ライフサイエンスコーパス: AMP-PNP

1 AMP-PNP by itself supported hydrolysis of casein and oth

2 AMP-PNP or ATPgammaS activation required both nucleotide

3 AMP-PNP, a nonhydrolyzable ATP analog, at a concentratio

4 e of fast turnover, the non-hydrolyzable N(3)AMP-PNP bound preferentially to NBD1.

5 5'-Adenylylimidodiphosphate (AMP-PNP) and pyrophosphate, two compounds that disrupt c

6 ysable analogue 5'-adenylylimidodiphosphate (AMP-PNP) and the inhibitory effect of ATPgammaS was reve

7 le ATP analogue 5'-adenylylimidodiphosphate (AMP-PNP) to prevent the run-down of IK(IR))and the Mg2+

8 the presence of 5'-adenylylimidodiphosphate (AMP-PNP), ADP, and ATP, yielding maximal values between

9 e ATP analogue, 5'-adenylylimidodiphosphate (AMP-PNP), bound preferentially to NBD1, but upon additio

10 lls loaded with 5'-adenylylimidodiphosphate (AMP-PNP), KN93, or the CaMKII inhibitory peptide, ICl(Ca

11 nalogue of ATP, 5'-adenylylimidodiphosphate (AMP-PNP), reduced the amplitude and rate of activation o

12 le ATP analogue 5'-adenylylimidodiphosphate (AMP-PNP; 3-5 mM), the leptin-induced hyperpolarization a

13 e ATP analogues 5'-adenylylimidodiphosphate, AMP-PNP (2 mM) or beta, gamma-methylene-adenosine 5'-tri

14 ions were varied by adding ATP, Mg(2+), ADP, AMP-PNP, and KCl.

15 + uptake in the presence of ATP but not ADP, AMP-PNP, or BA.

16 n became cooperative in the presence of ADP, AMP-PNP, or ADP.Vi yielding Hill coefficients of 1.8 and

17 P; no binding occurs in the presence of ADP, AMP-PNP, or ATPgammaS.

18 Strong dissociating agents, AMP-PNP and PPi, made significant differences at all rat

19 cked murine CFTR Cl- channels open, although AMP-PNP increased the Po of murine CFTR.

20 ional reconstruction of endogenous p97 in an AMP-PNP bound state at 24 A resolution.

21 ted whether interactions with the ATP analog AMP-PNP and ADP can shift the conformational ensemble of

22 The nonmetabolizable ATP analog AMP-PNP cannot be substituted for ATP in this action.

23 rfusion with the non-hydrolyzable ATP analog AMP-PNP dramatically reduce the amplitude of dBest1 curr

24 P, and cocrystallization with the ATP analog AMP-PNP suggests that binding of nucleotides regulates t

25 lish that, in the presence of the ATP analog AMP-PNP, or ADP, a maximum of six DnaC monomers bind coo

26 tor with the hydrolysis-resistant ATP analog AMP-PNP.

27 th either ATP or the non-hydrolyzable analog AMP-PNP, and these cycles of elongation and compression

28 presence of the ATP non-hydrolyzable analog AMP-PNP, have been performed, using the fluorescence sto

29 The nonhydrolyzable analog AMP-PNP and ATP-gamma S also stimulate ADP release from

30 e presence of the ATP nonhydrolyzable analog AMP-PNP, the DnaB helicase binds polymer DNA with a site

31 nd is not supported by the nucleotide analog AMP-PNP.

32 tate, ATP, or a non-hydrolyzable ATP analog (AMP-PNP), with differential effects on matrix Ca(2+) buf

33 inability of the nonhydrolyzable ATP analog, AMP-PNP, to cause a similar effect is explained by the i

34 presence of the ATP nonhydrolyzable analog, AMP-PNP, the DnaB helicase fully preserves its hexameric

35 presence of the ATP nonhydrolyzable analog, AMP-PNP, the E. coli DnaB helicase preferentially binds

36 with an RNA oligonucleotide and ATP analogs AMP-PNP, ADP-BeF(3)(-), or ADP-AlF(4)(-).

37 presence of the nonhydrolyzable ATP analogue AMP-PNP (adenyl-5'-yl imidophosphate), the ectonucleotid

38 GspE structures in complex with ATP analogue AMP-PNP and Mg(2+) reveal for the first time, alternatin

39 The nonhydrolyzable ATP analogue AMP-PNP binds in a unique mode that fails to induce lobe

40 d to ADP or the nonhydrolyzable ATP analogue AMP-PNP cannot nucleate actin filaments, but addition of

41 RNA complex, and binding of the ATP analogue AMP-PNP induces a conformational change in the enzyme.RN

42 presence of the nonhydrolyzable ATP analogue AMP-PNP, the drug binding site was in a low-affinity con

43 of ADP or the non-hydrolysable ATP analogue AMP-PNP, the interaction with short ssDNA oligonucleotid

44 by ATP or the non-hydrolyzable ATP analogue AMP-PNP.

45 affinity in the presence of the ATP analogue AMP-PNP.

46 r by using the non-hydrolysable ATP analogue AMP-PNP.

47 PGK in complex with the nucleotide analogue AMP-PNP.

48 he presence and absence of the ATP analogue, AMP-PNP.

49 drolysis products, or with the ATP analogues AMP-PNP or ADP.BeF(x)() the myosin filaments are substan

50 ATP affinity but reduced ATPase activity and AMP-PNP-dependent N-terminal association, whereas the ts

51 T22I displayed enhanced ATPase activity and AMP-PNP-dependent N-terminal dimerization, indicating a

52 he magnitude at which the binding of ADP and AMP-PNP affects the affinity of DNA binding by RSCt sugg

53 uirement for ATP in the cis ring, as ADP and AMP-PNP are unable to promote folding.

54 of the structures presented herein, ADP and AMP-PNP bound, are new structures, and the ADP x AlF3 st

55 litate a robust coprotease activity, ADP and AMP-PNP do not activate RecA at all.

56 ween the structures of RecA bound to ADP and AMP-PNP, which differ from uncomplexed RecA only in a sl

57 head 1 is able to distinguish ATP, ADP, and AMP-PNP to signal head 2 to bind the microtubule and rel

58 sm studies with nucleotide analogues AMP and AMP-PNP, product ADP, and an analogue of the peptide sub

59 dition to their roles in protection, ATP and AMP-PNP also slowly stimulate cyclase activity.

60 When ATP and AMP-PNP were combined in the pipette, however, the maint

61 P; ADP is ineffective, whereas ATPgammaS and AMP-PNP are considerably less able to promote binding an

62 nonhydrolyzable ATP analogues ATPgammaS and AMP-PNP, however, only a single thermal transition is ob

63 When vitamin B12 and AMP-PNP are simultaneously present, the extent of comple

64 dence that in the presence of forked DNA and AMP-PNP, higher-order complexes can form.

65 However, magnesium and AMP-PNP do not affect the mechanism of enzyme-ssDNA inte

66 TP binding was reversed by ATP, AMP-PCP, and AMP-PNP with KIs of approximately 3.2, 4.2, and 4.6 mM,

67 of 5'-adenylamido-diphosphate (AMP-PNP), and AMP-PNP- promoted association of N-termini in intact Hsp

68 ADP and GTP were less potent, and AMP-PNP was inactive.

69 rmation that promotes strand separation, and AMP-PNP does not mimic ATP in this regard.

70 SAXS analyses of ADP, ATPgammaS, ADP-Vi, and AMP-PNP-bound states in solution showed that asymmetric

71 r representative ATP hydrolysis states: APO, AMP-PNP, hydrolysis transition state ADP x AlF3, and ADP

72 ven in the presence of non-hydrolysable ATP (AMP-PNP).

73 hate = tripolyphosphate > ATP-Mg(2+) = ATP = AMP-PNP > ADP = tetrapolyphosphate > cAMP = Mg(2+).

74 y at 10 mM: for myosin II ATP-Mg(2+) = ATP = AMP-PNP (5'-adenylyl imidodiphosphate) > pyrophosphate =

75 The non-hydrolysable analogue of ATP, AMP-PNP, did not substitute for ATP in its effects on th

76 esence of the nonhydrolyzable analog of ATP, AMP-PNP.

77 er preincubation at 30 degrees C unless ATP, AMP-PNP, or GCAP is present.

78 Structures of ArsA with ATP, AMP-PNP, or ADP.AlF(3) bound at the A2 nucleotide bindin

79 d MEK1 (npMEK1) has a high affinity for both AMP-PNP and ADP (Kd approximately 2microM).

80 Most notably, bound AMP-PNP was only observed when trapped in the closed sta

81 hosphorylation of NBD1-R was reduced >75% by AMP-PNP or AMP-PCP (0.25 mM) and >50% by TNP-ATP (0.25 m

82 9D mutation strongly disrupted activation by AMP-PNP but not by ATPgammaS, indicating that these anal

83 The enhanced affinity afforded by AMP-PNP/Mn(2+) may be a useful strategy for increasing a

84 se inhibitor KT5823 or replacement of ATP by AMP-PNP reduced NP(o), while activation of cGMP-dependen

85 Since the delay of closing by AMP-PNP is thought to occur via NBD2, K464A's effect on

86 f ERK2, protection from hydrogen exchange by AMP-PNP binding was observed within conserved ATP bindin

87 contrast, higher protection from exchange by AMP-PNP was observed in active ERK2 compared to inactive

88 membrane domains (TMDs) is not influenced by AMP-PNP binding, a notion confirmed by double electron-e

89 ion is facilitated by Mg(2+) ions but not by AMP-PNP or ATP gamma S.

90 structure, the beta(TP) site was occupied by AMP-PNP and the beta(DP) site by ADP, where its binding

91 - and beta(TP)-subunits are both occupied by AMP-PNP, whereas in the earlier structure, the beta(TP)

92 n the channel was locked in an open state by AMP-PNP.

93 was not mimicked by stable ATP derivatives (AMP-PNP or AMP-PCP) and was abolished by incubation of c

94 of this C-terminal structure also diminished AMP-PNP binding, as well as the catalytic activity of th

95 the presence of 5'-adenylamido-diphosphate (AMP-PNP), and AMP-PNP- promoted association of N-termini

96 dition of 1 mM 5'-adenylylimido-diphosphate (AMP-PNP, an inhibitor of kinesins) or incubation with ki

97 ion coefficient of the ternary complex DnaB-(AMP-PNP)-depsilonA(pepsilonA)19, s20,w = 12.4, suggests

98 the ATP binding site of the 6-PF-2-K domain (AMP-PNP, PO(4), and water).

99 anosarcina mazei PylRS complexed with either AMP-PNP, Pyl-AMP plus pyrophosphate, or the Pyl analogue

100 ower steady-state open probability following AMP-PNP addition (0.68 +/- 0.08 vs. 0.92 +/- 0.03 for wi

101 increased the apparent affinity of Hsp90 for AMP-PNP and completely inhibited the ATPase activity.

102 nucleotides: ATP approximately ATPgammaS >> AMP-PNP approximate GTP > ADP.

103 However, AMP-PNP binding together with K+ can induce a form of Hs

104 the presence of 5'-adenylim-idodiphosphate (AMP-PNP), the motor domain of ncd binds to the microtubu

105 The inhibitor adenylyl imidodiphosphate (AMP-PNP) induces stochastic pauses in the movement of be

106 olysable analogue adenylyl imidodiphosphate (AMP-PNP) partially substituted for ATP, although none wa

107 olyzable analogue adenylyl imidodiphosphate (AMP-PNP) protects equally well.

108 re effective than adenylyl imidodiphosphate (AMP-PNP), a hydrolysis-resistant ATP analog; however, th

109 pipette ATP with adenylyl imidodiphosphate (AMP-PNP), a non-hydrolysable analogue.

110 g in wild type by adenylyl imidodiphosphate (AMP-PNP), a non-hydrolysable ATP analogue, is markedly d

111 or its analogue, adenylyl imidodiphosphate (AMP-PNP), is required for the strong activation.

112 or followed by 5'-adenylyl imidodiphosphate (AMP-PNP)-induced microtubule affinity purification of th

113 In adenylyl-imidodiphosphate (AMP-PNP), a nonhydrolyzable ATP analog, each kinesin-1 d

114 ell as GTP and 5'-adenylyl-imidodiphosphate (AMP-PNP), were accompanied by a corresponding decrease i

115 ) (ATPgammaS) and adenylyl-imidodiphosphate (AMP-PNP).

116 P, 5'-adenylyl beta, gamma-imidodiphosphate (AMP-PNP) and adenosine 5'-(alpha, beta-methylene)triphos

117 log 5'-adenylyl-beta,gamma-imidodiphosphate (AMP-PNP) similarly stabilize the packaged viral genome d

118 , and 5'-adenyl-beta,gamma-imidodiphosphate (AMP-PNP) with the two domains of functional membrane-bou

119 og 5'-adenylyl-beta, gamma-imidodiphosphate (AMP-PNP), ADP, or ADP + Pi using both dimeric (MC1) and

120 with adenylyl beta, gamma-imidodiphosphate (AMP-PNP), some protection from cold dissociation was obs

121 ine 5'-adenylyl-beta,gamma-imidodiphosphate (AMP-PNP), was determined at 2.6 A resolution.

122 ue, 5'-adenylyl beta,gamma-imidodiphosphate (AMP-PNP), was investigated by using the fluorescence ani

123 ue, 5'-adenylyl-beta,gamma-imidodiphosphate (AMP-PNP), which in the gating models was proposed to bin

124 st, 5'-adenylyl-beta,gamma-imidodiphosphate (AMP-PNP).

125 sence of ATPgammaS, adenylyl imidophosphate (AMP-PNP), ADP, diadenosine tetraphosphate and GTPgammaS.

126 (adenosine 5'-beta,gamma-imidotriphosphate [AMP-PNP]) served as the negative control.

127 inished in K464A mutants due to reduction in AMP-PNP's apparent on-rate and acceleration of its appar

128 inhibited with 1 mM of the kinesin inhibitor AMP-PNP (adenylyl-imidodiphosphate) and by anti-kinesin

129 bitor blebbistatin and the kinesin inhibitor AMP-PNP had no significant effect.

130 were inhibited by the ATP synthase inhibitor AMP-PNP (gamma-imino ATP, a nonhydrolyzable ATP analog)

131 es of the protein with 55% displaying intact AMP-PNP and an unphosphorylated substrate and 45% displa

132 ystal structures of apo Pim-1 kinase and its AMP-PNP (5'-adenylyl-beta,gamma-imidodiphosphate) comple

133 bearing the modification on the ribose, MANT-AMP-PNP and MANT-ADP, and on the base, epsilonAMP-PNP an

134 th magnesium 5'-adenylylimidodiphosphate (Mg-AMP-PNP) and 3-phospho-D-glycerate (3-PG) has been deter

135 sidues from the N-terminal domain and the Mg-AMP-PNP interacting with residues from the C-terminal do

136 thout ADP or the nonhydrolysable ATP mimetic AMP-PNP.

137 otubule complexes formed in 1 mM ADP, 0.5 mM AMP-PNP, suggesting that release of a single AMP-PNP mol

138 spite this apparently tight binding, neither AMP-PNP nor ATPgammaS activated even the strongest GOF m

139 TP, but in the presence of K+, Cs+, or NH4+, AMP-PNP activated casein degradation even better than AT

140 Nonhydrolyzable AMP-PNP and adenosine 5'-(beta,gamma-methylenetriphospha

141 In contrast, neither nonhydrolyzable (AMP-PNP, AMP-PCP) nor hydrolyzable ATP analogs (GTP, CTP

142 The presence of either ATP or ADP but not AMP-PNP leads to GroEL dissociation at lower pressures.

143 GroEL-alphabeta complex with Mg-ATP, but not AMP-PNP, resulted in the release of alpha monomers.

144 the presence of a nonhydrolyzable nucleotide AMP-PNP, have been imaged with the atomic force microsco

145 The ITC-determined affinity of nucleotide (AMP-PNP, ADP) binding to the npMEK1.PD0325901 complex wa

146 ration-dependent manner with the addition of AMP-PNP having more pronounced effect.

147 Strikingly, addition of AMP-PNP to the solution containing preformed GroEL14(Gro

148 me as the affinity of ATP, the affinities of AMP-PNP and AMP-PCP are approximately 2 and approximatel

149 ylate cyclase inhibitors; and application of AMP-PNP, a competitive substrate for adenylate cyclase.

150 Although binding of AMP-PNP is not disrupted by the mutation, the apparent a

151 We find that binding of AMP-PNP shifts the ensemble towards more extended rather

152 he dissociation rate on the concentration of AMP-PNP and ADP indicated that polypeptide dissociation

153 presence of the saturating concentration of AMP-PNP, the sedimentation coefficient of the hexamer is

154 t from pauses occurs at 2 s-1 independent of AMP-PNP concentration.

155 Interaction of AMP-PNP-Mg(2+) and a MBP that is locked in a closed conf

156 3) The binding mode of AMP-PNP to Pim-1 kinase is unique and does not involve a

157 isplaying transfer of the gamma-phosphate of AMP-PNP onto the substrate peptide yielding AMP-PN and a

158 ing the metal ion and the gamma phosphate of AMP-PNP.

159 ation of wild-type kinase in the presence of AMP-PNP (an unhydrolyzable ATP analog) or the autophosph

160 f RSCt for DNA is reduced in the presence of AMP-PNP and ADP in a concentration-dependent manner with

161 F(1)-ATPase, crystallized in the presence of AMP-PNP and ADP, but in the absence of azide, has been d

162 sin bound to microtubules in the presence of AMP-PNP and found close agreement with previous models d

163 , DnaC-DnaB-ssDNA, formed in the presence of AMP-PNP as compared to ADP.

164 (binding to microtubules in the presence of AMP-PNP but not ATP).

165 Moreover, the presence of AMP-PNP diminishes the intrinsic affinity of the PriA pr

166 main to the protofilament in the presence of AMP-PNP is very similar for both motors.

167 d-type Rad51 bound to DNA in the presence of AMP-PNP was trapped in the elongated state.

168 hout the kinase extension in the presence of AMP-PNP.

169 cts bound to microtubules in the presence of AMP-PNP.

170 4 (GroES7) complex formed in the presence of AMP-PNP.

171 Substitution of AMP-PNP or ADP for ATP markedly prolonged the decay of I

172 tants reveal that nucleotide binding (ADP or AMP-PNP (adenosine 5'-(beta,gamma-imino)triphosphate)) i

173 In contrast, in the presence of ADP or AMP-PNP only one molecule of oligomeric GroES can be tig

174 n the presence of a 10-fold excess of ADP or AMP-PNP over ATP.

175 0 mM KCl the addition of ATP, but not ADP or AMP-PNP, resulted in a time-dependent, linear increase i

176 as well as in the presence of either ADP or AMP-PNP.

177 or both npMEK1 and pMEK1 using either ADP or AMP-PNP.

178 g currents were repeatedly evoked in ADP- or AMP-PNP-loaded cells, but dialysis of adenosine 5'-O-(3-

179 Binding of ATP or AMP-PNP (adenosine 5'-(beta, gamma-imino)triphosphate),

180 While ATP or AMP-PNP (adenylyl-imidodiphosphate) binding to wild-type

181 Interestingly, ATP or AMP-PNP prevented the effects of Pi on Ca(2+) uptake.

182 h more slowly, and is facilitated by ATP (or AMP-PNP) and Ca(2+).

183 n had no effect, whereas perfusion of ATP or AMP-PNP, a nonhydrolyzable analog of ATP, significantly

184 s and prevented further activation by ATP or AMP-PNP.

185 ssary to accommodate the cryo-EM map of "p97-AMP-PNP", suggesting a change in the orientation of N do

186 d [gamma-32P]ATP in the presence of AMP-PCP, AMP-PNP, or TNP-ATP.

187 orm of scallop Ca-ATPase was occupied by Pi, AMP-PNP, AMP-PCP, or ADP despite the presence of saturat

188 n velocity measurements of the DnaB protein-(AMP-PNP)-5'-fluorescein-(dT)20 ternary complex show that

189 rom the structure of the binary complex RepA-AMP-PNP, indicating that, in equilibrium, the RepA hexam

190 C-terminal truncation mutants also required AMP-PNP-dependent dimerization.

191 t conditions, using either ATP, ATP gamma S, AMP-PNP or ADP as nucleotide cofactors, we always find t

192 AMP-PNP, suggesting that release of a single AMP-PNP molecule from the enzyme is the common rate-limi

193 that, in equilibrium, the RepA hexamer-ssDNA-AMP-PNP complex exists as a mixture of partially open st

194 structure of the tertiary complex RepA-ssDNA-AMP-PNP is very different from the structure of the bina

195 metric bacterial ABC protein that shows that AMP-PNP binds selectively to the noncanonical NBD to pre

196 This argues strongly that AMP-PNP does not inhibit ATP hydrolysis at NBD2 and ther

197 ormational change in a region associated the AMP-PNP adenine binding site.

198 s not adopted by the apo protein, nor by the AMP-PNP bound protein.

199 ate I in TM5 helices, later confirmed by the AMP-PNP-bound BtuCD-F crystal structure.

200 In the AMP-PNP preincubation, low Ca2+ concentrations are not r

201 likely catalysis-competent placement of the AMP-PNP and Mg(2+) components and indicates a tendency f

202 hodopsin is essential for development of the AMP-PNP incubation effect.

203 We also found that the AMP-PNP incubation effect was not altered by addition of

204 1-cis-retinal and hydroxylamine prior to the AMP-PNP incubation and by measurement of the GCAP2 conce

205 translocation channel in agreement with the AMP-PNP.BtuCD-F x-ray structure.

206 Thus, AMP-PNP binding simultaneously protects residues within

207 N-tail mutant had both a slower response to AMP-PNP (activation half-time of 140 +/- 20 s vs. 21 +/-

208 t exhibited a markedly inhibited response to AMP-PNP, a poorly hydrolysable ATP analogue that can nea

209 , beta,gamma-imidoadenosine 5'-triphosphate (AMP-PNP), and copper and undergoes nucleotide-dependent

210 , beta,gamma-imidoadenosine-5'-triphosphate (AMP-PNP), have been examined, using the fluorescence int

211 o beta,gamma-imidoadenosine 5'-triphosphate (AMP-PNP).

212 adenosine 5'-(beta,gamma-imido)triphosphate (AMP-PNP) bound at the degenerate site.

213 adenosine 5'-(beta,gamma-imido)triphosphate (AMP-PNP), and maleate.

214 adenosine-5'-(beta,gamma-imido)triphosphate (AMP-PNP), even though it cannot support steady-state cat

215 adenosine-5'-(beta,gamma-imido)triphosphate (AMP-PNP), onto a substrate peptide within protein crysta

216 adenosine 5'-[beta,gamma-imido]triphosphate (AMP-PNP), a non-hydrolyzable ATP analog, has no effect o

217 adenosine 5'-(beta,gamma-imino)triphosphate (AMP-PNP) and adenosine 5'-O-(thiotriphosphate) (ATPgamma

218 denosine 5'-(beta,gamma -imino)triphosphate (AMP-PNP) or ADP, less than 10% of the LOOP1 epitopes wer

219 adenosine 5'-(beta,gamma-imino)triphosphate (AMP-PNP), and guanosine 5'-3-O-(thio)triphosphate (GTPga

220 adenosine 5'-(beta,gamma-imino)triphosphate (AMP-PNP), or other NTPs do not support the activity.

221 nformational state of the helicase, with two AMP-PNP molecules bound, has dramatically higher ssDNA-a

222 mutant channels deactivated very slowly upon AMP-PNP or ATPgammaS removal (taudeac approximately 100

223 ATP analog; however, this study mainly used AMP-PNP to focus on the role of adenine nucleotide bindi

224 ographic characterization of inactive versus AMP-PNP-liganded structures of FAK1 showed that a large

225 e from inactivation by NEM is also lost when AMP-PNP is present during the IAAmide treatment.

226 With AMP-PNP, binding of a small amount (<20%) of a second Gr

227 (108-268) holoenzyme structure (1.62 A) with AMP-PNP/Mn(2+) showed that we trapped the RIIbeta subuni

228 mulated 4-6-fold the peptidase activity with AMP-PNP present and eliminated the time lag, but KCl had

229 GTP in the pipette, or by replacing ATP with AMP-PNP or UTP.

230 Movement did not occur without ATP, with AMP-PNP, or with ATP plus antibody.

231 e structure of G. lamblia CK in complex with AMP-PNP.

232 that mediate non-canonical interactions with AMP-PNP.

233 A complex of RON(M1254T) with AMP-PNP and Mg(2+) reveals a substratelike positioning o

234 er segment homogenates are preincubated with AMP-PNP (EC50 = 0.65 +/- 0.20 mM), GCAP2 enhanced the re

235 ent on twitchin phosphorylation is seen with AMP-PNP and ATPgammaS.

236 domain, bound C subunit poorly, whereas with AMP-PNP, a non-hydrolyzable ATP analog, the affinity was

237 Without AMP-PNP, GCAP2 stimulated the control activity only 3-4-

238 ciation of the Mt.MC1 complex at 14 s-1, yet AMP-PNP has no effect on the Mt.MC1 complex.