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Enzyme activity is a measure of the quantity of active enzyme present and is thus dependent on various physical conditions, which should be specified. It is calculated using the following formula: a = n t = r × V {\displaystyle \mathrm {a} =\mathrm {n} _{\text{t}}=\mathrm {r} \times \mathrm {V} }
The hydrolysis of a protein (red) by the nucleophilic attack of water (blue). The uncatalysed half-life is several hundred years. Proteolysis is the breakdown of proteins into smaller polypeptides or amino acids.
The non-enzymatic glycosylation is also known as glycation or non-enzymatic glycation. It is a spontaneous reaction and a type of post-translational modification of proteins meaning it alters their structure and biological activity.
Enzyme activators are molecules that bind to enzymes and increase their activity. They are the opposite of enzyme inhibitors. These molecules are often involved in the allosteric regulation of enzymes in the control of metabolism. In some cases, when a substrate binds to one catalytic subunit of an enzyme, this can trigger an increase in the ...
PLP is covalently attached to the enzyme via a Schiff Base linkage formed by the condensation of its aldehyde group with the ε-amino group of an enzymatic Lys residue. The Schiff base, which is conjugated to the enzyme's pyridinium ring, is the focus of the coenzyme activity. Ping Pong Bi Bi mechanism of PLP dependent enzyme catalyzed ...
A simplified reaction mechanism for N-acetylglutamate synthase (NAGS). Two mechanisms for N-acetyltransferase function have been proposed: a two-step, ping-pong mechanism involving transfer of the relevant acetyl group to an activated cysteine residue [10] and a one-step mechanism through direct attack of the amino nitrogen on the carbonyl group. [11]
When used to model enzyme rates in vivo , for example, to model a metabolic pathway, this representation is inadequate because under these conditions product is present. As a result, when building computer models of metabolism [1] or other enzymatic processes, it is better to use the reversible form of the Michaelis–Menten equation.
Glucose oxidase enzyme powder from Aspergillus niger. GOx is a dimeric protein, the 3D structure of which has been elucidated. The active site where glucose binds is in a deep pocket. The enzyme, like many proteins that act outside of cells, is covered with carbohydrate chains. GOx is a glucose oxidising enzyme with a molecular weight of 160 kDa.