ライフサイエンスコーパス: Michaelis constant

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

2 rmine the observed maximum reaction rate and Michaelis constant.

3 d the rate constant of demethylation not the Michaelis constant.

4 were significantly larger than the observed Michaelis constants.

5 ity by increasing ATP affinity, reflected in Michaelis constants.

6 ic domain influencing both the catalytic and Michaelis constants.

7 rable with substrate concentration (apparent Michaelis constant = 0.71 +/- 0.06 micromol/L; maximum v

8 ke activity (comparable with natural enzyme, Michaelis constant = 0.87 millimolars).

9 Cd influx across root-cell plasma membranes (Michaelis constant, 20-40 nm; maximum initial velocity,

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

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

12 -1 was obtained with this substrate, and the Michaelis constant appears to be considerably higher tha

13 on range of approximately 5-100 nM (apparent Michaelis constant approximately 23 nM), with Hill coeff

14 The interfacial Michaelis constants are changed by less than 10-fold for

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

16 al urease between pHout 2.5 and 6.5, and its Michaelis constant at pHout 7.5 was 300 mmol/L but at pH

17 The increase of the apparent Michaelis constant by several orders of magnitude, resul

18 of the wild-type enzyme and a slightly lower Michaelis constant, clearly indicating that the quaterna

19 The Michaelis constants derived from these data indicate sim

20 Michaelis constants determined for both NAD/propanal and

21 Finally, we have shown that the Michaelis constants exhibited by these substrates are ac

22 of 680 +/- 226 microM (n = 3, +/-S.E.), the Michaelis constant for (RS)-mevalonate was increased >30

23 rminal to the catalytic domain and lower the Michaelis constant for acetylated substrates.

24 The Michaelis constant for aminoisobutyrate (AIB) binding to

25 The Michaelis constant for ATP was most affected by modifica

26 The Michaelis constant for carnitine was 0.83 +/- 0.08 mM an

27 The Michaelis constant for GABA transport is not greatly aff

28 Moreover, the Michaelis constant for GST-ATF2 was 12-fold greater than

29 From initial velocity experiments, the Michaelis constant for HVS was 3.5 microM, while CH3 and

30 The Michaelis constant for NaCl depended on the solute used

31 tial activation was dominated by a decreased Michaelis constant for peptide substrate, from KM,PEP >/

32 is), which has lower values for kcat and the Michaelis constant for pyruvate ( K m PYR), was intrinsi

33 (5) The Michaelis constant for recovery of O2 evolution by Ca2+

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

35 Mn2+ ions by electrostatic steering; (2) the Michaelis constant for the calcium requirement for Yss a

36 The Michaelis constant for the methylated peptide (K(m)(pep)

37 Values of the Michaelis constant for the three substrates IMP, GTP, an

38 These substitutions lower K(m3) (the Michaelis constant for trisite ATP hydrolysis) relative

39 titutions confer a 3-4 fold reduction in the Michaelis constant for tRNAs carrying the amber-suppress

40 The pH optimum and measured Michaelis constant for urea of external urease and ureas

41 As a result, the Michaelis constant for Zn2+ uptake was lower in the brea

42 The Michaelis constants for AdoMet (K(m)(AdoMet)) were 12 an

43 MT; EC) was purified to homogeneity, and the Michaelis constants for betaine, dimethylacetothetin, an

44 Steady-state kinetic analyses show that the Michaelis constants for both the dRP and AP lyase activi

45 The apparent Michaelis constants for Dextranase were estimated based

46 The Michaelis constants for DNA (K(m)(CG)) and S-adenosyl-L-

47 nd R845Q showed significant increases in the Michaelis constants for either bicarbonate or carbamoyl

48 erminal regulatory domain did not affect the Michaelis constants for either substrate but did increas

49 The Michaelis constants for fibro-blasts and SCC-25 cells we

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

51 Michaelis constants for GGPP and Ypt1p were 1.6 and 1.1

52 The apparent Michaelis constants for Glc1P, Man1P, and Gal1P are 13.0

53 significantly impair nucleotide binding: the Michaelis constants for IMP and GTP increase by 60-fold

54 oped and used to measure individual rate and Michaelis constants for loading, initiation and extensio

55 Q829A, and R675A mutants displayed elevated Michaelis constants for MgADP in the partial back reacti

56 Additionally, the Michaelis constants for MgATP and sulfate (or molybdate)

57 ts for pyruvate and lactate differ 8-9-fold; Michaelis constants for NADH, NAD(+), and the NAD(+) ana

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

59 The Michaelis constants for purine bases are altered only sl

60 Michaelis constants for pyruvate and lactate differ 8-9-

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

62 have been used to determine equilibrium and Michaelis constants for substrate binding and the rate c

63 rer substrate of IDH-K/P than is EcIDH, with Michaelis constants for the kinase and phosphatase activ

64 e bacterial cells were shown to have similar Michaelis constants for their substrates as previously s

65 Michaelis constants for tRNA(Phe) and DMAPP are 96 +/- 1

66 The Michaelis constants for wild type and K4AK9 ((K(m)(pep))

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

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

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

70 18K, and E290K) cause large increases in the Michaelis constant indicating a reduced affinity for cyt

71 inhibition model, the range of values of the Michaelis constant K(M) in intact PSII (0.5-1.5 mM) was

72 d it significantly decreased the interfacial Michaelis constant K(m)(B).

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

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

75 25 cell monolayers transport naproxen with a Michaelis constant (K(m)) and maximum velocity (V(max))

76 Values for the Michaelis constant (K(m)) and the catalytic constant (k(

77 The Michaelis constant (K(m)) does not change upon substitut

78 s (k(cat)), with an only minor effect on the Michaelis constant (K(m)) explained by decelerated intra

79 r than that with galacturonate; however, the Michaelis constant (K(m)) for galacturonate was lower th

80 ach case, there was a 2-fold increase in the Michaelis constant (K(M)) for oxalate self-exchange (fro

81 ow activity with menaquinone and an apparent Michaelis constant (K(m)) for ubiquinone seven times gre

82 The Michaelis constant (K(m)) for wild-type thrombin-TM comp

83 We postulated that glucokinase (GK), a high-Michaelis constant (K(m)) hexokinase expressed in brain

84 Since the Michaelis constant (K(m)) is the principal determinant o

85 aT2 mediated saturable calcium uptake with a Michaelis constant (K(m)) of 0.66 mm when expressed in X

86 entrative, sodium-dependent mechanism with a Michaelis constant (K(m)) of 153 micro g/ml (501 microM)

87 -AVP complex hydrolyzed the substrate with a Michaelis constant (K(m)) of 3.7 microM and a catalytic

88 lutamine uptake by GlnT is saturable, with a Michaelis constant (K(m)) of 489 +/- 88 microM at pH 7.4

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

90 The system was used both to yield the Michaelis constant (K(m)) of the P450 biotransformation

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

92 , including enzyme turnover number (k(cat)), Michaelis constant (K(m)), and catalytic efficiency (k(c

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

94 Mutation of Cys337 raises the UDP-GlcUA Michaelis constant (K(m)), suggesting that this residue

95 ad marginal effects on the oxidase substrate Michaelis constant (K(m)).

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

97 The Michaelis constants (K(m)) for both 3-phospho-D-glycerat

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

99 3-fold less compared with G9aFL, while their Michaelis constants (K(m)) for recombinant H3 were simil

100 and MeAIB uptake by SAT2 are saturable, with Michaelis constants (K(m)) of 200-500 microm.

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

102 The Michaelis constants (K(m)) were found to be between 5- a

103 meters, including turnover numbers (k(cat)), Michaelis constants (K(m)), and inhibition constants (K(

104 The Michaelis constant, K(M), for the actin activation of S1

105 enzyme, as measured by either changes in the Michaelis constant, K(m), the binding affinity, K(a), or

106 The apparent Michaelis constants, K(M), of the P. multocida HA syntha

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

108 ng and nonspecific binding (reflected in the Michaelis constant Km and the dissociation constant for

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

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

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

112 at is 3 orders of magnitude greater than the Michaelis constant (KM = 68 +/- 4 microM).

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

114 The Michaelis constant (Km) and maximal rate (Vmax) values f

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

116 d, while Y100aHN has been shown to lower the Michaelis constant (KM) by three- to fivefold.

117 K is more active even though the interfacial Michaelis constant (Km) for E54K (0.034 +/- 0.01 mol fra

118 more than 10 times weaker, and the substrate Michaelis constant (Km) is >6-fold greater (weaker bindi

119 In contrast, neither the apparent Michaelis constant (Km) nor the apparent substrate-bindi

120 on; and 3) saturability, with an approximate Michaelis constant (Km) of 0.34 mmol/L and maximum veloc

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

122 e-dependent and saturable having an apparent Michaelis constant (Km) of 22 microM.

123 tant (Ki) equal to 1.9 microM, increased the Michaelis constant (Km) of scuPA/suPAR from 18 nM to 49

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

125 558 microM to 53 microM, and the interfacial Michaelis constant (Km) was reduced from 0.21 to 0.06 by

126 There was a range of Michaelis constants (Km) and maximal transport velocitie

127 X in a dose- and time-dependent manner, with Michaelis constants (Km) being found to be lower than th

128 the two assays have similar sensitivity and Michaelis constants (Km) for adenosine 5'-triphosphate a

129 The Michaelis constants (Km) for DL-potassium mevalonate (28

130 The toxins displayed similar Michaelis constants (Km) for UDP-glucose, but the maxima

131 the UMP/CMP kinase preferentially uses ATP (Michaelis constant [Km] = 29 microM when UMP is the othe

132 alue observed for steady-state O2 evolution (Michaelis constant, KM approximately 1.4 mM), and for li

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

134 The Michaelis constant, Km, of recombinant DG42 in membranes

135 Further, we measure the Michaelis constant, Km, of the rod PDE activated by tran

136 f the bound enzyme (KL), and the interfacial Michaelis constants, KM and kcat.

137 drolysis of the trans peptide divided by the Michaelis constant, ktH/KMtrans = 0.3 min-1 mM-1 was obt

138 fied and characterized with respect to Vmax, Michaelis constants, light and dark decays, quantum yiel

139 tant of 0.16 mm oxalate, comparable with the Michaelis constant observed for oxalate transport (0.23

140 Apparent Michaelis constants obtained from catalytic limiting cur

141 CaT1 mediates saturable Ca(2+) uptake with a Michaelis constant of 0.44 mM.

142 The Michaelis constant of 1.9 micro mol/L agrees with previo

143 apical to basolateral side, saturable with a Michaelis constant of 45+/-9 nM, and partially sensitive

144 luded a saturable component with an apparent Michaelis constant of 45.5 +/- 6.5 mumol/L and a maximum

145 The steady-state Michaelis constant of ATP substrate (K(M,T)) is comparab

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

147 gh analyte concentrations, which exceeds the Michaelis constant of lactate oxidase by several orders

148 ing its last seven amino acids decreased the Michaelis constant of PDE6 by 2.5-fold.

149 , a polyphenol found in red wine, lowers the Michaelis constant of SIRT1 for both the acetylated subs

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

151 cular mass disulfide, mycothione, exhibiting Michaelis constants of 8 and 73 microM for NADPH and myc

152 The Michaelis constants of the D52A and D52A/N46A ChEWL comp

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

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

155 ubstitution did not substantially change the Michaelis constants or alter allosteric regulation of GK

156 at concentrations that correlate with their Michaelis constants or inhibition constants, consistent

157 the corresponding enzyme having an increased Michaelis constant, or K(m), (decreased binding affinity

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

159 he 15 mutations cause large increases in the Michaelis constant (R31E, D34K, D37K, E118K, and E290K).

160 Determination of the apparent Michaelis constants showed that the affinity of the GTP-

161 that possess lipophilic side chains exhibit Michaelis constants that underestimate enzyme affinity.

162 how that while each site maintains a similar Michaelis constant, the catalytic efficiency of M(pro) v

163 is significantly higher than the phosphatase Michaelis constant, two stable steady states of the CaMK

164 ase the dissociation constant (K(D)) and the Michaelis constant under single-turnover conditions (K(M

165 s indicated that the M27 AGP displays normal Michaelis constant values for the substrates glucose-1-p

166 ter for both lysine (Lys) and histidine with Michaelis constant values of 175 and 400 microM, respect

167 Kinetic analysis of this enzyme demonstrated Michaelis constant values of ribulose-5-phosphate (226 m

168 Apparent Michaelis constant values were 0.7 mM for NH4(+), 5.7 mM

169 rrents were saturable with carnitine and the Michaelis constant was 1.8 +/- 0.4 mM.

170 The values of the interfacial Michaelis constant were also little perturbed (ca. 4-fol

171 Michaelis constants were 0.13, 0.8, and 2.6 mM for D-pan

172 Michaelis constants were 156, 17, and 86 microM for CTP,

173 beroylanilide hydroxamic acid (SAHA) and the Michaelis constant, with Fe(II)- and Co(II)-HDAC8 having

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