Many enzymatic reactions in biochemistry are far more complex than the celebrated Michaelis-Menten scheme, but the observed turnover rate often obeys the hyperbolic dependence on the substrate concentration, a relation established almost a century ago for the simple Michaelis-Menten mechanism. To resolve the longstanding puzzle, we apply the flux balance method to predict the functional form of...

Many chemical reactions in biological cells occur at very low concentrations of constituent molecules. Thus, transcriptional gene-regulation is often controlled by poorly expressed transcription-factors, such as E.coli lac repressor with few tens of copies. Here we study the effects of inherent concentration fluctuations of substrate-molecules on the seminal Michaelis-Menten scheme of biochemic...

• This paper studies the Michaelis–Menten model (MM), which plays an important role in pharmacokinetics, from a theoretical as well as a computational point of view. An analytical method for the nonlinear least squares estimation of the MM is introduced. It is proved that the MM model has not a unique parameter estimation (through the nonlinear least squares), and there is not a unique optimal ...

Reliable estimates of Michaelis constants (K(m)) and inhibitor constants may be obtained, in the absence of control over the amount of enzyme being added to any assay system, provided the following constraints are met. Michaelis-Menten kinetics are obeyed. Two rate measurements must be made with the same sample of enzyme: at low and high substrate concentration for determining K(m) or minus and...

Biological networks have been recently found to exhibit many topological properties of the so-called complex networks. It has been reported that they are, in general, both highly skewed and directed. In this paper, we report on the dynamics of a Michaelis-Menten like model when the topological features of the underlying network resemble those of real biological networks. Specifically, instead o...