Theory on the rate equation of Michaelis-Menten type single-substrate enzyme catalyzed reactions
type: Item
instance of: scholarly article
title: Theory on the rate equation of Michaelis-Menten type single-substrate enzyme catalyzed reactions
zbMATH Open document ID: 1385.92024
author: Peng Zhang
publication date: 2018-03-23T00:00:00Z
Mathematics Subject Classification ID: 92C45
zbMATH DE Number: 6852512
zbMATH Keywords: single-substrate enzyme
zbMATH Keywords: Michaelis-Menten kinetics
zbMATH Keywords: steady state approximation
Wikidata QID: Q59306606
MaRDI profile type: Publication
full work available at URL: s10910-017-0791-3
OpenAlex ID: W2952255773
cites work: Mathematical biology. Vol. 1: An introduction.
cites work: Invariant manifold methods for metabolic model reduction
cites work: A simplified perturbation solution of Michaelis-Menten kinetics equations in a ``total'' framework
cites work: A perturbation solution of Michaelis-Menten kinetics in a ``total'' framework
cites work: The Quasi-Steady-State Assumption: A Case Study in Perturbation
cites work: On the appropriate use of asymptotic expansions in enzyme kinetics
cites work: Michaelis-Menten kinetics at high enzyme concentrations
cites work: Quasi-steady-state kinetics at enzyme and substrate concentrations in excess of the Michaelis-Menten constant
cites work: Extending the quasi-steady state approximation by changing variables
cites work: On the Lambert \(w\) function
cites work: Q3997538
cites work: Enzyme kinetics at high enzyme concentration
cites work: Enzyme kinetics far from the standard quasi-steady-state and equilibrium approximations
cites work: On the validity of the steady state assumption of enzyme kinetics
cites work: An Algorithm for Least-Squares Estimation of Nonlinear Parameters
cites work: Design and analysis of computer experiments. With comments and a rejoinder by the authors
DOI: 10.1007/S10910-017-0791-3
published in: Journal of Mathematical Chemistry
description: scientific article; zbMATH DE number 6852512