Search results
Results From The WOW.Com Content Network
Therefore, because of sulfa drugs' competitive inhibition, they are excellent antibacterial agents. An example of competitive inhibition was demonstrated experimentally for the enzyme succinic dehydrogenase, which catalyzes the oxidation of succinate to fumarate in the Krebs cycle. Malonate is a competitive inhibitor of succinic dehydrogenase ...
Stereoisomers of Soman, a G-series nerve agent and suicide inhibitor of acetylcholinesterase.Note the non-carbon chiral center.. In biochemistry, suicide inhibition, also known as suicide inactivation or mechanism-based inhibition, is an irreversible form of enzyme inhibition that occurs when an enzyme binds a substrate analog and forms an irreversible complex with it through a covalent bond ...
Acetylcholinesterase (HGNC symbol ACHE; EC 3.1.1.7; systematic name acetylcholine acetylhydrolase), also known as AChE, AChase or acetylhydrolase, is the primary cholinesterase in the body. It is an enzyme that catalyzes the breakdown of acetylcholine and some other choline esters that function as neurotransmitters :
Enzyme induction is a process in which a molecule (e.g. a drug) induces (i.e. initiates or enhances) the expression of an enzyme. Enzyme inhibition can refer to the inhibition of the expression of the enzyme by another molecule; interference at the enzyme-level, basically with how the enzyme works.
An example of a substrate analog that is also a suicide substrate/Trojan horse substrate is penicillin, which is an inhibitory substrate analog of peptidoglycan. [8] Some substrate analogs can still allow the enzyme to synthesize a product despite the enzyme’s inability to metabolize the substrate analog.
An enzyme inhibitor is characterised by its dissociation constant K i, the concentration at which the inhibitor half occupies the enzyme. In non-competitive inhibition the inhibitor can also bind to the enzyme-substrate complex, and the presence of bound substrate can change the affinity of the inhibitor for the enzyme, resulting in a second ...
Most inhibitors of CYP2C9 are competitive inhibitors. Noncompetitive inhibitors of CYP2C9 include nifedipine, [39] [40] phenethyl isothiocyanate, [41] medroxyprogesterone acetate [42] and 6-hydroxyflavone. It was indicated that the noncompetitive binding site of 6-hydroxyflavone is the reported allosteric binding site of the CYP2C9 enzyme. [43]
As glucokinase is a monomeric enzyme with only a single binding site [16] for glucose the cooperativity cannot be explained in terms of classical models of equilibrium cooperativity, but requires a kinetic explanation, such as a slow-transition model [17] or a "memonical" model that invokes enzyme memory. [18]