competitive inhibition


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Related to competitive inhibition: Uncompetitive inhibition

competitive inhibition

[kəm′ped·əd·iv ‚in·ə′bish·ən]
(biochemistry)
Enzyme inhibition in which the inhibitor competes with the natural substrate for the active site of the enzyme; may be overcome by increasing substrate concentration.
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The results of this study showed that MA selectively inhibits CYP1A2 and CYP2B6 in HLMs by competitive inhibition.
Overall, our results show that M6P is capable of reducing TGF-[beta]1-induced fibroblast proliferation and suggest that this is accomplished through competitive inhibition of the M6P/IGF-II receptor of fibroblasts.
You speculate that tryptophan has created competitive inhibition between the tryptophan has created competitive inhibition between the serotonin and dopamine pathways, and you turn to laboratory testing to help restore neurotransmitter balance.
To account for the competitive inhibition effects between chlorophenols and phenol degradation, the specific degradation rate of phenol in the presence of 2-cp or 4-cp is described as (n = 2, 4):
Although competitive inhibition has been considered the primary mechanism through which P and OM interactions increase solution P concentrations (Staunton and Leprince 1996), metal complexation and dissolution reactions (affecting Fe and Al soil oxides) (Lopez-Hernandez et al.
The findings indicate a much more complex mode than competitive inhibition.
However, because 3-DA prevents Hcy production through competitive inhibition of the enzyme S-adenosyl-homocysteine hydrolase (SAHH), 3-DA interferes with popular assays of tHcy that are enzyme-conversion immunoassays based on SAHH (1, 2, 4).
19) Competitive inhibition of signaling proteins and peptides via analogues also holds great promise, and several strategies are being studied.
One assay is a CI-ELISA, short for competitive inhibition enzyme-linked immunosorbent assay.
Biocontrol, also known as competitive inhibition, utilizes nonpathogenic microorganisms to prevent pathogens from growing.
Imetelstat is a lipidated short chain oligonucleotide that binds with high affinity and specificity to the catalytic site of telomerase, resulting in competitive inhibition of enzyme activity.
Moreover, the presence of hydroxyl group at C-2 position of triterpenic acid in MA compared with oleanolic acid could magnify its competitive inhibition on human CYP3A4 activity.

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