Die Kinetik der Invertinwirkung.¶
Michaelis, L., & Menten, M. L. (1913). Die Kinetik der Invertinwirkung. Biochemische Zeitschrift, 49, 333-369.
Cited by¶
6 citations across 6 artifacts.
Each citation links to the sentence it supports in the citing article.
Primes¶
- Function (Mapping)
- In biology, dose-response curves, enzyme kinetics (Michaelis-Menten
This sourceFounding enzyme-kinetics paper (v = V_max·[S] / (K_m + [S])). Precursor: Henri, Victor. Lois générales de l'action des diastases (Paris: Hermann, 1903). Modern English translation and reassessment: Johnson, Kenneth A., and Roger S. Goody. "The Original Michaelis Constant: Translation of the 1913 Michaelis-Menten Paper." Biochemistry 50, no. 39 (October 2011): 8264–8269, DOI 10.1021/bi201284u.
- In biology, dose-response curves, enzyme kinetics (Michaelis-Menten
- Inhibition
- The otherwise-active transformation is an enzyme-catalyzed reaction converting substrate S to product, proceeding at a native rate set by Michaelis-Menten kinetics.
This sourceOriginal derivation of the Michaelis-Menten rate law setting the native rate of an enzyme-catalyzed reaction. (English translation: Goody & Johnson, Biochemistry 50 (2011): 8264–8269, https://doi.org/10.1021/bi201284u.)
- The otherwise-active transformation is an enzyme-catalyzed reaction converting substrate S to product, proceeding at a native rate set by Michaelis-Menten kinetics.
- Nonlinearity
- Form-of-nonlinearity: a named structural class — polynomial (`x²`, `x³`, `xy`), saturation (`tanh`, Hill function, Michaelis-Menten
This sourceFounding enzyme-kinetics paper (v = V_max·[S] / (K_m + [S])). Precursor: Henri, Victor. Lois générales de l'action des diastases (Paris: Hermann, 1903). Modern English translation and reassessment: Johnson, Kenneth A., and Roger S. Goody. "The Original Michaelis Constant: Translation of the 1913 Michaelis-Menten Paper." Biochemistry 50, no. 39 (October 2011): 8264–8269, DOI 10.1021/bi201284u.
- Form-of-nonlinearity: a named structural class — polynomial (`x²`, `x³`, `xy`), saturation (`tanh`, Hill function, Michaelis-Menten
- Reaction Intermediate
- Consider the enzyme-catalyzed conversion of substrate S to product P under the Michaelis-Menten mechanism.
This sourceOriginal formulation of the enzyme-substrate complex as the reaction intermediate governing catalytic rate. (English translation: Goody & Johnson, Biochemistry 50 (2011): 8264–8269.)
- Consider the enzyme-catalyzed conversion of substrate S to product P under the Michaelis-Menten mechanism.
- Receptor Saturation
- As Michaelis and Menten (1913) originally derived for enzyme-substrate kinetics,
This sourceFounding enzyme-kinetics paper (v = V_max·[S] / (K_m + [S])). Precursor: Henri, Victor. Lois générales de l'action des diastases (Paris: Hermann, 1903). Modern English translation and reassessment: Johnson, Kenneth A., and Roger S. Goody. "The Original Michaelis Constant: Translation of the 1913 Michaelis-Menten Paper." Biochemistry 50, no. 39 (October 2011): 8264–8269, DOI 10.1021/bi201284u.
- As Michaelis and Menten (1913) originally derived for enzyme-substrate kinetics,
Domain-specific¶
- Kinetics
- The same kinetic framework carries from organic-reaction mechanisms (SN1 vs. SN2 rate law differences determining stereochemical outcome), through phase-transformation kinetics in materials science (nucleation and growth rates determining microstructure under a given annealing schedule), to pharmacokinetics (absorption and elimination rate constants determining whether a drug reaches therapeutic concentration before being cleared), and to enzyme catalysis and metabolic-flux analysis, where Michaelis-Menten kinetics describes the saturation behavior of enzyme-catalyzed rate-limiting steps
Supported in partVerified against a saved copy of the source
“Michaelis, L. und MiB Maud L. Menten. Die Kinetik der Invertin-”
- The same kinetic framework carries from organic-reaction mechanisms (SN1 vs. SN2 rate law differences determining stereochemical outcome), through phase-transformation kinetics in materials science (nucleation and growth rates determining microstructure under a given annealing schedule), to pharmacokinetics (absorption and elimination rate constants determining whether a drug reaches therapeutic concentration before being cleared), and to enzyme catalysis and metabolic-flux analysis, where Michaelis-Menten kinetics describes the saturation behavior of enzyme-catalyzed rate-limiting steps
Verification¶
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Links previously used in the corpus¶
Before the registry existed this work was also linked 1 other way.
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