ライフサイエンスコーパス: enzyme reaction

1 nsfer effects and reduced efficiencies of an enzyme reaction.

2 trol conformational changes required for the enzyme reaction.

3 luorescent product, resorufin, via a coupled-enzyme reaction.

4 lso defines key residues responsible for the enzyme reaction.

5 ve site that are thought to be important for enzyme reaction.

6 metabolized to malate followed by the malic enzyme reaction.

7 ty change cooperatively occurs in continuous enzyme reaction.

8 ding sites of the enzyme changes (lowers) in enzyme reaction.

9 tivity effects that has been reported for an enzyme reaction.

10 o generate the pyruvate product in the malic enzyme reaction.

11 the molecule could be asymmetric during the enzyme reaction.

12 the bioluminescence produced by the coupled enzyme reaction.

13 dynamics and the catalytic redox step of the enzyme reaction.

14 g its entire length during all stages of the enzyme reaction.

15 alactopyranoside, as the model system of the enzyme reaction.

16 p to determine the key kinetic parameters of enzyme reaction.

17 rometry confirms the expected product of the enzyme reaction.

18 tial rates from nonlinear progress curves of enzyme reactions.

19 the transient-state time courses of the two enzyme reactions.

20 g how light energy can be harnessed to power enzyme reactions.

21 e prehydride charge-transfer complex in both enzyme reactions.

22 n of the corresponding genes and by in vitro enzyme reactions.

23 te how this impacts on experimental KIEs for enzyme reactions.

24 on studies of interacting systems as well as enzyme reactions.

25 es covering ~1800 (70%) of sequence assigned enzyme reactions.

26 oach for studying the mechanistic details of enzyme reactions.

27 rganic enzyme cofactors are involved in many enzyme reactions.

28 MM molecular dynamics approach in simulating enzyme reactions.

29 nterpreting 18O kinetic isotope effects upon enzyme reactions.

30 in comparisons of changes in patterns during enzyme reactions.

31 s a nucleophilic catalyst in both the normal enzyme reaction and in the formation of a covalent compl

32 ling and the capacity of CD38 to catalyze an enzyme reaction and produce cADPR, ADPR, and/or nicotina

33 titative relationship between the rate of an enzyme reaction and the concentration of its substrate.(

34 iology, occurring, for example, in proteins, enzyme reactions and across proton channels and pumps.

35 incorporates all of the forward and reverse enzyme reactions and regulatory circuits of the branched

36 In order to understand the evolution of enzyme reactions and to gain an overview of biological c

37 reference database, consists of metabolites, enzymes, reactions and metabolic pathways.

38 Cyc as a reference, consists of metabolites, enzymes, reactions and metabolic pathways.

39 ors and cofactors, on the initial rate of an enzyme reaction, and it could be applied to a comprehens

40 amic links for microbial metabolic pathways, enzyme reactions, and their substrates and products.

41 In this method, enzyme reactions are carried out in solution using subst

42 Our earlier studies show that the two enzyme reactions are linked by the coenzyme product, NAD

43 e of protein conformational changes in these enzyme reactions are summarized.

44 In vitro enzyme reactions are traditionally conducted under condi

45 has increasingly been found to contribute to enzyme reactions at room temperature.

46 from traditional approaches used to analyze enzyme reactions at steady state, but they are also appl

47 ter, prespotted reaction volumes to activate enzyme reactions at targeted positions on a microarray.

48 for quantitative similarity searches between enzyme reactions at three levels: bond change, reaction

49 The separated products of the enzyme reaction can be quantitated by radiometric scanni

50 equence of this flexibility is that the same enzyme reaction can occur via multiple reaction pathways

51 t with simpler molecular mechanical methods, enzyme reactions can be modeled.

52 The kinetic parameters of the enzyme reaction catalyzed by the ectoenzyme pantetheinas

53 pathways, elements with multiple functions, enzyme reaction chains, and equilibrium enzymes.

54 y 7-fold in the dehydration direction of the enzyme reaction compared to wild-type (WT).

55 After stopping the enzyme reaction, compounds were extracted by perchloric

56 iciency (E(d)), substrate concentration, and enzyme reaction conditions were evaluated.

57 4alpha-demethylase activity in reconstituted enzyme reactions confirmed UDO and UDD as potent and sel

58 zzled and Chordin in the gastrula embryo and enzyme reaction constants were all in the 10(-8) M range

59 that lock topoisomerase II at a point in the enzyme reaction cycle where the enzyme forms a closed cl

60 ms and 2) the chemical rate constants of the enzyme reaction cycle.

61 ty relationships, to study chemical steps in enzyme reaction cycles.

62 ion of this nonlinear regression approach to enzyme reactions demonstrated satisfactory results.

63 In this case, the enzyme reaction displays a later transition state compar

64 -color fluorescence assay to monitor coupled enzyme reactions during Okazaki fragment maturation is d

65 this system, increasing overall encapsulated enzyme reaction efficiency, factor(s) required for the p

66 The rates of enzyme reactions fall within a relatively narrow range.

67 e biosensor was developed exploiting coupled enzyme reactions for quantifying L-lactate in oral fluid

68 pete with plasma levels of Br- and steer the enzyme reaction from a 2e- oxidation to a 1e- oxidation

69 e acting as a genuine cofactor in the single-enzyme reaction, functions in the luciferase-coupled rea

70 ese studies underscore a concerted series of enzyme reactions governing histone modifications that pr

71 ments that lack this nutrient; thus, unusual enzyme reactions have also evolved to cleave the C-P bon

72 operties of rat FDH suggest that the overall enzyme reaction, i.e. NADP(+)-dependent conversion of 10

73 Studies of the molecular basis of the enzyme reaction in Triton micelles revealed that (a) a n

74 By initiating enzyme reactions in crystals, we have trapped hExo1 reac

75 al, we screen approximately 10(8) individual enzyme reactions in only 10 h, using < 150 microL of tot

76 standpoints, requires measuring the rates of enzyme reactions in their native environment and interpr

77 Negative cooperativity in enzyme reactions, in which the first event makes subsequ

78 ansitions over the entire time-course of the enzyme reaction initiated by fast mixing of the enzyme a

79 Formation of the acetyl-S-enzyme reaction intermediate by Y130L, F204L, and Y376L

80 impaired formation of the covalent acetyl-S-enzyme reaction intermediate exhibited diminished (D159A

81 Formation of the [(13)C]acetyl-S-enzyme reaction intermediate of HMG-CoA synthase in D(2)

82 ethyl protons of HMG-CoA synthase's acetyl-S-enzyme reaction intermediate suggests a hydrophobic acti

83 , which indicate that E95A forms an acetyl-S-enzyme reaction intermediate with the same distinctive s

84 rmation of the covalent [1,2 -(13)C]acetyl-S-enzyme reaction intermediate.

85 y to form significant levels of the acetyl-S-enzyme reaction intermediate.

86 designed geometric factors of the substrate-enzyme reaction intermediates, such that catalysis is li

87 have proven to be very useful in identifying enzyme reaction intermediates.

88 In contrast to all other enzyme reactions investigated previously, including DHFR

89 Single-enzyme reactions involving abortive complexes, and rando

90 known mechanisms of the alkaline phosphatase enzyme reaction is tested to predict the measurements fo

91 y to monitor the progress of single-molecule enzyme reactions is often limited by the need to use flu

92 P69 dimerization is because of a crisscross enzyme reaction joining two substrate molecules bound to

93 We propose the slowing of enzyme reaction kinetics in the smaller droplets was the

94 nderscore the significant differences in the enzyme reaction kinetics with different substrate partic

95 uchel et al. for the analysis of consecutive enzyme reactions leads to a simple description of the ca

96 hy (PET) has been used clinically to measure enzyme reactions, ligand-receptor interactions, cellular

97 nhibition by binding to the substrate of the enzyme reaction, making them examples of an unusual clas

98 rized enzymes; however, its Mg(2+)-dependent enzyme reaction mechanism may be analogous to one propos

99 r formation has no significant effect on the enzyme reaction mechanism.

100 alf-of-the-sites or flip-flop models for the enzyme reaction mechanism.

101 ng in this, the first committed, step of the enzyme reaction mechanism.

102 CiE database contains 223 distinct step-wise enzyme reaction mechanisms and holds representatives fro

103 out of proteins is important, both for many enzyme reaction mechanisms and proton pumping across mem

104 ces using the MACiE database of 202 distinct enzyme reaction mechanisms as a knowledge base.

105 elease of a web-based search tool to explore enzyme reaction mechanisms in MACiE.

106 Classification in Enzymes) is a database of enzyme reaction mechanisms, and can be accessed from htt

107 Classification in Enzymes) is a database of enzyme reaction mechanisms, and is publicly available as

108 language extension that describes a suite of enzyme reaction mechanisms.

109 enzymes to the prediction and validation of enzyme reaction mechanisms.

110 work of one organism, including metabolites, enzymes, reactions, metabolic pathways, predicted operon

111 work of one organism, including metabolites, enzymes, reactions, metabolic pathways, predicted operon

112 the fluorescent labeling is performed on the enzyme reaction mixture.

113 ial electrophoretic assays from 16 different enzyme reaction mixtures at 20 s intervals in parallel.

114 Enzyme reaction mixtures cyclize (3RS)-[4,4,13,13,13-2H5

115 by assaying the amount of product formed in enzyme reaction mixtures that contained test compounds.

116 complexes are shown to serve as hydrogenase enzyme reaction models, H(2) uptake and H(2) production,

117 model to simulate the acetyl-CoA synthetase enzyme reaction network using the data derived from time

118 encoding various specific microscopic intra-enzyme reaction networks (micro-models), and (ii) lead t

119 l chemical mechanism (catalytic steps) of an enzyme reaction, not only the overall reaction.

120 demonstrate the direction-dependent surface enzyme reaction of ExoIII with double-stranded DNA as we

121 We have demonstrated a multistep enzyme reaction on a chip to determine the key kinetic p

122 SEED) has been developed to measure multiple enzyme reactions on a monolith electrode due to immunosp

123 -HSD/isomerase) catalyzes the two sequential enzyme reactions on a single protein that converts dehyd

124 pearance of the final product of the coupled enzyme reaction or a decrease in the susceptibility of t

125 ty is achieved without the need for indirect enzyme reactions or specialized instrumentation.

126 iewpoint may be presumed to be applicable to enzyme reactions other than those of the alpha-amino aci

127 tate NMR has led to the postulation of a new enzyme reaction pathway and raised once again the questi

128 , provided the following key features of the enzyme reaction pathway.

129 nted programming concepts to define glycans, enzymes, reactions, pathways and compartments for modeli

130 repair on thermal stability was confirmed by enzyme reactions performed over 0-45 degreesC.

131 on zone increased linearly with time over an enzyme reaction period of 30 min and at a rate that was

132 The coupled-enzyme reaction permits rapid signal amplification from

133 y for their applications in food processing, enzyme reactions, pharmaceuticals and cosmetics.

134 Both products of the CD38 enzyme reaction play important roles in signal transduct

135 To determine the rate-limiting step in the enzyme reaction, pre-steady-state kinetic analyses were

136 The enzyme reaction precursors are formed easily from two re

137 The transient kinetic behavior of enzyme reactions prior to the establishment of steady st

138 The enzyme reaction product of this new substrate emits at a

139 The electrochemical oxidation of the enzyme reaction product, 1-naphtol, measured by differen

140 e the rate of molecular self-assembly of the enzyme reaction product.

141 The cell-free enzyme reaction products obtained were characterized by

142 First, the published enzyme reaction products of cyanuric acid hydrolase are

143 The radiolabeled enzyme reaction products were predominantly (95%) single

144 e studied by video microscopy of the stained enzyme reaction products.

145 CP mutants highlight different states of the enzyme reaction, providing an underlying structural basi

146 Enzyme reaction rate constant (k) was placed in the 0-4

147 he scheme makes it possible to calculate the enzyme reaction rate explicitly by combining chemical ki

148 probability is very small, the effect on the enzyme reaction rate is considerably larger, for example

149 that Trp-11 is involved in regulation of the enzyme reaction rate, contradictory to a previous sugges

150 MFA) has been widely used to measure in vivo enzyme reaction rates (i.e., metabolic flux) in microorg

151 n enzymes are very rare, and the majority of enzyme reactions rely upon nucleophilic and general acid

152 gy coupling between ATP hydrolysis and other enzyme reactions requires the phosphorylation of substra

153 At the completion of the enzyme reaction, residual substrate is detected with an

154 The product of enzyme reaction, resorufin, exhibits fluorescence emissi

155 The product of enzyme reaction, resorufin, exhibits fluorescence emissi

156 AB with the involvement of the 27 most-known enzyme reaction rules of 22 enzymes, as an extension of

157 ble biochemical reaction from a given set of enzyme reaction rules that allows the de novo synthesis

158 le biochemical pathways using a given set of enzyme reaction rules.

159 d amino acid residue functions that occur in enzyme reaction sequences using the MACiE database of 20

160 lfatide from the total sulfatide used in the enzyme reaction (sulfatide-Azure A present in a parallel

161 Our results suggest that pairs of similar enzyme reactions tend to proceed by different mechanisms

162 is approximately three times greater for the enzyme reaction than the uncatalyzed reaction, and the o

163 Here we show an enzyme reaction that operates effectively on a PNA/DNA h

164 The enzyme reactions that create these molecules are an inte

165 ytical methods are discussed and examples of enzyme reactions that have been successful on these surf

166 In the early days, radical enzyme reactions that use S-adenosylmethionine (SAM) coo

167 For this enzyme reaction, the large magnitude of the KIE arises m

168 contribute, but, in contrast to unimolecular enzyme reactions, their role appears to be secondary to

169 tific microwave reactors can accelerate this enzyme reaction, they may not be easily accessible.

170 As a model enzyme reaction, this work examined the transfer of a me

171 Plots of ECL increase vs enzyme reaction time monitor relative rates of DNA damag

172 R, the initial slope of ECL increase versus enzyme reaction time normalized for amounts of enzyme an

173 The rate of increase in ECL with enzyme reaction time reflects relative DNA damage rates.

174 wave voltammetric (SWV) peaks increased with enzyme reaction time, and relative DNA damage rates at p

175 ions by using the output of an autocatalytic enzyme reaction to drive both the polymerization and sub

176 the initial velocities or the time course of enzyme reactions to an arbitrary molecular mechanism rep

177 bioreactors, allowing a range of significant enzyme reactions to be processed simultaneously.

178 ssel has been used in this work to carry out enzyme reactions under varying substrate concentrations.

179 F metabolites was measured subsequent to the enzyme reaction using catalytic voltammetric oxidation w

180 method requires nothing more than running an enzyme reaction using forcing concentrations of reactant

181 Enzyme reactions using a combination of human ER mannosi

182 incorporates direct hybridization and single enzyme reaction via the formation of single probe-RNA-pr

183 proach for a field-effect based detection of enzyme reactions via detecting changes in the pH value d

184 A more complex two-step enzyme reaction was also designed.

185 This enzyme reaction was measured continuously by positioning

186 ing, a state-of-the-art approach to simulate enzyme reactions, we have provided further evidence agai

187 AS, and Q147K ADCS mutants were prepared and enzyme reactions were analyzed by high-performance liqui

188 Products from enzyme reactions were identified by gas chromatography-m

189 A total of 335 enzyme reactions were retrieved from MACiE and were mapp

190 al tunneling and coupled motion in the malic enzyme reaction when NAD+ and malate are used as substra

191 ticularly useful in producing substrates for enzyme reactions when the dihydropterin substrate cannot

192 rapi oxide (de = 20-25%) are produced in the enzyme reaction, whereas two diastereomers of these comp

193 elease is the overall rate-limiting step for enzyme reaction with NGD+.

194 change of Escherichia coli ATCase during the enzyme reaction with physiological substrates.

195 pulation methods, we investigate restriction enzyme reactions with double-stranded (ds)DNA oligomers

196 ticle and offers a means of detecting single-enzyme reactions without fluorescence detection.