ライフサイエンスコーパス: Michaelis

1 Michaelis and Menten's classic 1913 paper on enzyme kine

2 Michaelis-Menten analysis demonstrates that the kinetic

3 Michaelis-Menten apparent constant, KM(app), was determi

4 Michaelis-Menten enzyme kinetic studies provide mechanis

5 Michaelis-Menten kinetic theory does not, therefore, see

6 Michaelis-Menten kinetics permit estimates of maximal su

7 Michaelis-Menten kinetics provides a solid framework for

8 Michaelis-Menten kinetics revealed a Km of 169 mum and a

9 Michaelis-Menten kinetics studies revealed a classic non

10 Michaelis-Menten kinetics was used to treat transitions

11 Michaelis-Menten modeling of the single-light pulse reve

12 Michaelis-Menten parameters of 4-nitrophenyl glucopyrano

13 Michaelis-Menten studies indicated an allosteric mechani

14 Michaelis-Menten transport kinetics indicates that eithe

15 Michaelis-Menten, competitive inhibition, and site-direc

16 us polar interactions in the human uPA:PAI-1 Michaelis complex.

17 MP*Mn(2+) intermediate; ligase*ATP*(Mn(2+))2 Michaelis complex; and ligase*Mn(2+) complex-highlight a

18 crystal structure of the NgrRnl*ATP*(Mn2+)2 Michaelis complex.

19 -AMP*Mn2+ intermediate and a LIG*ATP*(Mn2+)2 Michaelis complex.

20 limitations) allowed the linearization of 7 Michaelis-Menton reactions between 6 species to simulate

21 A Michaelis complex in an (O) S2 conformation, coupled wit

22 A Michaelis complex of BpGH117 with neoagarobiose reveals

23 ation rate (Vmax) of 107 revolutions/s and a Michaelis constant (Km) of 154 muM at 26 degrees C.

24 50 3a2 protein expression was measured and a Michaelis-Menten enzyme kinetic analysis was performed a

25 e extent to which flux can be explained by a Michaelis-Menten relationship between enzyme, substrate,

26 Our process model combined a Michaelis-Menten-type equation of substrate availability

27 Kinetic experiments delineate a Michaelis-Menten-type mechanism, with measured rate acce

28 rate decreases as growth slows, exhibiting a Michaelis-Menten dependence on the abundance of the cell

29 at the kinetics of tethered kinases follow a Michaelis-Menten-like dependence on effective concentrat

30 It follows a Michaelis-Menten mechanism.

31 ycoside substrate reveals a preference for a Michaelis complex in an (O)S2 conformation (consistent w

32 Indeed, the ability of a ligand to form a Michaelis complex and favorable conditions for proton tr

33 step mechanism for chain threading to form a Michaelis complex and that the free energy barrier to ch

34 cles, Nafion(R) and glucose oxidase (GOx), a Michaelis-Menten constant (K'(m)) of 20-30 mM is obtaine

35 t the crystal structures of CthPnk-D38N in a Michaelis complex with GTP*Mg(2+) and a 5'-OH oligonucle

36 1.5-A crystal structure of CthPnk-D38N in a Michaelis complex with GTP-Mg(2+) and a 5'-OH RNA oligon

37 n reaction-diffusion simulations including a Michaelis-Menten expression for the urease reaction with

38 H Family 7 cellobiohydrolase Cel7A, namely a Michaelis complex with a full cellononaose ligand and a

39 experimental setup to enable the study of a Michaelis-Arbuzov reaction at two different temperatures

40 This is the first time that a Michaelis complex of a glycosyltransferase has been desc

41 nd monohydroxy-TriBECH were best fitted to a Michaelis-Menten enzyme kinetic model.

42 inverse least-squares analysis coupled to a Michaelis-Menten prognostic model was conducted to estim

43 al response with time showed a good fit to a Michaelis-Menten surface cleavage model, enabling the ex

44 Here we used a Michaelis-Menten substrate-based kinetics framework to e

45 iency of this approach is demonstrated via a Michaelis-Menten analysis which yields a Michaelis const

46 ds reproducible AcFET characteristics with a Michaelis constant KM of (122 +/- 4) muM for the immobil

47 In the intact PLPS with a Michaelis-like intermediate in the glutaminase active si

48 orable binding of the probe with TrxR with a Michaelis-Menten constant (K(m) ) of 15.89 mum.

49 in the presence of their substrates, with a Michaelis-Menten-like concentration dependence.

50 locity can effectively be described within a Michaelis-Menten framework.

51 a a Michaelis-Menten analysis which yields a Michaelis constant, Km, of 353 muM.

52 e substrates after major rearrangement of a "Michaelis loop" that closes the cleft.

53 und states to stiff and catalytically active Michaelis complexes.

54 2O2 with a detection limit of 0.48microM and Michaelis-Menten constant (Km) value of 44.2microM.

55 )M, current maxima (Imax) of 92.55microA and Michaelis-Menten (Km) constant of 30.48microM.

56 insights gleaned from linking Arrhenius and Michaelis-Menten kinetics for both photosynthesis and so

57 rocesses, we expanded the Dual Arrhenius and Michaelis-Menten model, to apply it consistently for all

58 single-turnover catalytic rate constants and Michaelis constants of the incorporation of the native n

59 en the logarithms of the inhibition (Ki) and Michaelis (Km) constants.

60 Combining nonlinear optical microscopy and Michaelis-Menten kinetics-based simulations, we isolated

61 ark simulated genetic regulatory network and Michaelis-Menten dynamics, as well as real world data se

62 ere tested with respect to kinetic order and Michaelis-Menten kinetics.

63 es involving classic enzymatic reactions and Michaelis-Menten-type kinetic analysis.

64 Apparent Michaelis constants K(M)(app) and j(max) were determined

65 single-cell level, resulting in an apparent Michaelis contant Km of 15.3 muM +/- 1.02 (mean +/- stan

66 ) mol L(-1) (3.4 nmol L(-1)) and an apparent Michaelis-Menten rate constant of 3.2x10(-6)molL(-1), wh

67 C levels showed that V(NO) exhibits apparent Michaelis-Menten behavior for B5 and B5R.

68 t the results based on the measured apparent Michaelis-Menten parameters Km and Vmax.

69 the OHSCs, we obtained the overall apparent Michaelis constant and maximum reaction rate for sequent

70 From these results, apparent Michaelis-Menten constants as well as the kinetic parame

71 The apparent Michaelis constants for Dextranase were estimated based

72 110 +/- 1.3 nA/(mM mm(2)) with the apparent Michaelis-Menten constant (K(M)(app)) derived from an L-

73 The apparent Michaelis-Menten constant (K(M)(app)) of HRP on the nano

74 The apparent Michaelis-Menten constant (K(m)) and Hb adsorption in th

75 The apparent Michaelis-Menten constant (Km(app)) was 694 +/- 8 muM.

76 The apparent Michaelis-Menten constant (KM(app)) was calculated to be

77 The apparent Michaelis-Menten constant (Km(app)) was calculated to be

78 The apparent Michaelis-Menten constant Kapp(M) value was 21 microM.

79 The apparent Michaelis-Menten constant of Hb on the PpPDA@Fe3O4 nanoc

80 of uric acid concentration and the apparent Michaelis-Menten kinetic parameter (Km) is estimated to

81 cm(-2) for the urea biosensor, with apparent Michaelis-Menten constants (KM,app), obtained from the c

82 We applied Michaelis-Menten kinetics featuring regulatory factors t

83 similar form with the mechanistically-based Michaelis-Menten kinetics for enzymatic processes, which

84 ted glucosinolates respond similarly to both Michaelis-Menten and specific activity analyses.

85 dynamics simulations on the covalently bound Michaelis-Menten complex.

86 l change that locks the substrate in a caged Michaelis complex that provides optimal stabilization of

87 activation by stabilization of active caged Michaelis complexes may be generalized to the many other

88 rect initial rate fits can affect calculated Michaelis-Menten or EC(50)/IC(50) kinetic parameters.

89 We applied the classic Michaelis-Menten enzyme kinetics to demonstrate a novel

90 eir mean activity is consistent with classic Michaelis-Menten kinetics.

91 The enzyme exhibits classical Michaelis-Menten kinetics and acts cooperatively with a

92 We used two classical Michaelis parameters, Vmax and KM, to kinetically charac

93 A model of the acetyl-CoA Michaelis complex demonstrates the compression anticipat

94 del is based on a hybrid framework combining Michaelis-Menten and mass action kinetics for the mitoti

95 ined a diffusion equation with a competitive Michaelis-Menten equation.

96 for nitrite oxidation assuming one-component Michaelis-Menten kinetics.

97 , were better described with a two-component Michaelis-Menten model, indicating a high-affinity compo

98 in less than 5 min, resulting in conclusive Michaelis-Menten and inhibition curves.

99 with comparable accuracy to the conventional Michaelis-Menten formalism.

100 arbitrary complexity beyond the conventional Michaelis-Menten scheme, which unrealistically forbids p

101 s significantly lower than the corresponding Michaelis constant, for example, in the Omnia assays of

102 We exploited the abundance-dependent Michaelis-Menten kinetics of trypsin digestion to select

103 ase (OGT) as a model system through detailed Michaelis-Menten kinetic analysis of various substrates

104 these experiments with previously determined Michaelis-Menten constants (Kms) for the enzyme activity

105 Using this assay, we determined Michaelis-Menten kinetic constants (K(m), k(cat), and k(

106 NDC1 displayed Michaelis-Menten kinetics and was markedly inhibited by

107 The two Ptr4CLs exhibited distinct Michaelis-Menten kinetic properties.

108 maximal velocities V(max) and the effective Michaelis-Menten constants K(M) under physiologically re

109 cysteine uptake by transporters that exhibit Michaelis-Menten kinetics.

110 P2 substrates CCK8 and vasopressin exhibited Michaelis-Menten kinetics independent of membrane choles

111 ese structures closely resemble the expected Michaelis complexes with the pro-R hydrogens of the meth

112 We report the first Michaelis-like complex structures of MASP-1 and MASP-2 f

113 yosin, though the Km(app) (apparent (fitted) Michaelis-Menten constant) of F-actin speed with ATP tit

114 that long-chain (C14-C18) substrates follow Michaelis-Menten kinetics, whereas short and medium chai

115 rates of H(+) gradient dissipation followed Michaelis-Menten kinetics, suggesting the involvement of

116 Influx followed Michaelis-Menten kinetics for NH3 (but not NH4(+)), as a

117 PGE2/glutathione transport followed Michaelis-Menten kinetics irrespective of cholesterol.

118 lements which served as the cornerstones for Michaelis' and Menten's seminal 1913 paper.

119 hase reactor could be described by a fractal Michaelis-Menten model with a catalytic efficiency nearl

120 From Michaelis-Menten analysis, HAWS has a similar K(m) (Mich

121 strates 2,4,6-TCP and 2,4,6-TBP deviate from Michaelis-Menten kinetics at high concentrations.

122 Modeling of the serpin B8-furin Michaelis complex identified serpin exosites in strand 3

123 de class of systems matching classical (e.g. Michaelis-Menten, Hill, Adair) scenarios in the infinite

124 demonstrate a strategy to convert the graded Michaelis-Menten response typical of unregulated enzymes

125 Purified lipase had Michaelis-Menten constant (Km) and catalytic constant (k

126 on of the acyl-enzyme complex from the Henry-Michaelis complex formed by beta-lactam antibiotics and

127 quantitative analyses using a heterogeneous Michaelis-Menten model.

128 decay time constant based on a heterogeneous Michaelis-Menten model.

129 SLC38A9 transports arginine with a high Michaelis constant, and loss of SLC38A9 represses mTORC1

130 I-polyubiquitin chain assembly by hyperbolic Michaelis-Menten kinetics with respect to Ubc5B approxim

131 rative) behavior without DNA but hyperbolic (Michaelis-Menten) kinetics in its presence, consistent w

132 Although the initial Michaelis and final trapped acyl-intermediate complexes

133 factors Xa and IXa by enhancing the initial Michaelis complex interaction of inhibitor with protease

134 .g. degradation rate, production rate, Kcat, Michaelis-Menten constant, etc.) and the initial concent

135 ss-action kinetics, classic enzyme kinetics (Michaelis-Menten, Briggs-Haldane, and Botts-Morales form

136 al amine-borane so that saturation kinetics (Michaelis-Menten type steady-state approximation) operat

137 M values (kcat =catalytic rate constant; KM =Michaelis constant).

138 hat conformational sampling of the LanM/LanA Michaelis complex could play an important role in the ki

139 he use of acetate buffers resulted in larger Michaelis-Menten constants, up to 14.62 +/- 2.03 mM.

140 yme catalysis was taken in 1913, when Leonor Michaelis and Maud Menten published their studies of suc

141 ters were determined from graphics of linear Michaelis-Menten equation, and it was found that investi

142 A low Michaelis-Menten constant (K(m)) of 0.12 mM, indicate th

143 ensitivity (392 mA cm(-2) M(-1)) and a lower Michaelis-Menten constant (0.224 mM).

144 aximal Velocity (Vmax ), and five-fold lower Michaelis Constant (Km ) than previously characterized T

145 is-Menten analysis, HAWS has a similar K(m) (Michaelis constant) as wild type, suggesting initial enz

146 Furthermore, we have measured Michaelis-Menten kinetics on these highly active constru

147 thionine beta-elimination with a near-native Michaelis constant (Km = 3.3 mm) but a poor turnover num

148 We described non-Michaelis-Menten kinetics with equations containing para

149 gopeptidase), we unexpectedly discovered non-Michaelis-Menten kinetics in short time-scale measuremen

150 analytical tools for enzymes displaying non-Michaelis-Menten kinetics are underdeveloped, and transi

151 nd flux are crucial for the emergence of non-Michaelis-Menten kinetics.

152 ACD showed sigmoidal, non-Michaelis-Menten kinetics for actin (K(0.5) = 30 microM)

153 e maximal E3 rates and show that, due to non-Michaelis-Menten behavior, the maximal flux is different

154 The nonlinear Michaelis-Menten (MM) and Hill models best described the

155 n of the substrate by PTPN1 and PTPN2 obeyed Michaelis-Menten kinetics, with KM values of 770 +/- 250

156 The rotation rates obeyed Michaelis-Menten kinetics with a maximal rotation rate (

157 proteinase K, and thermolysin) while obeying Michaelis-Menten kinetics.

158 The observed Michaelis-Menten constant (Km) and catalytic constant (K

159 Together with the disappearance of Michaelis-Menten kinetics on the expanded pi-surfaces of

160 particular application to the evaluation of Michaelis-Menten and EC(50)/IC(50) kinetic parameters, a

161 The low value of 0.13 x 10(-4) M of Michaelis-Menten constant (K(m)) indicate the enhanced a

162 This enables rapid quantification of Michaelis-Menten constants (KM) for different substrates

163 eneralizations of the hyperbolic response of Michaelis-Menten kinetics x/(K+x), with fluctuating K or

164 ent uptake systems in plants with the use of Michaelis-Menten kinetic modeling.

165 1.8x10(-9) mol/cm(2)) and the small value of Michaelis-Menten constant (0.76 mM) confirmed an excelle

166 A lower value of Michaelis-Menten constant (Km), of 0.062 mM for the cova

167 octaose (2.30 A resolution) provide views of Michaelis complexes for a beta-agarase.

168 rised differential equation systems based on Michaelis-Menten kinetics.

169 tion, the effect of multiple active sites on Michaelis-Menten compliant rate accelerations in a porou

170 ry complex that forms preceding an operative Michaelis complex.

171 nalization flux (Jint) followed first-order (Michaelis-Menten) kinetics with a calculated maximum int

172 fferent models were considered: first-order; Michaelis-Menten; reductant; competition; and combined m

173 ts of the temperature dependency of the PEPc Michaelis-Menten constant for its substrate HCO3 (-), an

174 l conformational change to form a productive Michaelis complex with glucuronoxylan.

175 ational rearrangement to form the productive Michaelis complex.

176 tion of the 3D X-ray structure of the pseudo-Michaelis complex of an inactive (D220N) variant of C. p

177 Published Michaelis constants for plant uptake of Cd and Zn likely

178 Here we constructed and validated a putative Michaelis complex in silico and used it to elucidate the

179 uring SNARE-stimulated ATP hydrolysis rates, Michaelis-Menten constants for disassembly, and SNAP-SNA

180 a combination of microscopic reaction rates, Michaelis-Menten constants, and biochemical concentratio

181 meters, such as decay rates, reaction rates, Michaelis-Menten constants, and Hill coefficients.

182 By recasting Michaelis-like functions as thermodynamic functions, we

183 hia coli LigA), captured as their respective Michaelis complexes, which illuminate distinctive cataly

184 dividual initial rate fits and the resulting Michaelis-Menten or EC(50)/IC(50) kinetic model fits, as

185 coli, which exhibits prototypical reversible Michaelis-Menten kinetics.

186 sp and hydrophobic steroid in the reaction's Michaelis complex.

187 rebindings drastically alter the reaction's Michaelis-Menten rate equations.

188 rotenal, beta-apo-14'-carotenal) do not show Michaelis-Menten behavior under the conditions tested.

189 wo most common BSEP variants p.444V/A showed Michaelis-Menten kinetics irrespective of membrane chole

190 Both enzymes showed Michaelis-Menten kinetics with the K(m) lower for protei

191 hat BEF relations, on average, follow simple Michaelis-Menten curves when species are randomly delete

192 response curve than that observed for simple Michaelis-Menten kinetics.

193 icients obtained upon applying DRA to simple Michaelis-Menten type proteomic and gene regulatory syst

194 earlier work from the Hwa lab, a simplified Michaelis-Menten model suggested that the decrease in k(

195 A two-stage, Michaelis-Menten-type kinetic model is proposed by consi

196 n motif are poorly accounted for by standard Michaelis-Menten kinetics, but require more detailed mas

197 This allows us to use standard Michaelis-Menten theory to analyze the time evolution.

198 teractions that destabilize the ground-state Michaelis complex.

199 ing this framework, we also demonstrate that Michaelis-like functions, another class of cis-regulator

200 The Michaelis constant (K(m)) of all FI mutants toward a sma

201 The Michaelis constant (K(M)) value for ferricyanide was 0.8

202 The Michaelis constants (K(M)) scale with the change in k(ca

203 The Michaelis-Menten constant (K(m)) was determined as 3.3 m

204 The Michaelis-Menten constant (Km) and catalytic constant (k

205 The Michaelis-Menten constant (Km) value of Hb at the modifi

206 The Michaelis-Menten constant (Km) was found to be 1.3 nM.

207 The Michaelis-Menten constant, KM , for PO4 remained constan

208 The Michaelis-Menten equation has been widely used for over

209 The Michaelis-Menten equation provides a hundred-year-old pr

210 The Michaelis-Menten kinetic constant (Km) and maximum react

211 The Michaelis-Menten model describing the kinetics of enzyma

212 At its optimal pH of 4.0, the Michaelis-Menten parameters of K(m) and k(cat) for FlgJ

213 utler-Volmer (BV) electrode kinetics and the Michaelis-Menten (MM) formalism for enzymatic catalysis,

214 cytoplasm, and mitochondria approximate the Michaelis constants for sirtuins and PARPs in their resp

215 .9 x 10(7) (here k(cat) and k(uncat) are the Michaelis-Menten enzymatic rate constant and observed un

216 f the enzyme was also well maintained as the Michaelis constant of tyrosinase was determined to be 0.

217 ive mechanism could not be identified as the Michaelis-Menten parameters and maximal rate constants w

218 he substrate-binding energy expressed at the Michaelis complex, while enabling the full and specific

219 ics the enzyme-substrate interactions at the Michaelis complex.

220 that this mode of binding occurs in both the Michaelis and acylenzyme complexes of wild-type SFC-1.

221 ction with substrate as characterized by the Michaelis constant (Km) also exhibited positive catalyti

222 s and mouse liver were well-described by the Michaelis-Menten model.

223 For over a century, the Michaelis-Menten (MM) rate law has been used to describe

224 We characterize the Michaelis complex formed by mono-Zn(II) enzymes, and we

225 blocking the ability of ATP to decrease the Michaelis constant without affecting peptide-dependent a

226 rsed substrate preference by determining the Michaelis-Menten parameters describing the activity of w

227 kinetic model it was possible to extract the Michaelis constant of covalently immobilized penicillina

228 tions catalyzed by these nanorods follow the Michaelis-Menten kinetics.

229 duction by membrane-bound NDH-2 followed the Michaelis-Menten model; however, the maximum turnover wa

230 solvent- and catalyst-free procedure for the Michaelis-Arbuzov reaction under flow conditions was dev

231 bstrate, and an essential Mg(2+) to form the Michaelis complex where the metal cation bridges the pro

232 ates are the apo state (substrate free), the Michaelis complex analogue AK:Arg:Mg.AMPPNP (MCA), a pro

233 In addition, deviations from the Michaelis-Menten model in DNA competition experiments su

234 es is non-competitive, revealing that in the Michaelis complex, substrate does not contact the cataly

235 d 3.0 A from the GTP gamma phosphorus in the Michaelis complex, where it is coordinated by Asn38 and

236 eutral form of substrate predominates in the Michaelis complex.

237 ts support ground-state stabilization in the Michaelis complex.

238 ts demonstrated a consistent decrease in the Michaelis-Menten parameter kM with increasing soil avail

239 t Glu substitution for Ser-497 increased the Michaelis constant (Km) approximately 400%.

240 +/- 0.9 min(-1), P < 0.05) and increased the Michaelis-Menten constant K(M) (204 +/- 6 n(M) to 478 +/

241 d interpretive framework for doing so is the Michaelis-Menten (M-M) model, which is grounded on two a

242 For comparison, we also measure the Michaelis-Menten kinetics of ADAMTS13 cleavage of wild-t

243 e complex with TcUP and sulfate to mimic the Michaelis complex.

244 increased the maximum velocity, but not the Michaelis constant, of the 17,20 lyase reaction.

245 atalytic activity measurements that obey the Michaelis-Menten equation are well established.

246 t the conformational energy landscape of the Michaelis complex analogue is shaped in a way that at ro

247 reveal that it samples the structures of the Michaelis complex analogue or the apo state as its domin

248 some is preorganized in the formation of the Michaelis complex and does not suffer important changes

249 s studied through structural analysis of the Michaelis complex and synthesis and evaluation of novel

250 and kred/Kd, reflecting the breakdown of the Michaelis complex and the reaction of free enzyme with f

251 th the exosite in the x-ray structure of the Michaelis complex confirmed the importance of all residu

252 hate, Mg(2+), and APS provides a view of the Michaelis complex for this enzyme and reveals the presen

253 a P5C/proline analog provides a model of the Michaelis complex formed during hydride transfer.

254 ever, all previous crystal structures of the Michaelis complex mimics of the PKA catalytic subunit (P

255 re limited by a conformational change of the Michaelis complex prior to a rapid S(N)2 reaction with t

256 substrate association (i.e. formation of the Michaelis complex) was almost entirely entropy-controlle

257 eta-phosphate moieties upon formation of the Michaelis complex.

258 P20) and ATP to produce a close mimic of the Michaelis complex.

259 er by only about 8.9 kJ/mol than that of the Michaelis or apo complex conformations with the TSA liga

260 posite was revealed by the high value of the Michaelis-Menten constant (79.3 muM).

261 The low value of the Michaelis-Menten constant (K(m)=0.34 mM) indicates the h

262 The low value of the Michaelis-Menten constant (Km=0.47 mM) indicates the hig

263 stimation of the temperature response of the Michaelis-Menten parameters supports the use of substrat

264 sfying one of the founding hypotheses of the Michaelis-Menten reaction scheme, MM.

265 Based on the Michaelis-Menten plots, the Km with casein as substrate

266 However, its analysis has relied on the Michaelis-Menten reaction mechanism, which remains widel

267 t a two-parameter kinetic model based on the Michaelis-Menten scheme with a time-dependent activity c

268 explained by a simple kinetic principle: the Michaelis-Menten (MM) model.

269 ivity to natriuretic peptide, or reduced the Michaelis constant in the absence of ATP, consistent wit

270 he enzyme-substrate complex representing the Michaelis complex is of specific interest as it can shed

271 ses a single bound acyl-CoA representing the Michaelis complex with the first substrate, whereas the

272 the Q215 and Y217 side chains stabilize the Michaelis complex to OMP for the decarboxylation reactio

273 g energy, which is utilized to stabilize the Michaelis complex, resulting in a decrease in (K(m))(obs

274 t (K(i)) values similar to or lower than the Michaelis-Menten constant (K(m)) values of ATP.

275 hanistic assumptions more realistic than the Michaelis-Menten scheme.

276 ls hidden by conformational changes that the Michaelis complex of the enzyme and natural substrate un

277 We show that the Michaelis constant (KM) of transport from out-to-in is w

278 y with the VSV L protein, we showed that the Michaelis constants for GDP and pppAACAG (VSV mRNA-start

279 d constant (K(s)) was shown to relate to the Michaelis constant for substrate transport (K(m,g)), wit

280 sor exhibited characteristics similar to the Michaelis-Menten model of an enzymatic electrode, due to

281 ational changes involved in transforming the Michaelis complex to the trapped acyl-intermediate compl

282 f the turnover rates of the enzyme using the Michaelis-Menten model.

283 E recognized TAPTA as its substrate with the Michaelis constant Km and Imax equal to 0.24 mM and 0.13

284 tant enzymes with ligands representing their Michaelis complexes.

285 High cholesterol content shifted E17betaG to Michaelis-Menten kinetics.

286 tal conditions for fitting the H-function to Michaelis-Menten kinetics.

287 These methods are not limited to Michaelis-Menten assumptions, and our conclusions hold f

288 The catalytic behavior of Th-MOF tracked Michaelis-Menten equation and the affinity of this nanoz

289 ator, the results of which show that the two Michaelis complexes are in (2) H3 conformations.

290 supramolecular systems follow enzymatic-type Michaelis-Menten kinetics, with competitive product inhi

291 sm by an approach similar to that used under Michaelis-Menten kinetics.

292 s demonstrated that biodegradation underwent Michaelis-Menten kinetics rather than first-order kineti

293 ation (55-70 degrees C) were described using Michaelis-Menten model and first order reaction model, r

294 Enzymatic parameters were determined using Michaelis-Menten and Lineweaver-Burk plots.

295 tion in the human proximal tubule (PT) using Michaelis-Menten kinetics and molar urinary protein meas

296 hese mutations, is expressed at the wildtype Michaelis complex, and ca. 50% is only expressed at the

297 ent pH optima ranged from pH 5.4 to 6.4 with Michaelis-Menten constants between 0.84 +/- 0.09 and 4.6

298 nce in undrugged Escherichia coli cells with Michaelis-Menten binding of drugs that inactivate riboso

299 8)F-FDG, and the results were evaluated with Michaelis-Menten saturation kinetics.

300 A multispecies reactive transport model with Michaelis-Menten kinetics was developed to explain the c