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 ic domain influencing both the catalytic and Michaelis constants.

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

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

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

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

10 -1 was obtained with this substrate, and the Michaelis constant appears to be considerably higher tha

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

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

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

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

15 The Michaelis constants derived from these data indicate sim

16 Michaelis constants determined for both NAD/propanal and

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

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

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

20 The Michaelis constant for aminoisobutyrate (AIB) binding to

21 The Michaelis constant for ATP was most affected by modifica

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

23 The Michaelis constant for GABA transport is not greatly aff

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

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

26 The Michaelis constant for NaCl depended on the solute used

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

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

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

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

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

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

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

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

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

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

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

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

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

40 The apparent Michaelis constants for Dextranase were estimated based

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

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

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

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

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

46 Michaelis constants for GGPP and Ypt1p were 1.6 and 1.1

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

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

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

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

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

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

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

54 The Michaelis constants for purine bases are altered only sl

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

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

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

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

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

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

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

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

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

64 18K, and E290K) cause large increases in the Michaelis constant indicating a reduced affinity for cyt

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

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

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

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

69 25 cell monolayers transport naproxen with a Michaelis constant (K(m)) and maximum velocity (V(max))

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

92 3-fold less compared with G9aFL, while their Michaelis constants (K(m)) for recombinant H3 were simil

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

117 558 microM to 53 microM, and the interfacial Michaelis constant (Km) was reduced from 0.21 to 0.06 by

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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