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  2. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    Enzyme denaturation is normally linked to temperatures above a species' normal level; as a result, enzymes from bacteria living in volcanic environments such as hot springs are prized by industrial users for their ability to function at high temperatures, allowing enzyme-catalysed reactions to be operated at a very high rate.

  3. Isozyme - Wikipedia

    en.wikipedia.org/wiki/Isozyme

    This definition encompasses (1) enzyme variants that are the product of different genes and thus represent different loci (described as isozymes) and (2) enzymes that are the product of different alleles of the same gene (described as allozymes). [2]

  4. Biochemistry - Wikipedia

    en.wikipedia.org/wiki/Biochemistry

    By lowering the activation energy, the enzyme speeds up that reaction by a rate of 10 11 or more; a reaction that would normally take over 3,000 years to complete spontaneously might take less than a second with an enzyme. The enzyme itself is not used up in the process and is free to catalyze the same reaction with a new set of substrates.

  5. Active site - Wikipedia

    en.wikipedia.org/wiki/Active_site

    Organisation of enzyme structure and lysozyme example. Binding sites in blue, catalytic site in red and peptidoglycan substrate in black. (In biology and biochemistry, the active site is the region of an enzyme where substrate molecules bind and undergo a chemical reaction.

  6. Isomerase - Wikipedia

    en.wikipedia.org/wiki/Isomerase

    The enzyme's active site contains two Asp residues. After the substrate binds to the enzyme, the first Asp deprotonates the third carbon from one side of the molecule. This leaves a planar sp 2-hybridized intermediate. The second Asp is located on the opposite side of the active side and it protonates the molecule, effectively adding a proton ...

  7. List of enzymes - Wikipedia

    en.wikipedia.org/wiki/List_of_enzymes

    Function: Amylase is an enzyme that is responsible for the breaking of the bonds in starches, polysaccharides, and complex carbohydrates to be turned into simple sugars that will be easier to absorb. Clinical Significance: Amylase also has medical history in the use of Pancreatic Enzyme Replacement Therapy (PERT). One of the components is ...

  8. Flavin-containing monooxygenase - Wikipedia

    en.wikipedia.org/wiki/Flavin-containing_mono...

    The general function of these enzymes is to metabolise xenobiotics. [16] Hence, they are considered to be xenobiotic detoxication catalysts . These proteins catalyze the oxygenation of multiple heteroatom -containing compounds that are present in our diet, such as amine -, sulfide -, phosphorus -, and other nucleophilic heteroatom-containing ...

  9. Enzyme activator - Wikipedia

    en.wikipedia.org/wiki/Enzyme_activator

    Enzyme activators are molecules that bind to enzymes and increase their activity. They are the opposite of enzyme inhibitors. These molecules are often involved in the allosteric regulation of enzymes in the control of metabolism. In some cases, when a substrate binds to one catalytic subunit of an enzyme, this can trigger an increase in the ...