a<p>The kinetic parameters were calculated by fitting the initial velocities to various concentrations of acceptor substrates in the presence of 10 mm α-Man1<i>P</i> using the Michaelis-Menten equation.</p>b,c<p>The kinetic parameters were calculated by fitting the initial velocities toward various concentrations of donor substrates in the presence of 10 mm β-1,2-Man<sub>2</sub> (<i>b</i>) or 10 mmd-mannose (<i>c</i>) using the Michaelis-Menten equation.</p>d<p>Not detectable. To investigate the acceptor specificities, the synthetic reactions were examined using the following putative carbohydrate acceptors: d-allose, d-altrose, d-arabinose, d-fructose, d-galactosamine, d-galactose, d-galacturonic acid, d-glucosamine, d-glucose, d-glucuroni...
The mechanism of the enzyme reactions is expressed usually as follows. (ER : Michaelis complex) Mich...
The Michaelis-Menten equation for the kinetics of a simple enzyme-catalyzed reaction is based on the...
We provide here the underlying data of the publication "Kinetic modeling of phosphorylase-catalyzed ...
The principal aim of studies of enzyme-mediated reactions has been to provide comparative and quanti...
<p>The reaction mixtures contained (<i>A</i>) 50 mmd-mannose, 50 mm α-Man1<i>P</i>, and 64 nm Teth51...
*<p>Approximately 30 nmol Sia per 100 µg fetuin; 2 mM lactose was used as acceptor substrate.</p>**<...
<p>Kinetics parameters for different bacterial GMD enzymes using GDP-D-mannose as substrate.</p
The kinetic properties of enzymes are often reported using the apparent KM and Vmax appropriate to t...
To achieve transition from lab scale enzyme studies to industrial applications, understanding of enz...
Many b-galactosidases show large differences in galacto-oligosaccharide (GOS) production and lactose...
To explain the kinetics of enzyme-substrate reactions, Michaelis and Menten (1913) came up with a me...
A new micro-kinetic model is proposed for galacto-oligosaccharide (GOS) synthesis with β-galactosida...
We describe a new data-processing method for the kinetic quantification of substrates of enzyme-cata...
This chapter introduces the kinetic models of metabolism followed by examples on the construction of...
1045-1051The kinetics of immobilized enzymes can not be analyzed by means of the simple Michaelis-M...
The mechanism of the enzyme reactions is expressed usually as follows. (ER : Michaelis complex) Mich...
The Michaelis-Menten equation for the kinetics of a simple enzyme-catalyzed reaction is based on the...
We provide here the underlying data of the publication "Kinetic modeling of phosphorylase-catalyzed ...
The principal aim of studies of enzyme-mediated reactions has been to provide comparative and quanti...
<p>The reaction mixtures contained (<i>A</i>) 50 mmd-mannose, 50 mm α-Man1<i>P</i>, and 64 nm Teth51...
*<p>Approximately 30 nmol Sia per 100 µg fetuin; 2 mM lactose was used as acceptor substrate.</p>**<...
<p>Kinetics parameters for different bacterial GMD enzymes using GDP-D-mannose as substrate.</p
The kinetic properties of enzymes are often reported using the apparent KM and Vmax appropriate to t...
To achieve transition from lab scale enzyme studies to industrial applications, understanding of enz...
Many b-galactosidases show large differences in galacto-oligosaccharide (GOS) production and lactose...
To explain the kinetics of enzyme-substrate reactions, Michaelis and Menten (1913) came up with a me...
A new micro-kinetic model is proposed for galacto-oligosaccharide (GOS) synthesis with β-galactosida...
We describe a new data-processing method for the kinetic quantification of substrates of enzyme-cata...
This chapter introduces the kinetic models of metabolism followed by examples on the construction of...
1045-1051The kinetics of immobilized enzymes can not be analyzed by means of the simple Michaelis-M...
The mechanism of the enzyme reactions is expressed usually as follows. (ER : Michaelis complex) Mich...
The Michaelis-Menten equation for the kinetics of a simple enzyme-catalyzed reaction is based on the...
We provide here the underlying data of the publication "Kinetic modeling of phosphorylase-catalyzed ...