ライフサイエンスコーパス: Km

1 Km and Vmax values were 79.37mg/ml and 5.13U/ml, respect

2 Km was 4.28+/-0.34mM of the synthetic substrate N-benzoy

3 arbon dioxide reduction (kcat of 46.6 s(-1), Km of 15.7 muM), in an overall reaction that is thermody

4 ly the formate oxidation (kcat of 543 s(-1), Km of 57.1 muM), but also the carbon dioxide reduction (

5 trations [Vmax(app) = 12 nmolgdw(-1)min(-1); Km(app) = 180 nM; threshold = 130 pM in the Deltahyd23 (

6 process [Vmax(app) = 2.5 nmolgdw(-1)min(-1); Km(app) = 50 nM; threshold = 50 pM in the Deltahyd13 (Hy

7 structure at extremely fine scales (below 10 Km) in some regions, including Galicia.

8 orresponding wavelengths from 1000 Km to 100 Km.

9 LF) with corresponding wavelengths from 1000 Km to 100 Km.

10 0.3 m Na(+) In the presence of 5 mm Ca(2+), Km was further reduced to 0.05 mm, but without an apprec

11 een AveK, SimK 2.0 mm, and the IOLMaster 700 Km was -0.20 diopter (D) and -0.14 D, respectively, whil

12 A Km of approximately 0.80 mM for l-aspartate with a speci

13 chemically identified sites (GC-A-7E) had a Km approximately 10-fold higher than phosphorylated wild

14 Michaelis-Menten kinetics revealed a Km of 169 mum and a Vmax of 7550 nmol/mg/min for the sub

15 Blueberry PPO showed a Km of 15mM and Vmax of 2.57 DeltaA420nm/minx10(-1), dete

16 ified preparation reduced NO in vitro with a Km for NO of 500 nM.

17 TcPho91 is a low-affinity transporter with a Km for Pi in the millimolar range, and sodium-dependency

18 the intracellular H(+) concentration with a Km of 0.65 mm HCO3(-) in WT astrocytes, but slowly raise

19 Kd = 0.18 muM) and an ATPase activity with a Km of 0.99 mM.

20 tT1 converts 8-oxo-dGTP to 8-oxo-dGDP with a Km of approximately 50 muM and Vmax of approximately 0.9

21 700 converts 8-oxo-dGDP to 8-oxo-dGMP with a Km of approximately 9.5 muM and Vmax of approximately 0.

22 indicating a high-affinity component with a Km of just a few nanomolar.

23 l is an excellent synthetic substrate with a Km value of 1.2 mM.

24 p has an in vitro methylglyoxalase activity (Km = 5.5 mM and kcat = 7.8 s(-1)) that is significantly

25 n B cleaved IL-6 with micromolar affinities (Km of 4.7 and 12.0 muM, respectively) and with high effi

26 ion-release dynamics and apparent affinity (Km ) at opposite sides of the membrane, where specific s

27 lta showed nearly 200 times higher affinity (Km) and 150 times higher efficiency (kcat/Km) than wild

28 aled a relatively high perchlorate affinity (Km = 6 mum) and a characteristic substrate inhibition co

29 loss in apparent enzyme-substrate affinity (Km) and approximately 200x decrease in intrinsic catalyt

30 subsites showed similar substrate affinity (Km) values to the wildtype (WT) Km value but had a lower

31 generation potential, FIXa binding affinity, Km for FX of FXase complexes, thrombin activation effici

32 respectively) and similar affinity to Ag(+) (Km approximately 2.5 muM).

33 vates the LGC-55 more efficiently than Amph (Km = 9 and 152 mum, respectively) and generates saturati

34 alase activity with a kcat of 1475 s(-1) and Km of 10.1 +/- 1.7 mm Cyanide and azide inhibited the ca

35 apparent catalytic efficiency decreases, and Km increases with increasing enzyme concentration.

36 sms determining allotypes designated G1m and Km.

37 containing parameters equivalent to kcat and Km and modeled the underlying mechanism by an approach s

38 SsE(M1), SsE(M28), and hpPAF-AH in kcat and Km in hydrolyzing triglycerides, acetyl esters, and PAF

39 tions also significantly affect the kcat and Km values for the substrates.

40 , Cdc28-cyclin B, PKA, and PKC with kcat and Km values of 0.29 s(-1) and 81 nm, 0.11 s(-1) and 127 nm

41 rs by significant increases in both kcat and Km values, supporting suggestions that the earliest pept

42 sidues were mutated to alanine, and kcat and Km were assayed whenever kinase and/or cyclase activity

43 exhibited higher turnover number (kcat) and Km values for deoxyadenosine than for the regular substr

44 ers saturated with Km AMT1;1 = 89 microM and Km AMT2;1 = 123 microM, respectively.

45 ics provided similar Vmax (0.079 mM/min) and Km (0.36 mM) values as those found in the literature.

46 erpretation to obtain, for example, Vmax and Km for an enzymatic reaction in the extracellular space

47 that this isoform conferred higher Vmax and Km values as well as higher acidic pH-dependent activity

48 ndependent activity with comparable Vmax and Km values for different RLCs.

49 he catalytic efficiency with ABTS (kcat(app)/Km(app) = (1.7 x 10(7)) m(-1) s(-1)) is close to that of

50 ies are saturable processes with an apparent Km for Na of 7.3 and 4.3 mM, respectively; and are DIDS-

51 ction of TPP concentration, with an apparent Km of 0.17 +/- 0.064 muM; and highly specific for TPP an

52 The enzyme showed an apparent Km of 0.4 mM, and a specific activity (Vmax) of 20.0 mum

53 phosphate, respectively, as well as apparent Km values 6 and 7 muM for the pyrimidine analogs 5-fluor

54 Kinetic analysis revealed apparent Km values of 20 and 99 muM for the natural substrates ur

55 The apparent Km and Vmax of the amylase were 2.7 mg/ml and 34.30 u/mi

56 The apparent Km for dATP at site 2 is approximately 10 mum for mouse

57 ent with a specific lowering of the apparent Km for dGTP.

58 without significantly affecting the apparent Km for l-proline.

59 etic measurements indicate that the apparent Km of TREX1 for RNA is higher than that for DNA.

60 ron carriers act catalytically with apparent Km = 0.26 mum ferredoxin or 0.42 mum flavodoxin.

61 talyzing mimosine degradation, with apparent Km and Vmax values of 1.16x10(-4) m and 5.05x10(-5) mol

62 centrations of Pah1 (Km = 0.23 mum) and ATP (Km = 5.5 mum).

63 and dependent on the concentrations of ATP (Km = 4.5 mum) and Pah1p (Km = 0.75 mum).

64 The steady-state ATPase Km ,ATP, as well as the dissociation kinetics, reveal an

65 changes, in agreement with the low biosensor Km for O2 (2.6microM).

66 for by temperature-dependent changes in both Km and kcat (three substitutions) or either Km or kcat (

67 min(-1) toward glutathione for human ChaC2; Km of 2.2 +/- 0.4 mm and kcat of 225.2 +/- 15 min(-1) to

68 than ChaC1, although they showed comparable Km values (Km of 3.7 +/- 0.4 mm and kcat of 15.9 +/- 1.0

69 oximately ubiquitin thioester concentration (Km = 44 +/- 6 nm; kcat = 0.020 +/- 0.007 s(-1)) and subs

70 as its substrate with the Michaelis constant Km and Imax equal to 0.24 mM and 0.13 mA cm(-1), respect

71 The Michaelis-Menten kinetic constant (Km) and maximum reaction velocity (Vmax) for free trypsi

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

73 The apparent Michaelis-Menten constant (Km(app)) was calculated to be 1.22 mM.

74 rified lipase had Michaelis-Menten constant (Km) and catalytic constant (kcat) of 0.30mM and 2.16s(-1

75 of 0.48microM and Michaelis-Menten constant (Km) value of 44.2microM.

76 The Michaelis-Menten constant (Km) value of Hb at the modified electrode is 55.4 microM

77 A lower value of Michaelis-Menten constant (Km), of 0.062 mM for the covalently coupled enzyme over

78 low value of the Michaelis-Menten constant (Km=0.47 mM) indicates the high affinity of immobilized u

79 x ), and five-fold lower Michaelis Constant (Km ) than previously characterized TNT-active Arabidopsi

80 ation with a near-native Michaelis constant (Km = 3.3 mm) but a poor turnover number (kcat approximat

81 as characterized by the Michaelis constant (Km) also exhibited positive catalytic cooperativity that

82 or Ser-497 increased the Michaelis constant (Km) approximately 400%.

83 107 revolutions/s and a Michaelis constant (Km) of 154 muM at 26 degrees C.

84 analysis which yields a Michaelis constant, Km, of 353 muM.

85 Pretty good values for kinetic constants Km(app) (6.60mM), Vmax (17.69mumol/min mg protein) and k

86 Conversely, Km allotypes and CD32B or CD32C expression on NK cells d

87 eine, showing different affinities to Cu(+) (Km approximately 1 or 0.5 muM, respectively) and similar

88 rmed by CYP26A1, it was depleted by CYP26A1 (Km = 63 nM and intrinsic clearance = 90 mul/min per pmol

89 ld, by increasing kcat 7-fold and decreasing Km about 40-fold.

90 of 6.7 in the presence of NaCl, demonstrated Km and kcat/Km values for Lys-Ala-MCA of 688 muM and 11.

91 currents saturated with a voltage-dependent Km = 90 microM at -80 mV.

92 substrate parameters show that MAQ displays Km and kcat values essentially the same as those of the

93 e by promoting dNTP binding (decreasing dNTP Km), polymerase stimulates the helicase by increasing th

94 Km and kcat (three substitutions) or either Km or kcat (one substitution each).

95 As estimating Km and kcat requires multiple steps of data manipulation

96 0H2 to thioredoxin via protein-bound flavin; Km values for thioredoxin and F420H2 were 6.3 and 28.6 m

97 shown to possess high NAD(+)-glycohydrolase (Km (NAD) = 68 +/- 3 mum; kcat = 94 +/- 2 min(-1)) activi

98 ased the GMPR activity and increased the GMP Km value 10-fold.

99 pared from human embryonic kidney 293 (HEK) (Km 3.8 microM and Vmax 307 pmol/mg per minute) and HeLa

100 M and Vmax 307 pmol/mg per minute) and HeLa (Km 0.32 microM and Vmax 42 pmol/mg per minute) cells.

101 CO2 actively only above pH 8 and with a high Km ( approximately 34 mM).

102 rase) of HQT had a low pH optimum and a high Km for its substrate, CGA.

103 F-MRP1-enriched membrane vesicles had a high Km value for As(GS)3 (3-6 microM), regardless of the cel

104 mization activity), S84A (good kcat but high Km for l-THA elimination), and S84N mutants (nearly WT e

105 rvations provide an explanation for the high Km of LGK for levoglucosan.

106 tion and a possible explanation for the high Km values that have been noted for some DMSP lyases.

107 was sodium-dependent and exhibited a higher Km for ergothioneine, carnitine, and carnosine compared

108 ongly reduced polymerase activity and higher Km for dNTP during gap-filling.

109 nalysis showed that XXT5 has a 7-fold higher Km and 9-fold lower kcat compared with XXT1 and XXT2.

110 The immobilized enzyme showed higher Km 2.08mg/ml than the free enzyme whose Km is 0.45+/-.05

111 (13)NH4(+) responded with a nearly identical Km.

112 increase in kcat and a 1.4-fold decrease in Km following phosphorylation, providing a 7.4-fold incre

113 Glu25 by Gln caused a >/=25-fold increase in Km.

114 Furthermore, year-to-year variability in Km and Vmax values was significant.

115 olysis of Hsp70 translated into an increased Km for ATP usage by chloroplasts for protein import.

116 ty nitrate transport activity with increased Km, whereas equivalent changes in NPF6.4 (T106) disrupte

117 other three MLCK family members, whereas its Km (RLC and ATP) and KCaM values are similar.

118 t in OmpT catalytic efficiency, with a kcat /Km value of 6.1x10(6) L mol(-1) s(-1) .

119 ants (kcat ) and enzymatic efficiency (kcat /Km ).

120 possesses a catalytic capability with a kcat/Km above 10(5) M(-1) s(-1) at 70 degrees C, and at room

121 was found to be 14.0 +/- 1.2 muM with a kcat/Km of 9.1 x 10(9) M(-1) s(-1).

122 sic specificity and the enzyme activity kcat/Km.

123 um aromaticivorans (kcat = 27 s(-1) and kcat/Km = 1.1 x 10(5) M(-1) s(-1)) were determined.

124 aucimobilis SYK-6 (kcat = 2.2 s(-1) and kcat/Km = 4.0 x 10(4) M(-1) s(-1)) and Novosphingobium aromat

125 ow a strong pH effect on their kcat and kcat/Km constants, with a decrease in kcat/Km of 5500- and 9-

126 he products and determined the kcat and kcat/Km values as 9.3 +/- 0.6 s(-1) and 2.5 +/- 0.2 x 10(7) m

127 e presence of NaCl, demonstrated Km and kcat/Km values for Lys-Ala-MCA of 688 muM and 11.02 muM(-1) s

128 e biochemical parameters (Km, kcat, and kcat/Km) of the recombinant TcP5CDH were determined, exhibiti

129 influence on enzyme catalysis (kcat and kcat/Km), a feature overlooked in previous structural studies

130 DFP formation (Kcat and kcat/Km), DFP decay, and protein-caged hydrated ferric oxide

131 terium isotope effects on both kcat and kcat/Km, from 5 to 11, were observed with both substrates, in

132 higher catalytic efficiency measured as kcat/Km.

133 strate with higher efficiency than Asc (kcat/Km = 2.1 x 10(5) versus 3.5 x 10(4) M(-1)s(-1), respecti

134 Enzyme activity (often quantified by kcat/Km) is the main function of enzyme when it is active aga

135 for substrates with no C17 side chain (kcat/Km >10(5) s(-1) M(-1) for 4-estrendione, 5alpha-androsta

136 but not under subsaturating conditions (kcat/Km ).

137 Its specificity constant (kcat/Km) for Pah1 phosphorylated by Pho85-Pho80 was 1.6-, 4-,

138 d by determining specificity constants (kcat/Km), we show that ClpP1P2 prefers Met >> Leu > Phe > Ala

139 intermediate 6-amino-6-deoxyfutalosine (kcat/Km = 1.8 x 10(3) M(-1) s(-1)), but not the prototypical

140 spectively) and with high efficiencies (kcat/Km of 0.2 and 2.5 (M(-1)/s(-1)) x 10(6), respectively).

141 greater than the catalytic efficiency (kcat/Km = 1.3 x 10(7) M(-1) s(-1)) with this substrate, sugge

142 omain reduces the catalytic efficiency (kcat/Km of AdoMet) of ATXR5 up to 58-fold, highlighting the m

143 xhibiting reduced catalytic efficiency (kcat/Km) at colder temperatures and/or higher efficiency at w

144 The catalytic efficiency (kcat/Km) for the removal of a myristoyl group is slightly hig

145 ain increases the catalytic efficiency (kcat/Km) of D1 ATP hydrolysis 280-fold, by increasing kcat 7-

146 r 2; the relative catalytic efficiency (kcat/Km) of mEar 11 is diminished approximately 1000-1500-fol

147 The efficiency (Kcat/Km) of the AuNP conjugated AOx was increased by 18% from

148 y (Km) and 150 times higher efficiency (kcat/Km) than wild type (WT) PKCdelta toward N(6)-(benzyl)-AT

149 with a two-fold increase in efficiency (Kcat/Km) was achieved by physical entrapment of the activator

150 apparent in vivo catalytic efficiency, kcat/Km , to be lower than in vitro, with significant cell-to

151 le than wild-type rhodanese and exhibit kcat/Km,CN values that are 17- and 1.6-fold higher, respectiv

152 displayed the lowest Km and the highest kcat/Km for phloretin and UDPG compared to all previously rep

153 st kcat/Km value for Neu5Ac and highest kcat/Km values for ManNAc and pyruvate, which makes CgNal fav

154 d kcat/Km constants, with a decrease in kcat/Km of 5500- and 9-fold at pH 10.5, respectively.

155 -THA; approximately 5000-fold change in kcat/Km ratios) alternative substrates.

156 ate ( approximately 1200-fold change in kcat/Km ratios) and l (l-THA; approximately 5000-fold change

157 cat value and that DHX36 binding limits kcat/Km Similar results were obtained for unimolecular DNA G4

158 ported NALs, CgNal exhibited the lowest kcat/Km value for Neu5Ac and highest kcat/Km values for ManNA

159 Determination of kcat/Km showed that the reUmChlE hydrolyzed chlorogenic acid

160 r resulted in a 670-fold stimulation of kcat/Km.

161 lysis of the organophosphate omethoate (kcat/Km of (2.0 +/- 1.3) x 10(-1) M(-1)s(-1)) and paraoxon (k

162 Kinetic isotope effects of 1.5-2.3 (on kcat/Km ) were observed with 3,3-, 4,4-, and 3,3,4,4-deuterat

163 1.3) x 10(-1) M(-1)s(-1)) and paraoxon (kcat/Km of (4.6 +/- 0.8) x 10(3) M(-1)s(-1)), V- and G-agent

164 tion effects on the specificity ratio, (kcat/Km)Trp/(kcat/Km)Tyr, of 15 combinatorial mutants from a

165 ior next to the cleavage site sequence, kcat/Km values increased.

166 ine, with an ~10(4) higher specificity (kcat/Km) for asparagine despite only one methylene difference

167 9 had the highest apparent specificity (kcat/Km) for steroids with an isopropyl side chain at C17, su

168 d not contribute to enzyme specificity (kcat/Km).

169 ons containing O2 but no added H2O2 The kcat/Km for H2O2-driven degradation of chitin was on the orde

170 nitor promoter melting and measured the kcat/Km of 2-mer synthesis to quantify initiation efficiency

171 an for wild-type rhodanese, whereas the kcat/Km,GSSH values were similar for all three enzymes.

172 The kcat/Km,sulfite values for the variants in the sulfur transfe

173 on the specificity ratio, (kcat/Km)Trp/(kcat/Km)Tyr, of 15 combinatorial mutants from a previous stud

174 magnesium concentration (nH = 2) under kcat/Km conditions, suggesting that PRORP1 catalysis is optim

175 boxylation of 5-fluoroorotate (FO) with kcat/Km = 1.4 x 10(-7) M(-1) s(-1).

176 ad substrate promiscuity of Cps2L, with kcat/Km changes for monofluoro substitution at C-2, C-4, and

177 peptidyl-prolyl isomerase activity with kcat/Km of approximately 7.1 mum(-1) s(-1).

178 tic reductions in enzyme activity, with kcat/Km often <1.5% of wild-type.

179 ssays showed unambiguous catalysis with kcat/Km values on the order of 2-50 min(-1) muM(-1) Condensat

180 Mean keratometry (Km) values of IOLMaster 700 were compared for each type

181 its substrate and inhibitor enzyme kinetics (Km and IC50), (2) its amino acid sequence and (3) its ab

182 tion requires Na(+) (Km = 0.12 mm) or Li(+) (Km = 0.25 mm) for activity, indicating that Rnf acts as

183 2months), wide linear range (0.5-24mM), low Km (8.4mM), high Imax (77.2muAcm(-2)), low detection lim

184 difficult to develop because Pim-2 has a low Km for ATP and therefore requires a very potent inhibito

185 essed in either HEK293 or HeLa cells had low Km and Vmax values for As(GS)3, similar to HeLa wild-typ

186 erential product, as demonstrated by its low Km for 5-hydroxyconiferaldehyde.

187 refer to as gpASNase1, has the required low Km property consistent with that possessed by the cell-k

188 In group B, the presence of low-Km hexokinase-I in insulinoma beta-cells (not in adjacen

189 me) (21.3 versus 44.9 nmol/min/mg) and lower Km (substrate concentration at which half-maximal produc

190 ect as low as 1.31 muM of xanthine and lower Km value of 0.018 muM confirming its superior affinity t

191 aded heavy meromyosin 5c) has a 6-fold lower Km for actin filaments than Myo5c-S1 (single-headed myos

192 than GOX1 and GOX2 is a 5- to 10-fold lower Km for the substrate.

193 istent with previous reports, we found lower Km(app)(O2) values for FIH than for PHD2 with all HIF-de

194 FIH has lower Km(app)(O2) values for the tested ARDs than HIF-alpha su

195 gaged SAAM binding by the MAT mutants (lower Km value in contrast to native MATs), the gained activit

196 he Pentacam HR exhibited significantly lower Km and CCT measurements (P < .001, for all); however, no

197 The lower Km constants for human SAMHD1 induce activation at lower

198 al conditions, mainly because of their lower Km value for the DNA substrate.

199 Besides, MdP2'GT displayed the lowest Km and the highest kcat/Km for phloretin and UDPG compar

200 s, and particularly G221E, displayed a major Km increase for S-2288.

201 ereas the affinity of CAT for H2O2 (measured Km approximately 43 mM) is extraordinarily low.

202 (Imax) of 92.55microA and Michaelis-Menten (Km) constant of 30.48microM.

203 n was the favorite substrate with 2.16 mg/mL Km and 35.6 h(-)(1) Kcat values.

204 for an energy-sensing attribute (i.e., 1 mM Km for ATP) of the 5-InsP7-generating inositol hexakisph

205 This reaction requires Na(+) (Km = 0.12 mm) or Li(+) (Km = 0.25 mm) for activity, indi

206 reaction, and kinetics for both the NAD(+) (Km = 34 +/- 12 mum) and RhoA (Km = 17 +/- 3 mum) substra

207 Enzymatic characterization of the NAs (Km, Ki) and the in vitro fitness of viruses carrying wil

208 increase of Vmax and a variable decrease of Km.

209 y for the substrates (i.e. by a reduction of Km).

210 IOLMaster 700 were compared for each type of Km value from Pentacam HR, while other parameters were c

211 on had no effect on basal kinase activity or Km and Vmax values; however, PKGIalpha containing the C4

212 was dependent on the concentrations of Pah1 (Km = 0.23 mum) and ATP (Km = 5.5 mum).

213 centrations of ATP (Km = 4.5 mum) and Pah1p (Km = 0.75 mum).

214 apparent Michaelis-Menten kinetic parameter (Km) is estimated to be about 0.13 mM which indicates the

215 Its Kinetic parameters Km and kcat are better than horseradish peroxidase which

216 easured apparent Michaelis-Menten parameters Km and Vmax.

217 tional role; and the biochemical parameters (Km, kcat, and kcat/Km) of the recombinant TcP5CDH were d

218 C, respectively and the kinetic parameters (Km, Vmax and kcat) were determined to be 0.33 (mgml(-1))

219 atively much lower affinity for perchlorate (Km = 1.1 mm) and no substrate inhibition.

220 catalyzes l-alanine racemization with a poor Km (58 mm) but a high kcat (22 s(-1)).

221 and a weaker interaction with the protease (Km).

222 e, especially for spermidine and putrescine (Km values of 33 mum and 3.9 mm, respectively).

223 s RNase HI activity by lowering the reaction Km.

224 contrast, a fraction of kanamycin-resistant (Km(r)) and nalidixic acid-resistant (Nal(r)) isolates sh

225 th the NAD(+) (Km = 34 +/- 12 mum) and RhoA (Km = 17 +/- 3 mum) substrates were characterized for thi

226 he different kinetic parameters, the Rubisco Km for CO2 presented higher energy of activation than th

227 small molecules-analogous to how an enzyme's Km or Vmax are medicinally targeted-holds promise as a s

228 heterologous expression system is saturable (Km approximately 14.7 muM), and selective for Fe(2+) ove

229 to a dramatic stimulation of E2 sensitivity (Km) and catalytic rate (kcat), which together resulted i

230 P1 and AtPyrP2 showed that they have similar Km values for the substrate ARPP, with AtcpFHy/PyrP1 hav

231 nd aminoacylation assays, and showed similar Km for L-proline.

232 bstrate non-cooperatively and with a smaller Km value.

233 ngle-enzyme encapsulation (SEE) show smaller Km than free enzymes while maintaining comparable cataly

234 ficiency by increasing its histone substrate Km, comparable with that of Caenorhabditis elegans PRMT5

235 The A31I mutation reduces the substrate Km value; this is a key property to allow the required t

236 ogenic acid was the most suitable substrate (Km=0.56+/-0.07 mM and Vmax=53.15+/-2.03 UPPO mL(-1) min(

237 alog (K(i) = 64 +/- 18 nM) demonstrates that Km reflects intrinsic substrate affinity.

238 Results showed that Km value of Th-MOF with TMB as a substrate is much lower

239 The Km and kcat values of purified enzyme were 0.0672 mM and

240 The Km and Ki revealed that the I221L variant NA had approxi

241 The Km and Vmax values for purified Xyl2 were 9.6mg/mL and 2

242 The Km and Vmax values of immobilized invertase were found t

243 The Km and Vmax values on beechwood xylan were determined to

244 The Km for 5'-deoxyadenosine was found to be 14.0 +/- 1.2 mu

245 The Km value of SlGLS for geranylgeranyl diphosphate was 18.

246 The Km values of Psp68 are 1.6129 and 1.14 nM for DNA helica

247 The Km values of Psp68 for ATPase are 0.5126 and 0.9142 mM i

248 at was best fit by 22.3 +/- 4.9 min(-1), the Km for ATP by 0.104 +/- 0.024 mm, and the Ki for ADP by

249 ased the Km of AdoMet but did not affect the Km of the protein substrate.

250 ytic activity without markedly affecting the Km value for the all-trans-8'-apocarotenol substrate.

251 Such measurements can afford the Km for each ligand as well as the stoichiometry of ion-s

252 ed increase in activity without altering the Km values for the substrates.

253 neither mutant was activated by ATP, and the Km and Hill coefficient of each mutant assayed in the ab

254 e the kcat of transport without changing the Km values.

255 , increased Vmax 2.6-fold, and decreased the Km 13-fold, whereas the R655C mutation decreased the EC5

256 creased the Vmax 2.1-fold, and decreased the Km 4.7-fold.

257 sine acetylation significantly decreased the Km for the actin-activated ATPase activity of MHC isofor

258 ncreased the turnover rate and decreased the Km of AdoMet but did not affect the Km of the protein su

259 tic analyses were conducted to determine the Km and Vmax parameters of these two hydrolysates using t

260 ating Gln-282 to alanine (Q282A) doubled the Km(app) for 2-deoxy-d-glucose uptake and eliminated cis-

261 t functions to suppress kcat and elevate the Km for CTP.

262 For guaiacol, the Km and Vmax values were calculated as 24.88mM and 3.23EU

263 For H2O2, the Km and Vmax values were calculated as 3.247mM and 0.799E

264 c moss (Physcomitrella patens) harboring the Km-altering mutation in the essential stromal Hsp70-2 an

265 sly reported to result in an increase in the Km for ATP and a decrease in the enzyme's kcat.

266 Ser-510 or Thr-513 in WT-GC-A increased the Km 23- to 70-fold but the same mutations in GC-A-8E only

267 same mutations in GC-A-8E only increased the Km 8-fold, consistent with one site affecting the phosph

268 mates in GC-A-8E progressively increased the Km Double Ala substitutions for Ser-497 and either Thr-5

269 -oxoglutarate-binding residues increased the Km values for these factors 30-80-fold and reduced the V

270 Here, we report that increasing the Km for ATP hydrolysis of Hsp70 translated into an increa

271 Immobilization of the enzyme lowered the Km to 1/3rd compared to the soluble enzyme.

272 lar cholesterol reduced the Vmax but not the Km of the LAT1 mediated uptake of a model substrate into

273 Based on the Michaelis-Menten plots, the Km with casein as substrate was 16.8muM and Vmax was 82.

274 be an activator because ISL could reduce the Km and Ea of beta-glucuronidase reacting with GL.

275 RcdA in an all-or-none manner to reduce the Km of CtrA proteolysis 10-fold.

276 Specifically, the Km value of morphine to OATP2B1 (57.58 +/- 8.90 muM) is

277 y in vitro with a Ki 10 times lower than the Km value and efficiently impaired GAG synthesis in a cel

278 A study of enzyme kinetics revealed that the Km and Vmax of the purified recombinant MzASMT9 protein

279 ibitory properties of Tets and show that the Km value of Tets 1 and 2 for O2 is 30 mum, indicating th

280 as comparable for di- and tri-ubiquitin, the Km value was lower for tri-ubiquitin.

281 taB9/Q3) was minimally affected, whereas the Km value of the reaction was increased 57-fold compared

282 tion was increased 57-fold compared with the Km value obtained with prothrombinase assembled with fVa

283 be hexameric, has a high affinity for TMAO (Km = 3.3 mM; Vmax = 21.7 nmol min(-1) mg(-1) ) and only

284 ystem attests appreciable kinetics, owing to Km value as low as 0.015 mM and better loading capacity

285 s have comparable affinities for tryptophan (Km approximately 2 mum), and yet only bacterial TrpRSs a

286 , although they showed comparable Km values (Km of 3.7 +/- 0.4 mm and kcat of 15.9 +/- 1.0 min(-1) to

287 nt EMB14 is shown to hydrolyze GTP in vitro (Km = 2.42 +/- 0.3 mum).

288 3 to make GC-A-8E resulted in the same Vmax, Km, and EC50 as the phosphorylated WT enzyme.

289 layed significant enzymatic efficiency (Vmax/Km) with different substrates.

290 re 5.1mM and 23mM/min, respectively, whereas Km and Vmax values of immobilized trypsin were 7.88mM an

291 and Ach transport were performed from which Km values of 0.29 and 0.79 mM were derived, respectively

292 roperties of invertase were preserved, while Km values were slightly increased from 26 to 37mM.

293 cholesterol leads to an increased Vmax while Km remains unchanged.

294 gher Km 2.08mg/ml than the free enzyme whose Km is 0.45+/-.05mg/ml.

295 by wild-type HABP2 was Na(+)-dependent, with Km decreasing from 3.0 to 0.6 mm upon titration from 0 t

296 incorporated per telomerase per minute, with Km(dGTP) approximately 17 muM, indicating super-telomera

297 oA + NADH + H(+) = butyryl-CoA + NAD(+) with Km = 1.4 mum ferredoxin or 2.0 mum flavodoxin.

298 are good substrates for DNA polymerase, with Km values averaging 13-fold higher than those of natural

299 ediated by these transporters saturated with Km AMT1;1 = 89 microM and Km AMT2;1 = 123 microM, respec

300 for this hydrolase appears to be starch with Km 1.56 mg/mL, Vmax 1666.67 U/mg and kcat 485 s(-1) and

301 te affinity (Km) values to the wildtype (WT) Km value but had a lower turnover number and transfructo