Most biological processes are controlled by complex systems of enzymatic chemical reactions. Although the majority of enzymatic networks have very elaborate structures, there are many experimental observations indicating that some turnover rates still follow a simple Michaelis-Menten relation with a hyperbolic dependence on a substrate concentration. The original Michaelis-Menten mechanism has ...

Premise Photosynthetic light-response (PLR) curves for leaves are important components of models related to carbon fixation in forest ecosystems, linking the Mitscherlich equation and Michaelis–Menten traits leaf economics spectrum (LES). However, do not consider changes habits (i.e., evergreen deciduous) within-canopy shading variation these PLR curves. Methods Here, we measured sun shade 44 3...

The equation commonly called the Michaelis-Menten equation is sometimes attributed to other authors. However, although Victor Henri had derived the equation from the correct mechanism, and Adrian Brown before him had proposed the idea of enzyme saturation, it was Leonor Michaelis and Maud Menten who showed that this mechanism could also be deduced on the basis of an experimental approach that p...

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...

Enzymes are dynamic entities: both their conformation and catalytic activity fluctuate over time. When such fluctuations are relatively fast, it is not surprising that the classical Michaelis-Menten (MM) relationship between the steady-state enzymatic velocity and the substrate concentration still holds. However, recent single-molecule experiments have shown that this is the case even for an en...

When the concentration dependence of an enzymic reaction or a transport process can be described by the sum of two Michaelis-Menten terms, reliable data that relate reaction rate and substrate concentration can be obtained even when as much as 70 per cent of substrate was consumed during the assay. Each data pair consists of the average reaction rate during an assay and the concentration where ...

The Michaelis-Menten equation, a rectangular hyperbola with two ~arameters ~o b~ specified, . occurs prominently 1n enzyme k,netlcs." Often, ~n consulting situations we need to (i) obtain estlmates standard errors, and confidence intervals for the unknown parameters, which define this nonlinear model for one set of experimental conditions and (ii) compare the parameter estimates under different...

In a conformational nonequilibrium steady state (cNESS), enzyme turnover is modulated by the underlying conformational dynamics. On the basis of a discrete kinetic network model, we use an integrated probability flux balance method to derive the cNESS turnover rate for a conformation-modulated enzymatic reaction. The traditional Michaelis-Menten (MM) rate equation is extended to a generalized f...