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  2. Michaelis–Menten kinetics - Wikipedia

    en.wikipedia.org/wiki/Michaelis–Menten_kinetics

    Curve of the Michaelis–Menten equation labelled in accordance with IUBMB recommendations. In biochemistry, Michaelis–Menten kinetics, named after Leonor Michaelis and Maud Menten, is the simplest case of enzyme kinetics, applied to enzyme-catalysed reactions of one substrate and one product.

  3. Diffusion-limited enzyme - Wikipedia

    en.wikipedia.org/wiki/Diffusion-limited_enzyme

    Kinetically perfect enzymes have a specificity constant, k cat /K m, on the order of 10 8 to 10 9 M −1 s −1.The rate of the enzyme-catalysed reaction is limited by diffusion and so the enzyme 'processes' the substrate well before it encounters another molecule.

  4. Kinase - Wikipedia

    en.wikipedia.org/wiki/Kinase

    In biochemistry, a kinase (/ ˈ k aɪ n eɪ s, ˈ k ɪ n eɪ s,-eɪ z /) [2] is an enzyme that catalyzes the transfer of phosphate groups from high-energy, phosphate-donating molecules to specific substrates. This process is known as phosphorylation, where the high-energy ATP molecule donates a phosphate group to the substrate molecule.

  5. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    For example, it is sometimes difficult to discern the origin of an oxygen atom in the final product; since it may have come from water or from part of the substrate. This may be determined by systematically substituting oxygen's stable isotope 18 O into the various molecules that participate in the reaction and checking for the isotope in the ...

  6. Turnover number - Wikipedia

    en.wikipedia.org/wiki/Turnover_number

    In chemistry, the term "turnover number" has two distinct meanings.. In enzymology, the turnover number (k cat) is defined as the limiting number of chemical conversions of substrate molecules per second that a single active site will execute for a given enzyme concentration [E T] for enzymes with two or more active sites. [1]

  7. Biophysical chemistry - Wikipedia

    en.wikipedia.org/wiki/Biophysical_chemistry

    Biophysical chemistry is a physical science that uses the concepts of physics and physical chemistry for the study of biological systems. [1] The most common feature of the research in this subject is to seek an explanation of the various phenomena in biological systems in terms of either the molecules that make up the system or the supra-molecular structure of these systems. [2]

  8. Biochemical engineering - Wikipedia

    en.wikipedia.org/wiki/Biochemical_engineering

    Bioreactor. Biochemical engineering, also known as bioprocess engineering, is a field of study with roots stemming from chemical engineering and biological engineering.It mainly deals with the design, construction, and advancement of unit processes that involve biological organisms (such as fermentation) or organic molecules (often enzymes) and has various applications in areas of interest ...

  9. Binding constant - Wikipedia

    en.wikipedia.org/wiki/Binding_constant

    The binding constant, or affinity constant/association constant, is a special case of the equilibrium constant K, [1] and is the inverse of the dissociation constant. [2] It is associated with the binding and unbinding reaction of receptor (R) and ligand (L) molecules, which is formalized as: