Die Kinetik der Invertinwirkung.

Michaelis, L., & Menten, M. L. (1913). Die Kinetik der Invertinwirkung. Biochemische Zeitschrift, 49, 333-369.

Type

Journal article

Intellectual base

Primary research

Year

1913

Link

https://www.ncbi.nlm.nih.gov/pubmed/24180270

Cited from

chemistry_materials, mathematics, pharmacology_toxicology

Cited by

5 citations across 5 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.

• 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.)

• 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.

• 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.)

• 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.

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• https://www.biodiversitylibrary.org/bibliography/100066 ×1

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