ライフサイエンスコーパス: substrate inhibition

1 to the stability of a model P1 duplex using "substrate inhibition".

2 rovides a structural explanation for reduced substrate inhibition.

3 tivity and reaction optimization to overcome substrate inhibition.

4 elocity and dramatic concentration-dependent substrate inhibition.

5 N epsilon-Cbz group demonstrated pronounced substrate inhibition.

6 ffinity for perchlorate (Km = 1.1 mm) and no substrate inhibition.

7 n further increase sAC activity by relieving substrate inhibition.

8 ow concentrations of Fru-6-P, MgATP displays substrate inhibition.

9 NADPH and BSO exhibiting double competitive substrate inhibition.

10 of ascorbic acid or ACC leads to significant substrate inhibition.

11 is complex and exhibits sigmoidal curves and substrate inhibition.

12 ion and enhances the degree of ascorbic acid substrate inhibition.

13 tibodies eliminated the phenomenon of excess substrate inhibition.

14 teroid, whereas L211F/D214E displayed simple substrate inhibition.

15 trate binding, substrate phosphorylation and substrate inhibition.

16 ure stability and catalytic activity without substrate inhibition.

17 GMP was found to have partial substrate inhibition.

18 ome is a hysteretic enzyme and is subject to substrate inhibition.

19 ; higher concentrations resulted in dramatic substrate inhibition.

20 cleotide base is an important determinant of substrate inhibition.

21 e link between pore-size heterogeneities and substrate inhibition.

22 ered lactate accumulation, e.g., competitive substrate inhibition.

23 eas short and medium chains (C8-C12) exhibit substrate inhibition.

24 lycosides without intraring constraints show substrate inhibition.

25 s, and a number of these mutations abrogated substrate inhibition.

26 he allosteric site and thereby eliminate the substrate inhibition.

27 lypeptide accumulation, and possibly reduced substrate inhibition.

28 ther Ser or Ala give an enzyme that shows no substrate inhibition.

29 ly metal ion substrate not subject to severe substrate inhibition.

30 inhibition in addition to and distinct from substrate inhibition.

31 icant changes in the pH-dependent profile of substrate inhibition.

32 ivity and functions in a novel mechanism for substrate inhibition.

33 modest decreases in SrtA activity and led to substrate inhibition.

34 urately by a ping-pong mechanism with double substrate inhibition.

35 kinase domain that are active but devoid of substrate inhibition.

36 , which leads to the observation of apparent substrate inhibition.

37 ter K(m), a much smaller k(cat), and altered substrate inhibition.

38 site, which may explain previously observed substrate inhibition.

39 rved at high concentrations of rH3, implying substrate inhibition.

40 an did Calpha, but Cbeta1 was insensitive to substrate inhibition, a phenomenon that was observed wit

41 +/- 6 nm; kcat = 0.020 +/- 0.007 s(-1)) and substrate inhibition above 0.5 mum (Ki = 2.5 +/- 1.3 mum

42 5.7 nM and kcat = 0.032 +/- 0.001 s(-1)) and substrate inhibition above 2 muM.

43 tions of cyclohexanol produce noncompetitive substrate inhibition against varied concentrations of NA

44 AChE, a K(S) of 0.5+/- 0.2 mM obtained from substrate inhibition agreed with a K(S) of 0.4+/- 0.2 mM

45 ly reduced affinity for L-ornithine, loss of substrate inhibition, alkaline shift of pH optimum, and

46 mutation was identified that eliminates the substrate inhibition altogether.

47 er the Cu(I) or Cu(II) forms of TbetaM, with substrate inhibition ameliorated at very high ascorbate

48 Kinetic studies, including product and substrate inhibition analyses, initial velocity dependen

49 This also follows from data on substrate inhibition and activation, effects of NAD+ on

50 e R93A mutant also showed a complete loss of substrate inhibition and altered nucleotide binding affi

51 ivity is inhibited by ATP via noncompetitive substrate inhibition and by GTP via mixed-type inhibitio

52 f resorufin to less fluorescent compound(s), substrate inhibition and enzyme inactivation at higher (

53 In particular, substrate inhibition and enzyme inactivation at higher h

54 enhances SAT activity and releases SAT from substrate inhibition and feedback inhibition by cysteine

55 By contrast, SULT1E1 showed distinct substrate inhibition and formed both M1 and M2.

56 the conventional random bi-bi mechanism with substrate inhibition and is able to describe the kinetic

57 metabolism of arachidonic acid is subject to substrate inhibition and is also inhibited by the presen

58 A significant NADPH substrate inhibition and large K(M) rationalized the slo

59 This unreported paradigm explains substrate inhibition and reactivation by competitive inh

60 nonallosteric kinetic patterns demonstrating substrate inhibition and sigmoid velocity curves.

61 stitutions, and a new kinetic model based on substrate inhibition and sigmoidicity was generated.

62 rate the generality of the L-canavanine slow substrate inhibition and to distinguish the kinetic beha

63 the enzyme 10-fold less sensitive to excess substrate inhibition and two times less susceptible to t

64 Fe(II) and ACC exhibit substrate inhibition, and a second metal binding site is

65 ivation, autoactivation, partial inhibition, substrate inhibition, and biphasic saturation curves.

66 ng onto the active E6AP trimer suggests that substrate inhibition arises from steric hindrance betwee

67 A and displaying a similar profile of excess substrate inhibition as the double mutant.

68 re optimum of 50 degrees C, and demonstrates substrate inhibition, as well as showing a high basal le

69 important by taurocholate transport studies, substrate inhibition assays, confocal microscopy, and el

70 dylcholine (PC) and 0.2 mM Ca(2+), there was substrate inhibition at >100 microM AA.

71 ate was a partial inhibitor but also induced substrate inhibition at high ATP levels.

72 lts of pH-dependence experiments showed that substrate inhibition at high C(2)D(2) concentrations is

73 low substrate concentrations but results in substrate inhibition at high concentrations because of s

74 6A product analog (K(i) = 7 +/- 0.7 muM) and substrate inhibition at high concentrations require two

75 n assay, but a hydroxylation assay indicated substrate inhibition at high ornithine concentration.

76 , k(cat) = 450 s(-1)), the enzyme exhibiting substrate inhibition at high substrate concentrations.

77 +/- 32 nm; n = 1.8 +/- 0.1) and cooperative substrate inhibition at micromolar concentrations ([S](1

78 There was substantial substrate inhibition at millimolar levels of mevalonate.

79 A significant decrease in the K(i) for substrate inhibition at pH values corresponding to the v

80 ins the complex activity of AK, particularly substrate inhibition, based on the experimentally observ

81 oxygen, increasing IP-CoA would show strong substrate inhibition because it binds tightly to the red

82 All HadA(Phe441) variants lack substrate inhibition behavior, confirming that quadruple

83 state kinetic data showed that hIDO exhibits substrate inhibition behavior, implying the existence of

84 ular explanation for the previously baffling substrate-inhibition behavior of the enzyme.

85 ons eliminate the dual pH optima by reducing substrate inhibition between pH 5 and 7 and a triple mut

86 e variable reactivity in the host, including substrate inhibition, binding affinity, and accessibilit

87 CoA synthase that is insensitive to feedback substrate inhibition by acetoacetyl-CoA.

88 In addition, uncompetitive substrate inhibition by alpha-Kg and double inhibition b

89 Here we study the phenomenon of substrate inhibition by AMP and its correlation with dom

90 kinase activity displayed the characteristic substrate inhibition by APS (K(I) of 47.9 microM at satu

91 cat)/K(m) and a 15-fold increase in K(i) for substrate inhibition by APS compared with the oxidized e

92 ic efficiency and decreased effectiveness of substrate inhibition by APS compared with the oxidized f

93 ulting protein was completely insensitive to substrate inhibition by APS.

94 l velocity pattern that displays competitive substrate inhibition by ASA and dead-end inhibition patt

95 AcdA is the most sensitive to substrate inhibition by CF and 1,1,2-TCA and inhibition

96 ed concentrations of GGPP and induced potent substrate inhibition by dansyl-GCIIL when dansyl-GCIIL w

97 x flow restrictor also prevents the onset of substrate inhibition by diverting metabolic flux away fr

98 nity for ADP, which corresponds to a loss of substrate inhibition by formation of an E.ADP.APS dead e

99 e nucleotide binding site, one could observe substrate inhibition by fructose 6-phosphate and apparen

100 but the enzyme is especially susceptible to substrate inhibition by GDP.

101 described above but with the involvement of substrate inhibition by Gly-OMe.

102 Certain substitutions of these caused substrate inhibition by isoprenylcysteine, suggesting th

103 for measurement of NO. production, apparent substrate inhibition by L-arginine was almost completely

104 evealed that the values for (1.2 mM) and for substrate inhibition by L-Hcys ( = 2.0 mM) are lower tha

105 Data are consistent with uncompetitive substrate inhibition by naphthol as a result of formatio

106 Substrate inhibition by PRPP was observed.

107 not significantly faster than kcat, whereas substrate inhibition by serine suggests that breakdown o

108 avorable equilibrium but rather results from substrate inhibition by the most stable chair conformati

109 Significant substrate inhibition by this compound suggested that fur

110 Substrate inhibition by UDP-N-acetylmuramyl-L-alanine, t

111 hich inhibit the activity of Cdk2 on all its substrates, inhibition by pep8 has distinct substrate sp

112 Substrate inhibition can also be exhibited by diazocompo

113 Since the apparent substrate inhibition caused by MgATP binding is not seen

114 e affinity (Km = 6 mum) and a characteristic substrate inhibition compared with the highly similar re

115 (S) of 1.9+/-0.7 mM obtained by fitting this substrate inhibition curve agreed with a K(S) of 1.3+/-1

116 on constant of TK(low) was comparable to the substrate-inhibition dissociation constant, K(i)(HPA), d

117 amatically lowers the concentration at which substrate inhibition dominates the kinetics of fructose-

118 estigated by determining their effect on (i) substrate inhibition due to the binding of excess substr

119 Additionally, we find evidence of substrate inhibition during nitrite turnover and negativ

120 ating that Mg(2+) and GGPP exert synergistic substrate inhibition effects on CPS activity.

121 reaction kinetic fit with a non-competitive substrate-inhibition equation.

122 e were in reasonable agreement with observed substrate inhibition for acetylthiocholine and M7A and w

123 l stability that correlate with the observed substrate inhibition for each variant, signifying a pote

124 udes oxalate binding to a site that mediates substrate inhibition for YfdW.

125 st poisoning experiments provide evidence of substrate inhibition, further consistent with these conc

126 Elimination of substrate inhibition had no effect on the apparent V(max

127 Previous proposals to explain this substrate inhibition have included both kinetic and allo

128 The WNV protease showed substrate inhibition in assays utilizing fluorophore-lin

129 gs provide effective approaches for removing substrate inhibition in engineering pathways for efficie

130 Substrate inhibition in the direction of aldehyde reduct

131 obacterium tuberculosis displays substantial substrate inhibition in the direction of NADH oxidation

132 ffusion-controlled limit, and the absence of substrate inhibition in the poly(P)-dependent reaction s

133 substrate concentration dependent maxima and substrate inhibition in the steady-state reaction which

134 is study uncovers the molecular mechanism of substrate inhibition in tobacco glucosyltransferase NbUG

135 Thioredoxin exhibits substrate inhibition, increasing the K(M) for 3-MP ~15-f

136 2-methylthio-ADP also showed no substrate inhibition, indicating the nucleotide base is

137 educes substrate inhibition, suggesting that substrate inhibition is an evolutionary well conserved f

138 Previous modeling studies suggested that substrate inhibition is due to mutually exclusive produc

139 s an FRC variant for which oxalate-dependent substrate inhibition is modified to resemble that seen f

140 -3,17-dione (ADD) and 4-BNC displayed strong substrate inhibition (Ki S approximately 100 muM).

141 in vitro and that oxidation of l-Trp follows substrate inhibition kinetics (k(cat) = 0.89 +/- 0.04 s(

142 We also report substantial substrate inhibition kinetics for the SAD-catalyzed redu

143 Analysis of ATP substrate inhibition kinetics on ATP hydrolysis in hexam

144 These include an extended C-terminal motif, substrate inhibition kinetics, dependence of activity le

145 Specifically, observed "substrate inhibition" may result from substrate A in one

146 to take place, which is consistent with the substrate inhibition model for I(-) activation.

147 The substrate inhibition model suggested that peptide substr

148 Using a substrate inhibition model, the range of values of the M

149 The severe metal ion substrate inhibition observed during in vitro studies of

150 tion of the previously known but unexplained substrate inhibition observed for CYP2E1.

151 s nonproductively, thereby rationalizing the substrate inhibition observed with this particular stero

152 Substrate inhibition occurs in the order Cu(2+) > Zn(2+)

153 lts highlight the physiological relevance of substrate inhibition of a kinase, and reveal a novel int

154 ar adenosine is significantly potentiated by substrate inhibition of adenosine kinase.

155 etic experiments, we found that the apparent substrate inhibition of AK, formerly attributed to AMP,

156 Appreciating the existence of substrate inhibition of CD39 will help the interpretatio

157 n of UbcH7 approximately ubiquitin-dependent substrate inhibition of chain formation at micromolar co

158 epwise addition; this behavior resembles the substrate inhibition of enzymes and is discussed in term

159 Substrate inhibition of enzymes can be a major obstacle

160 indicating that residues 528 and 575 affect substrate inhibition of ERAP1 trimming.

161 We were also able to demonstrate evidence of substrate inhibition of in vivo radiotracer uptake in th

162 concentrations of exogenous pyruvate induced substrate inhibition of LDH activity in both enzymatic a

163 This substrate inhibition of LdUPRT provides a protective mec

164 Here, we show substrate inhibition of lycopene cyclase as the main lim

165 y that beta-carotene strongly attenuates the substrate inhibition of NbUGT72AY1, despite being a comp

166 Binding of this clamp abolishes substrate inhibition of the ATPase but leaves ATP bindin

167 Substrate inhibition of the process occurs through the f

168 There was substrate inhibition of the sulfation reaction at elevat

169 Substrate inhibition of the thiol-disulfide exchange rea

170 Substrate inhibition of UCH-L3 but not IsoT was noted fo

171 previously characterized PS/gamma-secretase substrates, inhibition of gamma-secretase activity resul

172 th ABCC1-specific export of glutathionylated substrates, inhibition of glutathione metabolism increas

173 3HB6H does not exhibit substrate inhibition on the flavin oxidation step, a com

174 Substrate inhibition, once dismissed, is now observed in

175 dditionally, LiAcs1 displayed a distinct CoA substrate inhibition pattern, partially alleviated by ac

176 Kinetic analyses of substrate inhibition profiles revealed that the enzyme f

177 Moreover, a substrate inhibition reaction step was required to accur

178 ically trapped intermediate during a suicide substrate inhibition reaction.

179 ated under our conditions to account for the substrate inhibition seen.

180 ation of multiple conserved residues reduces substrate inhibition, suggesting that substrate inhibiti

181 distinctive feature of TbetaM is very strong substrate inhibition that is dependent on the level of t

182 g site is not required to account for excess substrate inhibition, the kinetic behavior of trimethyla

183 yme to increase K(m) value and eliminate its substrate inhibition to construct "b2LOxS".

184 nal groups that are unprotonated for optimal substrate inhibition to occur.

185 l-Trp incubations results in modulation from substrate inhibition to sigmoidal kinetics (k(cat) = 1.7

186 n substrate binding was supported by reduced substrate inhibition upon introducing W773A, W689A, and

187 cal initial-rate methods including alternate substrate inhibition using ADPbetaS.

188 RNA-induced silencing can be blocked through substrate inhibition using single-stranded, stabilized o

189 Substrate inhibition was explained by blockade of produc

190 t unlike the H287C variant, pH dependence of substrate inhibition was largely eliminated.

191 The substrate inhibition was not competitive with MgATP and

192 Such substrate inhibition was not observed with the E. faecal

193 (m) of 45 microM S-adenosyl-l-methionine and substrate inhibition was observed above 200 microM.

194 In contrast, in the presence of UTP, substrate inhibition was observed at concentrations of d

195 n kinetics with respect to l-ornithine while substrate inhibition was observed at high concentrations

196 igmoidal under fixed PhP concentrations, but substrate inhibition was observed at high PhP concentrat

197 Substrate inhibition was observed at subsaturating conce

198 P = 45 mum +/- 5.6 mum, and kcat = 2.0 s(-1) Substrate inhibition was observed for AtRBSK (KiATP = 2.

199 Substrate inhibition was observed for most substrates.

200 Furthermore, strong substrate inhibition was observed for the AKR1C2 catalyz

201 microM) over other natural nucleosides, and substrate inhibition was observed when Ado concentration

202 ent from equilibrium binding studies, but no substrate inhibition was seen with 12-HDDA.

203 To understand substrate inhibition, we exploited the PatchDock algorit

204 influence of pore matrix heterogeneities on substrate inhibition, we use a numerical approach to sol

205 an Ordered Bi Bi mechanism with competitive substrate inhibition, where (i) the initially formed PDK

206 Steady-state kinetic studies indicated substrate inhibition which was best described by a model

207 m E. coli K-12 had significant levels of NAD substrate inhibition, which could be alleviated by the a

208 he first abasic site was subject to apparent substrate inhibition, which did not occur if the second

209 12-Oxododecanoic acid (12-ODDA) exhibited substrate inhibition, which is consistent with a preferr

210 The noncompetitive substrate inhibition, which was independent of UTP conce

211 re different: peak 1 activity was subject to substrate inhibition, while peak 2 activity was not.

212 t high concentrations of D-arginine yielding substrate inhibition, while the overall turnover is part

213 nstrate that soluble, recombinant CD39 shows substrate inhibition with ADP or ATP as the substrate.

214 The previously reported substrate inhibition with double-stranded substrates als

215 ies with pterins and folates (pH dependence, substrate inhibition with H2pteridines).

216 Furin exhibited striking substrate inhibition with hexapeptide but not tetrapepti

217 de, and exhibited positive cooperativity and substrate inhibition with O-acetyl-L-serine.

218 igh concentrations, ATP displays competitive substrate inhibition with respect to glucose, which is c

219 at high substrate concentrations may reflect substrate inhibition (with K(i) of approximately 4 mM).

220 ant, Y27R, characterized by complete loss of substrate inhibition without reduction of enzymatic acti