The word "allosteric enzyme" refers to a type of enzyme that can change its shape and activity in response to the binding of a small molecule. The pronunciation of this word is /ˌæləˈstɛrɪk ˈɛnzaɪm/, with the stress on the second syllable. The first syllable is pronounced with a short "a" sound, followed by the "l" consonant sound. The second syllable contains the "st" consonant cluster, pronounced with a voiceless "s", followed by the "ɛr" vowel sound. The final two syllables are pronounced with the "aɪ" diphthong and the "m" consonant sound.
An allosteric enzyme is a protein molecule that functions as a catalyst in biological reactions, aiding in the conversion of substrates into products. However, what distinguishes an allosteric enzyme from a regular enzyme is its ability to be regulated by small, non-substrate molecules known as allosteric modulators.
These allosteric modulators bind to specific sites on the allosteric enzyme, known as allosteric sites, which are distinct from the active site where the substrate binds. Upon binding, allosteric modulators cause a conformational change in the enzyme, either enhancing or inhibiting its enzymatic activity. This means that the presence of allosteric modulators can either increase or decrease the enzyme's ability to catalyze the conversion of substrates.
The regulation of allosteric enzymes is often crucial in maintaining the balance of biochemical pathways within cells. By modulating the enzyme's activity, cells can control the rate of specific reactions, preventing excessive buildup or depletion of important metabolites. This type of regulation allows cells to respond to changing conditions and maintain homeostasis.
Furthermore, allosteric enzymes typically display cooperativity, which refers to the phenomenon where the binding of one substrate molecule to an enzyme affects the binding of subsequent substrate molecules. This can result in sigmoidal enzyme kinetic curves, where the rate of reaction initially increases slowly, then rapidly, before eventually leveling off.
In summary, allosteric enzymes are protein catalysts that are regulated by the binding of small molecules to allosteric sites. This regulation allows cells to modulate enzyme activity, ensuring appropriate response and adaptation to cellular needs.
The word "allosteric" is derived from the Greek words "allos" meaning "other" or "different", and "stereos" meaning "solid" or "three-dimensional". The term was first introduced by the British biochemists William Kilgour and Charles Jencks in 1966 to describe a distinct behavior of enzymes.
The word "enzyme" originates from the Greek word "enzymos", which means "leavened". This term was first coined by the German physiologist Wilhelm Kühne in 1878 to describe a substance that promotes chemical reactions without being consumed itself.
Therefore, the word "allosteric enzyme" is a combination of the Greek origin of "allosteric" and the defined term "enzyme", referring to an enzyme that undergoes a change in shape or activity when bound by a molecule other than its substrate at an allosteric site.