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 is complex and exhibits sigmoidal curves and substrate inhibition.

6 N epsilon-Cbz group demonstrated pronounced substrate inhibition.

7 n further increase sAC activity by relieving substrate inhibition.

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

9 trate binding, substrate phosphorylation and substrate inhibition.

10 NADPH and BSO exhibiting double competitive substrate inhibition.

11 of ascorbic acid or ACC leads to significant 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 ure stability and catalytic activity without substrate inhibition.

16 GMP was found to have partial substrate inhibition.

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

18 ; higher concentrations resulted in dramatic substrate inhibition.

19 lypeptide accumulation, and possibly reduced substrate inhibition.

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

21 lycosides without intraring constraints show substrate inhibition.

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

23 he allosteric site and thereby eliminate the substrate inhibition.

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

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

26 inhibition in addition to and distinct from substrate inhibition.

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

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

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

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

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

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

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

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

35 site, which may explain previously observed substrate inhibition.

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

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

38 +/- 6 nm; kcat = 0.020 +/- 0.007 s(-1)) and substrate inhibition above 0.5 mum (Ki = 2.5 +/- 1.3 mum

39 5.7 nM and kcat = 0.032 +/- 0.001 s(-1)) and substrate inhibition above 2 muM.

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

41 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

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

43 mutation was identified that eliminates the substrate inhibition altogether.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

68 6A product analog (K(i) = 7 +/- 0.7 muM) and substrate inhibition at high concentrations require two

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

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

71 +/- 32 nm; n = 1.8 +/- 0.1) and cooperative substrate inhibition at micromolar concentrations ([S](1

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

94 Substrate inhibition by PRPP was observed.

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

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

97 Significant substrate inhibition by this compound suggested that fur

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

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

100 Substrate inhibition can also be exhibited by diazocompo

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

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

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

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

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

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

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

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

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

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

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

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

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

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

115 Substrate inhibition in the direction of aldehyde reduct

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

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

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

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

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

121 -3,17-dione (ADD) and 4-BNC displayed strong substrate inhibition (Ki S approximately 100 muM).

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

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

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

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

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

127 The substrate inhibition model suggested that peptide substr

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

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

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

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

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

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

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

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

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

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

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

139 This substrate inhibition of LdUPRT provides a protective mec

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

141 Substrate inhibition of the process occurs through the f

142 There was substrate inhibition of the sulfation reaction at elevat

143 Substrate inhibition of the thiol-disulfide exchange rea

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

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

146 3HB6H does not exhibit substrate inhibition on the flavin oxidation step, a com

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

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

149 ically trapped intermediate during a suicide substrate inhibition reaction.

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

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

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

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

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

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

156 Substrate inhibition was explained by blockade of produc

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

158 The substrate inhibition was not competitive with MgATP and

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

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

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

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

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

164 Substrate inhibition was observed at subsaturating conce

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

166 Substrate inhibition was observed for most substrates.

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

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

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

170 To understand substrate inhibition, we exploited the PatchDock algorit

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

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

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

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

175 12-Oxododecanoic acid (12-ODDA) exhibited substrate inhibition, which is consistent with a preferr

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

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

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

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

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

181 Furin exhibited striking substrate inhibition with hexapeptide but not tetrapepti

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

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

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