Enzyme kinetics

molecule upon which an enzyme acts

Model of enzyme kinetics

study of biochemical reaction rates catalysed by an enzyme

chemical property

type of regulation of enzyme activity

graph of enzyme kinetics

series of chemical reactions which are initiated by a stimulus acting on a receptor that is transduced to the cell interior through second messengers and ultimately to effector molecules, resulting in a cell response to the initial stimulus

relationship between the dissociation constant and the degree of dissociation of a weak electrolyte

the number of substrate molecule each enzyme site converts to product per unit time.

type of enzyme inhibition

Enzyme rate limited by diffusion

In biochemistry, ABTS ('''2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)''') is a chemical compound used to observe the reaction kinetics of specific enzymes. A common use for it is in the enzyme-linked immunosorbent assay (ELISA) to detect the binding of molecules to each other.

Cooperativity is a phenomenon displayed by systems involving identical or near-identical elements, which act dependently of each other, relative to a hypothetical standard non-interacting system in which the individual elements are acting independently. One manifestation of this is enzymes or receptors that have multiple binding sites where the affinity of the binding sites for a ligand is apparently increased, positive cooperativity, or decreased, negative cooperativity, upon the binding of a ligand to a binding site. For example, when an oxygen atom binds to one of hemoglobin's four binding

Diagram showing the proportion of a receptor bound to a ligand

graph of enzyme kinetics

graph of enzyme kinetics

Empirical model for microorganisms growth