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  2. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    The enzyme then catalyzes the chemical step in the reaction and releases the product. This work was further developed by G. E. Briggs and J. B. S. Haldane, who derived kinetic equations that are still widely used today. [69] Enzyme rates depend on solution conditions and substrate concentration. To find the maximum speed of an enzymatic ...

  3. List of unsolved problems in chemistry - Wikipedia

    en.wikipedia.org/wiki/List_of_unsolved_problems...

    Enzyme kinetics: Why do some enzymes exhibit faster-than-diffusion kinetics? [13] Protein folding problem: Is it possible to predict the secondary, tertiary and quaternary structure of a polypeptide sequence based solely on the sequence and environmental information? Inverse protein-folding problem: Is it possible to design a polypeptide ...

  4. Enzyme catalysis - Wikipedia

    en.wikipedia.org/wiki/Enzyme_catalysis

    Enzyme catalysis is the increase in the rate of a process by an "enzyme", a biological molecule. Most enzymes are proteins, and most such processes are chemical reactions. Within the enzyme, generally catalysis occurs at a localized site, called the active site.

  5. Biological process - Wikipedia

    en.wikipedia.org/wiki/Biological_process

    Biological processes are made of many chemical reactions or other events that are involved in the persistence and transformation of life forms. [1] Regulation of biological processes occurs when any process is modulated in its frequency, rate or extent.

  6. Biochemistry - Wikipedia

    en.wikipedia.org/wiki/Biochemistry

    The enzyme itself is not used up in the process and is free to catalyze the same reaction with a new set of substrates. Using various modifiers, the activity of the enzyme can be regulated, enabling control of the biochemistry of the cell as a whole. The structure of proteins is traditionally described in a hierarchy of four levels.

  7. Biocatalysis - Wikipedia

    en.wikipedia.org/wiki/Biocatalysis

    -Enzymes exhibit extreme selectivity towards their substrates. Typically enzymes display three major types of selectivity: Chemoselectivity: Since the purpose of an enzyme is to act on a single type of functional group, other sensitive functionalities, which would normally react to a certain extent under chemical catalysis, survive. As a result ...

  8. 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 ...

  9. Hydrolase - Wikipedia

    en.wikipedia.org/wiki/Hydrolase

    Hydrolase enzymes are important for the body because they have degradative properties. In lipids, lipases contribute to the breakdown of fats and lipoproteins and other larger molecules into smaller molecules like fatty acids and glycerol. Fatty acids and other small molecules are used for synthesis and as a source of energy. [1]