Sulfur compounds from the mushroom Boletus pseudocalopus and their bioactivity

Planta Medica ◽  
2012 ◽  
Vol 78 (11) ◽  
Author(s):  
CS Kim ◽  
KH Kim ◽  
SU Choi ◽  
KR Lee
Keyword(s):  
Sulfur Compounds

Modeling Trienzyme Biosensor at Internal Diffusion Limitation

2004 ◽  
Vol 9 (2) ◽  
pp. 139-144 ◽  
Author(s):  
J. Kulys
Keyword(s):  
Immobilized Enzymes ◽  
Internal Diffusion ◽  
Significant Response ◽  
Diffusion Limitation ◽  
Enzyme Reactions ◽  
Substrate Conversion ◽  
Apparent Stability ◽  
Biosensor Response

A model of biosensor containing three immobilized enzymes utilizing consecutive substrate conversion in the chain was developed. The modeling was performed at an internal diffusion limitation and a steadystate condition. The calculations showed that significant response of biosensors was produced if diffusion modules were larger than 1 for all enzyme reactions. Due to diffusion limitation the apparent stability of biosensor response increased many times in comparison to stability of the most labile enzyme of the chain.

A kinetic analysis of coupled sequential enzyme reactions

2018 ◽  
Author(s):  
Justin Eilertsen ◽  
Santiago Schnell
Keyword(s):  
Enzyme Assay ◽  
Sequential Reaction ◽  
Enzyme Reactions ◽  
Indicator Reaction ◽  
Single Substrate ◽  
Complex Sequences ◽  
Catalyzed Reactions ◽  
Enzyme Catalyzed Reactions ◽  
Single Enzyme

<div>As a case study, we consider a coupled enzyme assay of sequential enzyme reactions obeying the Michaelis--Menten reaction mechanism. The sequential reaction consists of a single-substrate, single-enzyme non-observable reaction followed by another single-substrate, single-enzyme observable reaction (indicator reaction). In this assay, the product of the non-observable reaction becomes the substrate of the indicator reaction. A mathematical analysis of the reaction kinetics is performed, and it is found that after an initial fast transient, the sequential reaction is described by a pair of interacting Michaelis--Menten equations. Timescales that approximate the respective lengths of the indicator and non-observable reactions, as well as conditions for the validity of the Michaelis--Menten equations are derived. The theory can be extended to deal with more complex sequences of enzyme catalyzed reactions.</div>

A kinetic analysis of coupled sequential enzyme reactions

2018 ◽  
Author(s):  
Justin Eilertsen ◽  
Santiago Schnell
Keyword(s):  
Enzyme Assay ◽  
Sequential Reaction ◽  
Enzyme Reactions ◽  
Indicator Reaction ◽  
Single Substrate ◽  
Complex Sequences ◽  
Catalyzed Reactions ◽  
Enzyme Catalyzed Reactions ◽  
Single Enzyme

<div>As a case study, we consider a coupled enzyme assay of sequential enzyme reactions obeying the Michaelis-Menten reaction mechanism. The sequential reaction consists of a single-substrate, single enzyme non-observable reaction followed by another single-substrate, single enzyme observable reaction (indicator reaction). In this assay, the product of the non-observable reaction becomes the substrate of the indicator reaction. A mathematical analysis of the reaction kinetics is performed, and it is found that after an initial fast transient, the sequential reaction is described by a pair of interacting Michaelis-Menten equations. Timescales that approximate the respective lengths of the indicator and non-observable reactions, as well as conditions for the validity of the Michaelis-Menten equations are derived. The theory can be extended to deal with more complex sequences of enzyme catalyzed reactions.</div>

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