru-6-P, MgATP displays substrate inhibition.

220 The effects of phosphate, MgATP, MgADP and Ca2+ were studied in Tm-reconstituted m

221 K(IR)6 channels from probands in physiologic MgATP.

222 ere not fully blocked, even at physiological MgATP concentrations (1 mmol/L).

223 of unblocked K(ATP) current at physiological MgATP concentrations correlates with the severity of the

224 was abolished by SUR1 mutations that prevent MgATP binding/hydrolysis.

225 energy change for the formation of profilin-MgATP-actin from MgATP-actin.

226 )] structures in the presence of Fe protein, MgATP, and dithionite.

227 f NifZ is required before that of Fe protein/MgATP, suggesting that NifZ may act as a chaperone that

228 ilitates the subsequent action of Fe protein/MgATP.

229 the opposite of those observed with reduced [MgATP].

230 a transient association between the reduced, MgATP-bound Fe protein and the MoFe protein and includes

231 either MgADP nor MgATP-gamma-S could replace MgATP.

232 n Akt1 and these peptide inhibitors requires MgATP.

233 The theoretical K(m) for APS (at saturating MgATP) and the K(m) for MgATP (at [APS](opt)) were 4.2 m

234 on by APS (K(I) of 47.9 microM at saturating MgATP).

235 he turnover rate of hydrolysis of saturating MgATP in the presence of saturating drug concentrations

236 iencies were observed during drug-stimulated MgATP hydrolysis, suggesting the presence of at least th

237 After the addition of stoichiometric MgATP to the alpha(3)(betaM(222)S/Y(345)W)(3)gamma subco

238 tants for the binding of the first substrate MgATP or its analogues.

239 otein and the binding of the first substrate MgATP, but is required for the assembling and sealing of

240 Similar experiments with the poor substrate MgATP leads to 0.9% labeling.

241 ed upon recognition of the correct subtrate, MgATP, in an enzyme-substrate ternary complex.

242 , we report that internal Mg(2+) rather than MgATP inhibits this current.

243 ctivity in excised patches ran down and that MgATP reactivated the channel.

244 These data demonstrate that MgATP provides substrate for lipid kinases, allowing the

245 erences in the Fe protein and indicated that MgATP-bound Fe protein resembles the structure of the Fe

246 nels with diabetogenic receptors reveal that MgATP-dependent hyper-stimulation of mutant SUR can comp

247 The data further suggest that MgATP hydrolysis by the nucleotide-binding domains of SU

248 The MgATP- and MgADP-induced conformational changes in BchL

249 The MgATP-bound conformation of the Fe protein of nitrogenas

250 The MgATP-induced association was strongly inhibited by prio

251 tin-dependent carboxylases and catalyzes the MgATP-dependent carboxylation of biotin, using bicarbona

252 y for galactose metabolism by catalyzing the MgATP-dependent phosphorylation of the C-1 hydroxyl grou

253 minal tail, phosphorylation also exposes the MgATP-binding site on NBD1.

254 nd Mg(2+) in addition to the one forming the MgATP complex is required to bind to cdk5/p25 for its ca

255 ove the concentration needed to generate the MgATP chelate complex, a 15-fold increase in the initial

256 of the native nitrogenase Fe protein in the MgATP-bound state.

257 stance to fluoropyrimidines by mediating the MgATP-dependent transport of 5'-fluoro-2'-deoxyuridine m

258 cations that affects the conformation of the MgATP-binding pocket leading to enzyme activation has be

259 tates indicates that the conformation of the MgATP-bound state in solution does not resemble the stru

260 variant may be a conformational mimic of the MgATP-bound state of the native Fe protein largely on th

261 We therefore studied the MgATP sensitivity of KCNJ11 mutant K(ATP) channels expre

262 no acid deletion recently suggested that the MgATP-bound state of the Fe protein may exist in a confo

263 This site is adjacent to the MgATP allosteric binding site and is only observed in th

264 interface with flavodoxin compared with the MgATP-bound state.

265 of MRP7 is specifically associated with the MgATP-dependent transport of 17beta-estradiol-(17-beta-D

266 echanics experiments, accounts well for the [MgATP]-velocity relationship if nonlinear cross-bridge e

267 Thus MgATP is probably the principal nucleotide regulating ch

268 extent of increase in [Mg(2+)](i) (and thus MgATP depletion) in response to inhibition of oxidative

269 Thus, MgATP acts as a source of Mg(2+) rather than a source of

270 netics of thymosin beta4 (Tbeta4) binding to MgATP-actin monomers.

271 c mechanism to become random with respect to MgATP and F6P and with MgATP released from the central c

272 ant channels were 2.5-fold less sensitive to MgATP inhibition and not activated by MgATP.

273 ng SUR1-Y356C displayed lower sensitivity to MgATP (IC(50) = 24 and 95 micromol/l for wild-type and m

274 X receptors with differential sensitivity to MgATP(2-) and regulation by Mg(2+), and demonstrate that

275 pped single phosphorylation event similar to MgATP.

276 Fe-4S](1+) reduced state (Fe(red)) binds two MgATP and forms a complex with the MoFe protein, with su

277 ssociation, coupled to the hydrolysis of two MgATP.

278 nd ACS-AcsFCh complex remains inactive until MgATP is added, thereby converting inactive to active AC

279 o give fructose 1,6-bisphosphate (FBP) using MgATP as the phosphoryl donor.

280 nges in gj and Vj-gating were observed using MgATP or K2ATP in pipette solutions, which increases or

281 ern in an in vitro motility assay at varied [MgATP].

282 rate that acto.S237C undergoes slow and weak MgATP binding, which limits the rate of steady-state cat

283 d for activation of multisite catalysis when MgATP is the substrate.

284 When [MgATP] was reduced to </=0.1 mM, the actin filament path

285 enger, caused rapid desensitization, whereas MgATP, at concentrations that activate lipid kinases, pr

286 1) to DNA coated with gp32 and gp59, whereas MgATP induces gp32 and gp59 to dissociate, leaving gp41

287 Similarly, under conditions in which MgATP was saturating, Km(Cbl) = 4.1 microm, kcat = 0.06

288 With MgATP as the added ligand, 80% of bound nucleotide was i

289 required for the loading of gp45, along with MgATP, and also for the subsequent binding of polymerase

290 andom with respect to MgATP and F6P and with MgATP released from the central complex half as fast as

291 um or free ATP to HCV helicase competes with MgATP, the true fuel for helicase movements, and leads t

292 idic torsion angle was 30 +/- 5 degrees with MgATP and 28 +/- 5 degrees with MgADP.

293 orsion angle, chi, was 55 +/- 5 degrees with MgATP, and 47 +/- 5 degrees with MgADP, which compares w

294 lization of the ternary complex of HPPK with MgATP and 6-hydroxymethyl-7,8-dihydropterin (HP), and is

295 helical order is substantially improved with MgATP at low temperature or with MgADP or in the absence

296 human IRAK-4 preactivated by incubation with MgATP.

297 ing movement that enhances interactions with MgATP, explaining the observed synergism.

298 e we show that methylphosphonate reacts with MgATP to form alpha-D-ribose-1-methylphosphonate-5-triph

299 interaction of these conserved residues with MgATP is required to stabilize the occluded nucleotide c

300 torsion angles were 55 +/- 5 degrees (GKy x MgATP) and 49 +/- 5 degrees (GKy x MgADP).