ライフサイエンスコーパス: catalytic efficiency

1 gn and construct a 3D hybrid to maximize the catalytic efficiency.

2 llyl complex that greatly diminished overall catalytic efficiency.

3 an free enzymes while maintaining comparable catalytic efficiency.

4 hydrogen abstraction and thus result in low catalytic efficiency.

5 DNA and nucleotides, resulting in diminished catalytic efficiency.

6 s revealed position 596 also plays a role in catalytic efficiency.

7 acid addition enhances their selectivity and catalytic efficiency.

8 levels, enzyme product profiles, and enzyme catalytic efficiency.

9 inal domain of the enzyme that may lower its catalytic efficiency.

10 nd, which controls substrate specificity and catalytic efficiency.

11 al cluster/support systems to achieve higher catalytic efficiency.

12 eugenol and also of isoeugenol with a lower catalytic efficiency.

13 he lipid moiety significantly influenced the catalytic efficiency.

14 parent actin affinity, resulting in a higher catalytic efficiency.

15 anges in the enzyme's binding properties and catalytic efficiency.

16 s synthetic organophosphates with remarkable catalytic efficiency.

17 for the microtubule, thus controlling their catalytic efficiency.

18 radients that dictate heat and mass flow and catalytic efficiency.

19 lation impeded substrate binding and reduced catalytic efficiency.

20 achieved without location-dependent loss of catalytic efficiency.

21 rate binding and its relationship to overall catalytic efficiency.

22 nhances enzymatic hydroxylation and improves catalytic efficiency.

23 l "cap," a region previously known to affect catalytic efficiency.

24 eplacing the His124 also resulted in a lower catalytic efficiency.

25 se P proteins, exhibit negligible changes in catalytic efficiency.

26 ng pathways in enzymes are critical to their catalytic efficiency.

27 , the goal often is to increase stability or catalytic efficiency.

28 and present comparable, extremely high COox catalytic efficiency.

29 ing was required for additional increases in catalytic efficiency.

30 the acyl-enzyme intermediate limits overall catalytic efficiency.

31 ate-limiting step over a 10(4)-fold range of catalytic efficiency.

32 his loop have either no or modest effects on catalytic efficiency.

33 nal contacts with protein substrates enhance catalytic efficiency.

34 n of the stimulatory effect of Tat on P-TEFb catalytic efficiency.

35 horylation, providing a 7.4-fold increase in catalytic efficiency.

36 ansformations and can strongly influence the catalytic efficiency.

37 t HDL essential for optimal LCAT binding and catalytic efficiency.

38 trate ARPP, with AtcpFHy/PyrP1 having higher catalytic efficiency.

39 , and resulting in partial permanent loss of catalytic efficiency.

40 eservation in both LCAT binding affinity and catalytic efficiency.

41 ained using pinacolborane with unprecedented catalytic efficiency.

42 d drug affinity is limited by a trade-off in catalytic efficiency.

43 vers compared with APX2 without compromising catalytic efficiency.

44 itical for both LCAT binding to HDL and LCAT catalytic efficiency.

45 unctional enzymes and just one has very high catalytic efficiency.

46 efficiently improve the enzyme activity and catalytic efficiency.

47 used yeast-display evolution to improve its catalytic efficiency.

48 rea of these materials and hence improve the catalytic efficiency.

49 both correct and mispair formation with high catalytic efficiency.

50 eacts with CO2 and produces CO with the same catalytic efficiency.

51 s but rather through directly increasing its catalytic efficiency.

52 cess the same substrates, but with different catalytic efficiencies.

53 lyglutamylated forms of CH2-THF with similar catalytic efficiencies.

54 statistics between mutations determine their catalytic efficiencies.

55 ighly evolvable and can be optimized to high catalytic efficiencies.

56 ctivity in reduction of l-cystine, where the catalytic efficiency (2,217 min(-1)microM(-1)) coupled t

57 Mutagenesis of Glu64 to Ala decreases the catalytic efficiency 27-fold, which demonstrates the imp

58 zyme showed very low K(m) (0.34 mM) and high catalytic efficiency (3.3x10(6)) with 4-methyl catechol.

59 aved and inactivated by plasmin in solution (catalytic efficiency = 8.3 x 10(3) M(-1)s(-1)).

60 eaction system showed significantly enhanced catalytic efficiency, about 30 fold higher than that of

61 The catalytic efficiency achieved for 3beta-HSD activity is

62 with at least five turnovers and no loss of catalytic efficiency after 3.7 h.

63 The CocH-Fc not only has a high catalytic efficiency against cocaine but also, like an a

64 There is little correlation in catalytic efficiencies among the five caspases, suggesti

65 Catalytic efficiencies and intrinsic scanning distances

66 The mechanism and origins of catalytic efficiencies and selectivities of these reacti

67 ally distinct categories based on both their catalytic efficiencies and their sequence-structural rel

68 e with a 2 order of magnitude improvement in catalytic efficiency and a mixture of zinc and manganese

69 Our results suggest that the reduced catalytic efficiency and a propensity of GlnRS mutants t

70 yst was recycled two times with some loss of catalytic efficiency and a small erosion of ee.

71 The reduced enzyme displayed improved catalytic efficiency and decreased effectiveness of subs

72 ing the modification order and enhancing the catalytic efficiency and fidelity of the synthetase.

73 xins, decamer formation is important for the catalytic efficiency and has been associated with an enh

74 gment 1 (S1) containing A1 (S1A1) has higher catalytic efficiency and higher affinity for actin than

75 me performance, calculated as the product of catalytic efficiency and relative expression level, was

76 Enzymes, though capable of high catalytic efficiency and remarkable reaction selectivity

77 Furthermore, we show that the catalytic efficiency and selectivity toward a rhomboid s

78 atalyzes azido-Ala in place of Gly with high catalytic efficiency and selectivity.

79 of phage HL is functionally independent, its catalytic efficiency and specificity is influenced by th

80 paradigms for understanding the evolution of catalytic efficiency and specificity, the use of bioinfo

81 m (GndHCl) = 0.53 M], without altering their catalytic efficiency and stereoselectivity properties.

82 NA(Pyl-opt) had no significant effect on the catalytic efficiency and substrate binding of PylRS enzy

83 , which include 4 M KCl, the enzyme exhibits catalytic efficiency and substrate saturation at metabol

84 ation of HAD hydrolases contributes to their catalytic efficiency and substrate specificity.

85 led >3 order of magnitude reductions in both catalytic efficiency and substrate stringency.

86 ect nt T opposite 3-dMeA with a much reduced catalytic efficiency and that both Pols exhibit a high p

87 revealed an intriguing relationship between catalytic efficiency and the base employed in the cross-

88 plays a crucial role in determining both the catalytic efficiency and the chemo-, regio- and enantios

89 llowed by PAGE-based assays to determine the catalytic efficiency and the misinsertion frequency oppo

90 availability of a range of enzymes with high catalytic efficiency and well defined substrate specific

91 respect to their substrate binding affinity, catalytic efficiency, and catalytic mechanism.

92 dsr1 also showed low succinate affinity, low catalytic efficiency, and increased resistance to SDH co

93 and specificity, oxidative regioselectivity, catalytic efficiency, and stability.

94 Based on expression levels, catalytic efficiency, and the fact that the lung cells o

95 h1p inhibited its PAP activity by decreasing catalytic efficiency, and the inhibitory effect was prim

96 also showed excellent binding affinities and catalytic efficiencies approaching that of natural enzym

97 The second site, characterized by low catalytic efficiency ( approximately 3 and approximately

98 MFAT exhibited much higher catalytic efficiency as a synthase of 11-cis-REs versus

99 iL can result in up to a 20-fold increase in catalytic efficiency as well as enhancement in polymer m

100 rticle shapes display significantly enhanced catalytic efficiency at 40 degrees C.

101 of protein cleavage sites and found similar catalytic efficiencies between the protein and peptide s

102 compounds, CYP2A13 does so with much higher catalytic efficiency, but the structural basis for this

103 C-terminal to the catalytic core potentiate catalytic efficiency by between 12- and 45-fold, with th

104 prp8 RH alleles link splicing fidelity with catalytic efficiency by biasing the relative stabilities

105 These mutations lower the catalytic efficiency by factors of 10-50, primarily by d

106 tion at Val-216 that leads to an increase in catalytic efficiency by increasing kcat, but not signifi

107 hermophilus UDGa to QD doublet increases the catalytic efficiency by over one hundred-fold and sevent

108 degrade different antibiotics in vitro with catalytic efficiencies comparable to that of an average

109 These clones possess 100-140 fold enhanced catalytic efficiency compared to hASNase1.

110 exhibits a more than three-fold increase in catalytic efficiency compared to the Pt loaded carbon sp

111 to an increased K(M) value and a much lower catalytic efficiency, confirming the role of this residu

112 However, the catalytic efficiency decreases for larger multiprotein c

113 sults show that inside the cell the apparent catalytic efficiency decreases, and Km increases with in

114 in the reactions of HPNP, GpU, and UpU, the catalytic efficiency depends very little on whether the

115 s is also operational in vivo, enhancing the catalytic efficiency during the final electron transfer

116 an covalently modify inactive Rabs with high catalytic efficiency even when GDP is bound to the GTPas

117 BiFae1B showed low catalytic efficiencies for both substrates.

118 The catalytic efficiencies for correct nucleotide insertion

119 The catalytic efficiencies for cyclization of 3-OPP and 4-OP

120 Common IDH1 mutations have moderate catalytic efficiencies for D2HG production, whereas rare

121 udy, we use quantitative MS to determine the catalytic efficiencies for hundreds of natural protease

122 s found to have 8-fold and 3,500-fold higher catalytic efficiencies for hydrolysis of ISG15-AMC than

123 oxidized and reduced isoforms have different catalytic efficiencies for hydrolysis of MetAP2 peptide

124 76G, and E140G/W164S/K176G variants attained catalytic efficiencies for oxidation of 2,2'-azino-bis(3

125 that HalM2 and ProcM have markedly different catalytic efficiencies for the various reactions they ca

126 rly, mGsta4, the murine GST with the highest catalytic efficiency for 4HNE, is down-regulated to appr

127 portant strategy to tune and to optimize its catalytic efficiency for a chemical reaction.

128 Both G151D and R150Q exhibit markedly lower catalytic efficiency for adenosine triphosphate hydrolys

129 he alanine with aspartate decreased the GalB catalytic efficiency for CHM by 9.5 x 10(4)-fold, and th

130 lacking the A3 domain exhibit 15-fold lower catalytic efficiency for cleavage after Arg(180) than fo

131 cocaine hydrolysis, and obtain a much higher catalytic efficiency for cocaine conversion than for con

132 seen with (rat) P450 2B1, which has a lower catalytic efficiency for DMN oxidation and a larger acti

133 ted]and N322A glycosynthases had much higher catalytic efficiency for glycosylating the nonfucosylate

134 mes have different substrate specificity and catalytic efficiency for hydrolysis of both small and ma

135 ts in an enzyme that displays 10-fold higher catalytic efficiency for L-Arg hydrolysis, 12-15 fold re

136 Importantly, SIRT4 catalytic efficiency for lipoyl- and biotinyl-lysine mod

137 Further analyses suggest that the changes in catalytic efficiency for mutant enzymes are correlated t

138 opposite adducts, with up to 150-fold higher catalytic efficiency for O(6)-MeG over guanine in the te

139 re dependent on the selected position, while catalytic efficiency for p-nitrophenyl acetate hydrolysi

140 Supporting this idea is the 200-fold lower catalytic efficiency for rNTP relative to deoxyribonucle

141 It demonstrates high catalytic efficiency for the activation of epoxides, fac

142 The specific catalytic efficiency for xylose compared to glucose was

143 activity above which further improvements in catalytic efficiency had little if any effect on growth

144 enase activity of the P450 enzymes, and this catalytic efficiency has inspired protein engineering to

145 time, we were able to determine hundreds of catalytic efficiencies in parallel.

146 e site amino acid trio in determining OleTJE catalytic efficiency in alkene production and in regulat

147 creased ribonucleotide binding and decreased catalytic efficiency in both primer-dependent and de nov

148 er substrate specificity and fine-tune their catalytic efficiency in cells.

149 d-Ala:d-Ser ligase activity, albeit with low catalytic efficiency in comparison with VanG.

150 ide to primase, which correlates with higher catalytic efficiency in vitro.

151 led to a 2 orders of magnitude reduction in catalytic efficiency in vitro.

152 The catalytic efficiency increased 8.4-fold upon cooperative

153 ions, the changes introduced likely improved catalytic efficiency indirectly in both cases by bolster

154 The catalytic efficiencies (k cat/K m) indicated that cellot

155 nging to simultaneously assess the intrinsic catalytic efficiencies (k(cat)/K(M)) of these modificati

156 ble to the fastest NGS chemistries, yet with catalytic efficiencies (k(pol)/K(D)) comparable to natur

157 SULT1A1 gave the highest catalytic efficiency (k(cat)/K(m)) and yielded a single

158 ely K23> K18> K27 approximately K36) and the catalytic efficiency (k(cat)/K(m)) for K9, K14, K18, and

159 the most active of the variants exhibited a catalytic efficiency (k(cat)/K(M)) of 400 M(-1) s(-1) fo

160 ne the kinetic parameters, k(cat), K(M), and catalytic efficiency (k(cat)/K(M)) of catalytic domain S

161 y (V(max)), catalytic constant (k(cat)), and catalytic efficiency (k(cat)/K(m)).

162 owing trend for turnover number (k(cat)) and catalytic efficiency (k(cat)/K(M)): Mn(2+) > Ni(2+) appr

163 nmol retinal/mg BCO1 x h, Km = 17.2 muM and catalytic efficiency kcat/Km = 6098 M(-1) min(-1).

164 of these proteases, turnover number kcat and catalytic efficiency kcat/KM, are largely unknown.

165 ubstrates; however, few data exist about the catalytic efficiencies (kcat/KM) of these substrates, wh

166 s only approximately 2-fold greater than the catalytic efficiency (kcat/Km = 1.3 x 10(7) M(-1) s(-1))

167 on or mutation of the PHD domain reduces the catalytic efficiency (kcat/Km of AdoMet) of ATXR5 up to

168 h five of the six clearly exhibiting reduced catalytic efficiency (kcat/Km) at colder temperatures an

169 rface modalities that permit plasma protease catalytic efficiency (kcat/km) determination by MALDI-TO

170 The catalytic efficiency (kcat/Km) for the removal of a myri

171 correlated with neither the logarithm of the catalytic efficiency (kcat/Km) nor catalytic proficiency

172 otide binding in the D2 domain increases the catalytic efficiency (kcat/Km) of D1 ATP hydrolysis 280-

173 less so than mEar 1 and mEar 2; the relative catalytic efficiency (kcat/Km) of mEar 11 is diminished

174 The catalytic efficiency (kcat/Km) of the variant toward the

175 The catalytic efficiency (Kcat/Km) was 238 s(-1) mM(-1).

176 CYP2B35 showed the highest catalytic efficiency (kcat/KM) with 7-heptoxycoumarin as

177 ained in vitro We found the apparent in vivo catalytic efficiency, kcat/Km , to be lower than in vitr

178 E73D/T77A double mutant regained most of the catalytic efficiency lost in the E73D single mutant.

179 ity of applications emanate from SaSrtA, low catalytic efficiency, LPXTG specificity restriction, and

180 nd selection led to > 2,000-fold increase in catalytic efficiency, mainly via higher k(cat) values.

181 inity for PChlide and an about 6-fold higher catalytic efficiency measured as kcat/Km.

182 d by a fractal Michaelis-Menten model with a catalytic efficiency nearly 17% better than the homogene

183 Catalytic efficiencies of 5-dimethylallyltryptophan synt

184 (with 2,6-dimethoxyphenol and p-hydroquinone catalytic efficiencies of approximately 70 and approxima

185 three single-subunit RNAPs measured from the catalytic efficiencies of correct and all possible incor

186 Fn had no effect on Micro-Pg activation, the catalytic efficiencies of Glu-Pg, Lys-Pg, and Mini-Pg ac

187 In this manuscript, a study of the catalytic efficiencies of inorganic oxoanions such as ar

188 specific for NADPH (Km = 18 to 33 muM), with catalytic efficiencies of more than 10-fold higher for N

189 The catalytic efficiencies of NHC-CO(2) adducts 3 were found

190 ke advantage of the inherent specificity and catalytic efficiencies of proteins.

191 The catalytic efficiencies of TAFI and protein C activation

192 The system proceeds with a catalytic efficiency of 10(5) M(-1) s(-1) and achieves t

193 BiFae1A showed a catalytic efficiency of 12mM s(-1) on para-nitrophenyl-a

194 complex substrate switchgrass increased the catalytic efficiency of a commercial cellulose-degrading

195 Catalytic efficiency of a sphere-shaped nanosized polyox

196 The 16-100-fold higher catalytic efficiency of AA initiation sequence relative

197 these results also reveal the origin of the catalytic efficiency of acetic acid in these transformat

198 of MG in GLO1(-/-) is achieved by increased catalytic efficiency of aldose reductase toward hemithio

199 site lysine residue that contributes to the catalytic efficiency of all nucleic acid polymerases.

200 properties similar to human peroxidases, the catalytic efficiency of bromide oxidation (kcat/KM(app))

201 329 residue and the NADP(+) cofactor for the catalytic efficiency of CHMO.

202 The catalytic efficiency of class D beta-lactamases depends

203 Catalytic efficiency of cleavage after Arg(180) is 7-fol

204 nally conjugated methylcoumarin enhances the catalytic efficiency of deacetylation catalyzed by cobal

205 eration of diarylamines and implies that the catalytic efficiency of diarylamine antioxidants is subs

206 led primers because of the intrinsically low catalytic efficiency of DnaG.

207 The catalytic efficiency of E30-6 for cocaine hydrolysis is

208 wo classes of mAbs, which both increased the catalytic efficiency of FVIIa more than 150-fold.

209 The catalytic efficiency of Gcs for acyl-ACP was 10-fold hig

210 wledge of the factors that contribute to the catalytic efficiency of LGK can be used to improve appli

211 The catalytic efficiency of Li3CARS to produce 3-carene was

212 The catalytic efficiency of mixed Cu(I)-Cu(II) system in sit

213 In nature, the catalytic efficiency of multienzyme complexes highly dep

214 The overall catalytic efficiency of oxidation was ~10-fold higher th

215 cone PDE6 that contribute to the accelerated catalytic efficiency of PDE6 were identified but require

216 recognition can be employed to increase the catalytic efficiency of peptide-capped Pd nanoparticles.

217 e effects of substituents and cavity size on catalytic efficiency of proline-rich cyclopeptoids under

218 nts were improved in various degrees and the catalytic efficiency of PULDeltaN5, PULDeltaN45, PULDelt

219 ate kinetic parameters demonstrates that the catalytic efficiency of QNS was severalfold higher for l

220 Whereas the catalytic efficiency of rhinovirus 3C protease is approx

221 case activity plays an essential role in the catalytic efficiency of RNase R.

222 Ile-184 in p66 (p66(184I)) decreased the catalytic efficiency of RT (k(pol)/K(d)(.dNTP)), primari

223 ntrations induce up to a 35-fold increase in catalytic efficiency of SIRT6 but not SIRT1.

224 this interaction substantially impaired the catalytic efficiency of Tet proteins in oxidizing 5-mC t

225 The median catalytic efficiency of the computationally selected enz

226 They increase the catalytic efficiency of the encapsulated enzymes while s

227 residue caused a 40- to 120-fold decrease in catalytic efficiency of the enzyme due to an increase in

228 e to degradation and maintained or increased catalytic efficiency of the enzyme in which the desired

229 In contrast, the mutation decreases the catalytic efficiency of the enzyme to 1% at the permissi

230 osteric site of COX-2 results in a decreased catalytic efficiency of the enzyme toward 2-AG, whereas

231 , and although adsorption likely reduces the catalytic efficiency of the enzyme, this reduction is al

232 ctivity, deletion of this domain reduced the catalytic efficiency of the enzyme.

233 eraction increases both the processivity and catalytic efficiency of the error-free bypass of a 8-oxo

234 mutations proved effective in enhancing the catalytic efficiency of the hemoprotein in these reactio

235 partment and the cytosol correlated with the catalytic efficiency of the N-myristoyltransferase actin

236 in an approximately 17-fold increase in the catalytic efficiency of the PCM activity and a concomita

237 luorescence of the cells correlated with the catalytic efficiency of the PTE variant expressed in eac

238 The catalytic efficiency of the resulting stereoselective, a

239 t of the complex leads to enhancement of the catalytic efficiency of the SET domain and thus the prop

240 reducing the K(m) (4-fold) and improving the catalytic efficiency of the SUPA complex (6-fold).

241 Additionally, the catalytic efficiency of Trx1 as an electron donor for RN

242 The catalytic efficiency of Trx1 was 3 and 20 times higher t

243 E3-UbcH5B-Ub complex, thereby improving the catalytic efficiency of Ub transfer.

244 anism establishing that Atpif1 regulates the catalytic efficiency of vertebrate Fech to synthesize ha

245 the significance of atomic positions on the catalytic efficiency of water oxidation.

246 with H2O2 were tested and compared with the catalytic efficiency of White's parent complex 1.Fe(OTf)

247 f iron and zinc in the active site and had a catalytic efficiency of ~10(3) M(-1) s(-1).

248 al signal of human CYP2A6 and to improve its catalytic efficiency on electrode surfaces.

249 if in a wild type member of GH5 enhanced its catalytic efficiency on glucan and mannan substrates by

250 228M-W263M) demonstrates a large increase in catalytic efficiencies over the wild-type enzyme, with i

251 a Cys93-Tyr157 crosslink that increases its catalytic efficiency over 10-fold.

252 s, and which displays a 100-fold increase in catalytic efficiency over wild-type GCK.

253 even designs expressed solubly and exhibited catalytic efficiencies similar to previously designed re

254 0(6) m(-1) s(-1), indicating that LPMOs have catalytic efficiencies similar to those of peroxygenases

255 ge of lycopene to yield acycloretinal with a catalytic efficiency similar to that of beta-carotene.

256 functional theory calculations show that the catalytic efficiency stems from the optimal distribution

257 Their catalytic efficiency strongly depends on the type of sub

258 properties of Dbl family proteins, including catalytic efficiency, substrate selectivity, and signali

259 rported inhibitor revealed no differences in catalytic efficiency, substrate specificity, and inhibit

260 parameters of diverse enzymes with disparate catalytic efficiencies, such as chymotrypsin, fumarase,

261 he oxygen evolution reaction in KOH with its catalytic efficiency surpassing the commercial Ir cataly

262 alysts for several reactions, but with lower catalytic efficiencies than naturally occurring enzymes.

263 eins purified in vitro show 10-20-fold lower catalytic efficiency than ChaC1, although they showed co

264 g more than three orders of magnitude higher catalytic efficiency than commonly used substrates of el

265 Although glyco-KLK2 has a considerably lower catalytic efficiency than glycan-free KLK2 toward peptid

266 aloduracin), catalyzes reactions with higher catalytic efficiency than ProcM, which modifies 29 diffe

267 -coumaraldehyde > sinapaldehyde, with higher catalytic efficiency than that of both wild-type SbCAD4

268 f tetrameric histone (H3/H4) substrates with catalytic efficiencies that are 40-300-fold higher than

269 generated two enzymes having NADH-dependent catalytic efficiencies that are greater than the wild-ty

270 oids the off-cycle intermediate and provides catalytic efficiencies that are superior to those of cat

271 helix, hydrolyses p-nitrophenyl acetate with catalytic efficiencies that match the most-efficient red

272 oxamniquine, yet we observed differences in catalytic efficiency that implicate kinetics as the dete

273 dity of the Bronsted acid is crucial for the catalytic efficiency: the less acidic phosphoric acids a

274 rotein of those mutants showed a decrease in catalytic efficiency, thereby suggesting a reason for th

275 lly design increases in pol processivity and catalytic efficiency through computational DNA binding p

276 ed novel HDAC8-specific substrates with high catalytic efficiency, thus presenting a general strategy

277 s than human TK1 with the following order of catalytic efficiencies: thymidine > deoxyuridine >> deox

278 improve both active site properties and the catalytic efficiency to be competitive with the native e

279 Its catalytic efficiency toward l-tyrosine was found to be 4

280 Catalytic efficiency toward synthetic substrate is lower

281 ases possess the higher binding affinity and catalytic efficiency toward their cognate CPs in compari

282 s of magnitude, achieving absolute values of catalytic efficiencies up to 10(6) M(-1) s(-1).

283 the presence of alpha-diazoesters with high catalytic efficiency (up to 4,900 turnovers) and excelle

284 sition, resulting in a greater NAD-dependent catalytic efficiency using site-directed mutagenesis.

285 Phosphorylation reduced (6-fold) the catalytic efficiency (V(max)/K(m)) of Pah1p and reduced

286 esis, evaluation of the pH dependence of the catalytic efficiency (V(max)/K(M)), and kinetic characte

287 purified recombinant human BCO1 in terms of catalytic efficiency values (kcat/Km).

288 label-free quantitation is used to ascertain catalytic efficiency values for individual peptide subst

289 The catalytic efficiency values of these substrates are lowe

290 erfacial PA binding (Km(B) = 4.2 mol %), and catalytic efficiency (Vmax = 557 mumol/min/mg).

291 dy-state kinetic analysis revealed that Dpo4 catalytic efficiency was strongly influenced by the prim

292 silica surfaces, the observed differences in catalytic efficiency were correlated with an unprecedent

293 eight MetO-containing compounds with similar catalytic efficiencies, whereas MSRB was specialized for

294 In contrast, CYP2B37 showed the highest catalytic efficiency with 7-ethoxy-4-(trifluoromethyl)co

295 cluding model lignin compounds, in which the catalytic efficiency with ABTS (kcat(app)/Km(app) = (1.7

296 avonoid prenyltransferases, but the apparent catalytic efficiency with genistein is considerably high

297 demonstrating that the enzyme has equivalent catalytic efficiency with pyridoxal, pyridoxamine and py

298 a greater than 400-fold improvement in OmpT catalytic efficiency, with a kcat /Km value of 6.1x10(6)

299 oth Zn(II) and Cu(II) complexes exhibit good catalytic efficiency, with a superiority of the 1,2-vici

300 eplacing the Glu126 also resulted in a lower catalytic efficiency, with yet a third type of EPR signa