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-Arbuzov and Wittig reactions provided phosphon

3 Michaelis-Menten analysis revealed that the ATPase has a

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

5 Michaelis-Menten experiments showed that Ric-8BFL elevat

6 Michaelis-Menten kinetic parameters from amino acid acti

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

8 Michaelis-Menten kinetics permit estimates of maximal su

9 Michaelis-Menten kinetics provides a solid framework for

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

11 Michaelis-Menten kinetics studies revealed a classic non

12 Michaelis-Menten parameters of 4-nitrophenyl glucopyrano

13 Michaelis-Menten plots were obtained from a single react

14 Michaelis-Menten studies indicated an allosteric mechani

15 Michaelis-Menten transport kinetics indicates that eithe

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

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

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

19 A Michaelis complex of BpGH117 with neoagarobiose reveals

20 A Michaelis-Menten function was fit to each cell's contras

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

22 thrombin species exhibit no variation and a Michaelis-Menten analysis reveals that chemistry of this

23 50 3a2 protein expression was measured and a Michaelis-Menten enzyme kinetic analysis was performed a

24 mical approaches and directly observe both a Michaelis complex and the oxazoline intermediate.

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 It follows a Michaelis-Menten mechanism.

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

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

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

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

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

35 1.5-A crystal structure of CthPnk-D38N in a Michaelis complex with GTP-Mg(2+) and a 5'-OH RNA oligon

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

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

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

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

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

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

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

43 e family GH29 alpha-L-fucosidase unveiling a Michaelis (ES) complex in a (1)C(4) (chair) conformation

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

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

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

51 fonticola and of complexes of its Ser70 Ala (Michaelis) and Glu166 Ala (acylenzyme) mutants with the

52 nding loop and Q142 gives a properly aligned Michaelis complex and facilitates the beta-elimination r

53 2O2 with a detection limit of 0.48microM and Michaelis-Menten constant (Km) value of 44.2microM.

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

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

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

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

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

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

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

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

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

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

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

65 is of ssDNA due to increases in the apparent Michaelis constant, highlighting a role for protein comp

66 The apparent Michaelis constants for Dextranase were estimated based

67 110 +/- 1.3 nA/(mM mm(2)) with the apparent Michaelis-Menten constant (K(M)(app)) derived from an L-

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

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

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

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

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

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

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

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

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

77 We applied Michaelis-Menten kinetics featuring regulatory factors t

78 By applying Michaelis-Menten kinetic analysis to C. difficile spore

79 pose a simple mathematical model by applying Michaelis-Menton equations of enzyme kinetics to study t

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

81 aximal cleavage rates (V(max)) calculated by Michaelis-Menten analysis differed by more than 100-fold

82 ternal metabolites are usually determined by Michaelis-Menten kinetic theory.

83 Stimulus-response functions were fitted by Michaelis-Menten equations and showed significantly lowe

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

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

86 lankton are largely dominated by the classic Michaelis-Menten (MM) uptake functional form, whose cons

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

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

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

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

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

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

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

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

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

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

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

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

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

100 her molecular weight oligomers and displayed Michaelis-Menten kinetics.

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

102 quires zinc for catalytic activity, displays Michaelis-Menten kinetics, and is inhibited by S-adenosy

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

104 Catalytically equilibrating Michaelis complexes (PNP.PO(4).inosine <--> PNP.Hx.R-1-P

105 -Trp oxidations (+/-cytochrome b(5)) exhibit Michaelis-Menten kinetics.

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

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

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

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

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

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

112 hydrolysis of various ceramides and followed Michaelis-Menten kinetics.

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

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

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

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

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

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

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

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

121 s an (O)S(2)/B(2,5) conformation in the GMII Michaelis complex and that the nucleophilic attack occur

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

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

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

125 quantitative analyses using a heterogeneous Michaelis-Menten model.

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

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

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

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

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

131 h the slow substrate D-histidine the initial Michaelis complex undergoes an isomerization involving m

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

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

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

135 osphatase rates and/or by sufficiently large Michaelis-Menten constants and sufficiently low amounts

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

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

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

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

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

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

142 ly by their respective maximum rates V(max), Michaelis constants K(M) and concentrations.

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

144 se stimulation experiments show that the net Michaelis-Menten constant (6.1+/-1.5 mM) is in between G

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

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

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

148 Cytochrome P450 3A4 (CYP3A4) displays non-Michaelis-Menten kinetics for many of the substrates it

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

150 odels have been proposed to describe the non-Michaelis-Menten behavior of human glucokinase.

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

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

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

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

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

156 rks where the individual interactions are of Michaelis-Menten type.

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

158 w the familiar Briggs-Haldane formulation of Michaelis-Menten kinetics derives from the outer (or qua

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

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

161 igns were characterized in vitro in terms of Michaelis-Menten kinetics (V(MAX) and K(M)), sensitivity

162 1.8x10(-9) mol/cm(2)) and the small value of Michaelis-Menten constant (0.76 mM) confirmed an excelle

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

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

165 A mechanism based on Michaelis-Menten kinetics with competitive inhibition is

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

167 ry complex that forms preceding an operative Michaelis complex.

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

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

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

171 trate-metal coordination in the precatalytic Michaelis complex that enhances catalysis.

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

173 ational rearrangement to form the productive Michaelis complex.

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

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

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

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

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

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

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

181 constants were calculated using a reversible Michaelis-Menten model.

182 rain glucose levels and calculate reversible Michaelis-Menten (MM) kinetic parameters.

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

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

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

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

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

188 activity in the colorimetric assay and shows Michaelis-Menten kinetic behavior using Kraft lignin as

189 ng LOXL2 to the same extent and have similar Michaelis constants (K(m) approximately 1 mm) and cataly

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

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

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

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

194 fetimes, and (e) separation of ground-state (Michaelis complexes) from transition-state effects.

195 Modeling of the ternary Michaelis complex implicated ZPI residues Glu-313 and Gl

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

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

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

199 The Michaelis constants (K(m)) for GSSG and beta-NADPH were

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

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

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

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

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

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

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

207 The Michaelis-Menten equation has played a central role in o

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

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

210 The Michaelis-Menten model describing the kinetics of enzyma

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

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

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

214 .9 x 10(7) (here k(cat) and k(uncat) are the Michaelis-Menten enzymatic rate constant and observed un

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

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

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

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

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

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

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

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

223 This general equation encompasses the Michaelis-Menten, Hill, Henderson-Hasselbalch, and Scatc

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

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

226 d to a bimolecular system, which follows the Michaelis-Menten equation if and only if there is no enz

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

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

229 -12 and the substrate on proceeding from the Michaelis complex to the transition state; and (3) a 6 x

230 half upon binding and half on going from the Michaelis complex to the TS.

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

232 nated configuration is preferred both in the Michaelis complex and at the decarboxylation transition

233 pockets, (ii) interacts productively in the Michaelis complex with the substrate, and (iii) stabiliz

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 re is no ground-state destabilization in the Michaelis complexes, but the C1' distortion at the TS is

239 However, an 11-fold increase in the Michaelis constant (over the free solution value) is obs

240 We discuss how parameters in the Michaelis-Menten approximation and in the underlying ODE

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

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

243 Go6976 progressively increased the Michaelis-Menten constant and decreased the Hill coeffic

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

259 Isomerization of the Michaelis complex, yielding an enzyme-substrate complex

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

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

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

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

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

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

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

267 g at R(1)-lead to significant impacts on the Michaelis constant (K(m)), maximum velocity (V(max)), ca

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

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

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

271 eported crystal structures of apo-PTP1B, the Michaelis complex of an inactive mutant, the phosphoenzy

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

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

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

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

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

277 cs of the trimolecular system reduces to the Michaelis-Menten kinetics.

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

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

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

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

282 tant enzymes with ligands representing their Michaelis complexes.

283 ulation of l-Trp kinetics from allosteric to Michaelis-Menten with a concurrent decrease in substrate

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

285 resence of 0-10 mM NaF, and data were fit to Michaelis-Menten curves.

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

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

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

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

292 eaction kinetics of AAO were described using Michaelis-Menten equation.

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

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

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

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

297 nover glycosylase assays are consistent with Michaelis-Menten kinetics.

298 erned by kinetic mass balance equations with Michaelis-Menten type expressions for reaction rates and

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