Enzyme inhibition

From WikiMD.org
Jump to navigation Jump to search

Enzyme Inhibition

Enzyme inhibition (pronunciation: /ˈɛnzaɪm ɪnˈhɪbɪʃən/) refers to the process where the activity of an enzyme is reduced by a molecule known as an inhibitor. This process is a crucial part of biochemical regulation within organisms.

Etymology

The term 'enzyme inhibition' is derived from the Greek words 'en' (meaning 'in') and 'zyme' (meaning 'leaven'), and the Latin word 'inhibitio' (meaning 'restraining').

Types of Enzyme Inhibition

There are two main types of enzyme inhibition: competitive inhibition and non-competitive inhibition.

  • Competitive inhibition occurs when the inhibitor binds to the same active site as the substrate, preventing the substrate from binding.
  • Non-competitive inhibition occurs when the inhibitor binds to a different site (allosteric site) on the enzyme, changing the shape of the enzyme and preventing the substrate from binding effectively.

Related Terms

  • Substrate: The molecule upon which an enzyme acts.
  • Active site: The region of an enzyme where substrate molecules bind and undergo a chemical reaction.
  • Allosteric site: A site on an enzyme other than the active site, to which a regulatory molecule binds.
  • Biochemical regulation: The control of biochemical pathways in an organism, often involving enzyme inhibition.

See Also

External links

Esculaap.svg

This WikiMD dictionary article is a stub. You can help make it a full article.


Languages: - East Asian 中文, 日本, 한국어, South Asian हिन्दी, Urdu, বাংলা, తెలుగు, தமிழ், ಕನ್ನಡ,
Southeast Asian Indonesian, Vietnamese, Thai, မြန်မာဘာသာ, European español, Deutsch, français, русский, português do Brasil, Italian, polski