Kcat oor Frans
Kcat
Vertalings in die woordeboek Engels - Frans
kcat
The activators increase kcat but have no effect on Km.
Les activateurs augmentent le kcat mais n'exerce aucun effet sur le Km.
constante catalytique
k catalytique
Geskatte vertalings
Vertoon algoritmies gegenereerde vertalings
voorbeelde
Advanced filtering
Voorbeelde moet herlaai word.
Although there was a six-fold increase in both Km and kcat values for the peptidic substrate (13.3 μM and 8.1 s−1, respectively), when compared with values for the natural substrate (2.04 μM and 1.41 s−1), the catalytic efficiency (0.69 μM−1
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The mechanism of ester hydrolysis catalyzed by carboxypeptidase A is discussed in the light of the above observations and the known crystal structure of the enzyme. A definition of specific and non-specific substrates for this enzyme based on the observed pH profiles for kcat/Km is proposed.
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The second-order acylation rate constants (kcat/Km(app)) obey a linear free energy relationship with ρ = +0.63 for phenyl hippurates and ρ = +0.46 for phenyl N-benzyloxycarbonyl-L-tryptophanates when substituents are introduced into the phenyl group of the ester function.
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For carbonic anhydrase II, this proton transfer is rate determining for the maximal turnover number kcat of 106 s−1.
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Analysis by plotting log [Mg2+]mid vs. pH showed that the binding of Mg2+ to the free enzyme involves two groups with pKa values in the vicinity of 7 and one group with a pKa value near 5.5. (The values referred to as [Mg2+]mid are the Mg2+ concentrations that resulted in kcat values midway between basal and maximum.)
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The enzyme has a kcat value for catalysis of approximately 185 sec-1 for 1, 4-β-D-xylobiose (X2) when measured at a pH of 5.3 and a temperature of 25°C; this is at least 10 -fold greater than reported for other xylosidases at 25oC and their optimal pH.
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Catalytic Functions 6 Substrate Specificity 6 Optimum pH and Temperature 6 Catalytic Constants KM and Kcat 6 Cofactors 6 Enzymatic Activity 6
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The (kcat/khyd) values for the yeast a-glucosidase-catalyzed reactions of 11 and 9 are 1.6 × 105 and 2.0 × 109, respectively, when compared to the spontaneous uncatalyzed reactions.
CapsaïcineGiga-fren Giga-fren
The catalytic efficiency (Kcat/KM) values for p-nitrophenyl-β-D-glucoside and cellobiose were respectively 240.48 mM-1s-1 and 134.80 mM-1s-1.
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Based on the observed effect of leaving-group ability, it is proposed that the rate-determining step for kcat (and likely for kcat/Km as well) with each bacterial enzyme is as follows: sialylation, which is concerted with conformational change for V. cholerae; and conformational change for S. typhimurium and C. perfringens.
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For the least efficient of the carbonic anhydrases, isozyme III, kcat/Km near 3 × 105 M−1 ∙s−1 is not diffusion controlled; nevertheless, proton transfer from zinc-bound water to solution is still rate limiting for a maximal turnover of 104 s−1.
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Low temperature adaptation in the ectothermic (flounder) enzyme is indicated by a reduced enthalpy of activation for kcat (enzyme turnover number, s−1) and increased catalytic efficiency.
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The kinetic constants for the Mn-independent oxidation of 2-methylanthracene at pH 4 were determined, and the values we obtained were a kcat of 145/min, KM,app of 23.8 mmol/L for the aromatic substrate, and KM,app of 0.2 mmol/L for hydrogen peroxide.
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These data indicate that it is difficult to bind Mg2+ at lower pH values, but the kcat and Km values of the enzyme, and therefore the rates of galactosylation (k2), degalactosylation (k3), and binding (Ks), do not change substantially as a function of pH provided that a Mg2+ is bound to the enzyme.
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There was a correlation of the relative inhibition with the size of the substituted residue but no relationship to the presence or absence of a negative charge, and as the relative inhibition by the planar and positively charged galactose analogs increased, k3 (hydrolysis; degalactosylation) and kcat/Km (catalytic efficiency) values decreased.
Durée de conservationGiga-fren Giga-fren
If the Mg2+ concentration was high enough, the kcat values at pH values down to 5.0 remained at the same high level as at pH 7 and 7.6 (600–620 s−1 with o-nitrophenyl-β-D-galactopyranoside as the substrate).
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It is known as the catalytic constant, symbolized by kcat (or sometimes as k0).
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Early in the season, carbon fixation per RuBisCO peaked near the expected turnover rate (kcat) for a C4 plant, but then declined.
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Relative to the spontaneous methanolysis rate constant (ko), the catalytic rate constant obtained at saturation, kcat, is larger for metal-ion catalysis than for H+ catalysis.
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Activation energy differences (DDGs), as determined by differences in the kcat/Km values, indicated that substitutions for His-391 caused very large destabilizations (22.8-35.9 kJ/mol) of the transition state.
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Another useful constant is kcat, also called the turnover number, which is the number of substrate molecules handled by one active site per second.
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Solvent isotope effects kcat(H2O)/ kcat(D2O) range from 2.1 to 3.0 with proton inventories (dependences of kcat(n) on n, the atom fraction of deuterium in the water component of the solvent) that are linear, regardless of the amount of acetonitrile in the medium.
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Significant differences among the two ecotypes were found for catalytic constant (Kcat) estimates obtained with purified PEPC.
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An isolated polypeptide comprising the amino acid sequence of serum paraoxonase (PON1) having catalytic efficiency of kcat/KM ≈106 M-1min-1 for a nerve-agent substrate.
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The hydrolysis of N-carbobenzyloxyaminoacyl-O-p-nitrophenyl esters derived from L-leucine, L-phenylalanine, and L-tryptophan, with catalysis by bovine pancreatic a-chymotrypsin at pH 7.00 at 25.00°C in water containing acetonitrile from 15.0% to 60% (v/v), exhibits values of kcat/Km that decrease as the 34th to 36th power of the activity of water and values of kcat that are essentially constant.
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67 sinne gevind in 9 ms. Hulle kom uit baie bronne en word nie nagegaan nie.