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 urned over HOSCN (kcat = 357 +/- 16 min(-1); Km = 31.9 +/- 10.3 muM) but were inactive against the re

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

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

8 0.3 m Na(+) In the presence of 5 mm Ca(2+), Km was further reduced to 0.05 mm, but without an apprec

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

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

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

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

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

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

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

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

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

18 The enzyme converts SA (with a Km of 58.29 microM) to both 2,3-dihydroxybenzoic acid (2

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

20 700 converts 8-oxo-dGDP to 8-oxo-dGMP with a Km of approximately 9.5 muM and Vmax of approximately 0.

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

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

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

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

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

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

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

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

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

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

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

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

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

34 sms determining allotypes designated G1m and Km.

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

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

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

38 , 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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

63 ing (Ks(A) = 11 mm), interfacial PA binding (Km(B) = 4.2 mol %), and catalytic efficiency (Vmax = 557

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

82 107 revolutions/s and a Michaelis constant (Km) of 154 muM at 26 degrees C.

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

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

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

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

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

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

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

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

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

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

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

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

95 0H2 to thioredoxin via protein-bound flavin; Km values for thioredoxin and F420H2 were 6.3 and 28.6 m

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

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

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

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

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

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

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

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

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

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

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

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

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

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

110 The mutant enzyme shows a 4-fold increase in Km (using cis-3-bromoacrylate), but not to the degree ob

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

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

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

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

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

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

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

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

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

120 sic specificity and the enzyme activity kcat/Km.

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

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

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

124 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

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

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

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

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

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

130 higher catalytic efficiency measured as kcat/Km.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

157 selectivity (as defined by the ratio of kcat/Km for KDO8P vs KDN9P) varied significantly.

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

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

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

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

162 No pH effects were seen with P3N on kcat/Km, kcat/Koxygen, and kcat; in contrast, with EN, the kc

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 en, and kcat; in contrast, with EN, the kcat/Km and kcat decreased with increasing pH defining two pl

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

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

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

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

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

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

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

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

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

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

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

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

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

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

184 2months), wide linear range (0.5-24mM), low Km (8.4mM), high Imax (77.2muAcm(-2)), low detection lim

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

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

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

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

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

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

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

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

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

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

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

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

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

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

247 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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

265 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

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

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

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

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

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

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

272 amino acids by alanine has no effect on the Km for the two substrates.

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