Bovine lens cytoplasmic aldehyde dehydrogenase exhibits Michaelis-Menten kinetics with acetaldehyde, glyceraldehyde 3-phosphate, p-nitrobenzaldehyde, propionaldehyde, glycolaldehyde, glyceraldehyde, phenylacetylaldehyde and succinic semialdehyde as substrates. The enzyme was also active with malondialdehyde, and exhibited an esterase activity. Steady-state kinetic analyses show that the enzyme ...

We demonstrate the versatility of Al2O3-passivated Si nanowire devices ("nanoribbons") in the analysis of enzyme-substrate interactions via the monitoring of pH change. Our approach is shown to be effective through the detection of urea in phosphate buffered saline (PBS), and penicillinase in PBS and urine, at limits of detection of <200 μM and 0.02 units/mL, respectively. The ability to extrac...

In this paper, the authors use the logistic temporal solution of the generalized Michaelis-Menten kinetics to provide a quantum basis for the tunnelling time and energy evaluations of Brownian enzymic reactions. The mono-substrate and mixed inhibition cases are treated and the associated quantum diagrams of the reaction mechanisms are depicted in terms of intermediate enzyme complexes. The meth...

Abstract. This article is concerned with the asymptotic accuracy of the Computational Singular Perturbation (CSP) method developed by Lam and Goussis to reduce the dimensionality of a system of chemical kinetics equations. The method exploits the presence of disparate time scales to model the dynamics by an evolution equation on a lower-dimensional slow manifold. In this article it is shown tha...

By combining the Michaelis-Menten kinetics of metabolism with the two-stage model of Moolgavkar and Knudson (1981) and the extended two-stage model of carcinogenesis proposed by Tan and Gastardo (1985), this paper proceeds to investigate the effects of metabolism of carcinogens on cancer tumor development. It is shown that the nonlinear kinetics of metabolism of carcinogens affect the dose-resp...

Michaelis and Menten's mechanism for enzymatic catalysis is remarkable both in its simplicity and its wide applicability. The extension for reversible processes, as done by Haldane, makes it even more relevant as most enzymes catalyze reactions that are reversible in nature and carry in vivo flux in both directions. Here, we decompose the reversible Michaelis-Menten equation into three terms, e...

Methods to treat kinetic data for the biodegradation of different plastic materials are comparatively discussed. Different samples commercial formulates were tested aerobic in compost, following standard ISO14855. Starting from raw data, conversion vs. time entries elaborated using relatively simple models, such as integrated equations zero, first and second order, through Wilkinson model, or a...

Inulosucrases catalyze transfer of a fructose moiety from sucrose to a water molecule (hydrolysis) or to an acceptor molecule (transferase), yielding inulin. Bacterial inulin production is rare and a biochemical analysis of inulosucrase enzymes has not been reported. Here we report biochemical characteristics of a purified recombinant inulosucrase enzyme from Lactobacillus reuteri. It displayed...

Soybean lipoxygenase-1 kinetics are known to show product and substrate inhibition. With linoleic acid as the substrate and using a simple Michaelis-Menten formulation, we have shown that K(ss), the substrate inhibition constant was increased by more than five-fold when initial oxygen concentration was increased from 228 to 1140 microM. Excess substrate inhibition is in fact almost avoided at h...