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Competitive inhibition

interruption of a chemical pathway when one substance inhibits the effect of another by competing with it for binding or bonding

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Record originEnglish Wikipedia
Text licenseCC BY-SA 4.0
Source revisionMar 29, 2026
Entity authorityQ912894
Source-derived summary

Competitive inhibition is interruption of a chemical pathway owing to one chemical substance inhibiting the effect of another by competing with it for binding or bonding. Any metabolic or chemical messenger system can potentially be affected by this principle, but several classes of competitive inhibition are especially important in biochemistry and medicine, including the competitive form of enzyme inhibition, the competitive form of receptor antagonism, the competitive form of antimetabolite activity, and the competitive form of poisoning (which can include any of the aforementioned types).

Enzyme inhibition type

In competitive inhibition of enzyme catalysis, binding of an inhibitor prevents binding of the target molecule of the enzyme, also known as the substrate. This is accomplished by blocking the binding site of the substrate – the active site – by some means. The Vmax indicates the maximum velocity of the reaction, while the Km is the amount of substrate needed to reach half of the Vmax. Km also plays a part in indicating the tendency of the substrate to bind the enzyme. Competitive inhibition can be overcome by adding more substrate to the reaction, which increases the chances of the enzyme and substrate binding. As a result, competitive inhibition alters only the Km, leaving the Vmax the same. This can be demonstrated using enzyme kinetics plots such as the Michaelis–Menten or the Lineweaver-Burk plot. Once the inhibitor is bound to the enzyme, the slope will be affected, as the Km either increases or decreases from the original Km of the reaction.

Editorial summary

This brief starts where responsible research should: with the source description of “Competitive inhibition” as interruption of a chemical pathway when one substance inhibits the effect of another by competing with it for binding or bonding. Everything that follows is an evidence route, not borrowed authority.

Editorial reviewUseful for establishing the present vocabulary of the subject while preserving a route back to the evidence on which that vocabulary rests. The current 250-word lead offers orientation but no explicit four-digit date, so chronology should not be assumed. The selected authority fields contribute no independent date. The account is most persuasive where Competitive, inhibition and interruption can be independently traced.
Editorial analysis

Why this record matters

The subject matters to the science & nature register because the source frames it as interruption of a chemical pathway when one substance inhibits the effect of another by competing with it for binding or bonding. Its deeper value depends on whether names, dates, institutions and citations support that framing.

Evidence profile

Stable identifiers, scientific names and standards terminology offer the best bridge between this overview and specialist evidence. The source revision retrieved here is dated Mar 29, 2026. The linked authority identifier is Q912894. None of the 0 selected statements returned an explicit reference.

Critical limits

Current terminology should not be projected backward without checking the classification used when the underlying evidence was created. The lead is largely declarative, so disagreement and counter-evidence require a deliberate search beyond the opening account. Authority statements aid reconciliation but still require their own references, qualifiers and ranks to be checked.

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Source & attribution

This entry incorporates text from Competitive inhibition” on English Wikipedia. Contributors are listed in the page history. Text is available under the Creative Commons Attribution-ShareAlike 4.0 License. Selected authority identifiers and statements are retrieved from Wikidata under CC0; their references and qualifiers remain part of the verification path.