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  2. Active site - Wikipedia

    en.wikipedia.org/wiki/Active_site

    The active site consists of amino acid residues that form temporary bonds with the substrate, the binding site, and residues that catalyse a reaction of that substrate, the catalytic site. Although the active site occupies only ~10–20% of the volume of an enzyme, [1]: 19 it is the most important part as it directly catalyzes the chemical ...

  3. Pyruvate dehydrogenase - Wikipedia

    en.wikipedia.org/wiki/Pyruvate_dehydrogenase

    The active site for pyruvate dehydrogenase (image created from ) holds TPP through metal ligation to a magnesium ion (purple sphere) and through hydrogen bonding to amino acids. While over 20 amino acids can be found in the active site, amino acids Tyr 89, Arg 90, Gly 136, Val 138, Asp 167, Gly 168, Ala 169, Asn, 196, and His 263 actually ...

  4. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    Only a small portion of their structure (around 2–4 amino acids) is directly involved in catalysis: the catalytic site. [30] This catalytic site is located next to one or more binding sites where residues orient the substrates. The catalytic site and binding site together compose the enzyme's active site. The remaining majority of the enzyme ...

  5. Heterogeneous catalysis - Wikipedia

    en.wikipedia.org/wiki/Heterogeneous_catalysis

    The adsorption site is not always an active catalyst site, so reactant molecules must migrate across the surface to an active site. At the active site, reactant molecules will react to form product molecule(s) by following a more energetically facile path through catalytic intermediates (see figure to the right).

  6. 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.

  7. Catalytic triad - Wikipedia

    en.wikipedia.org/wiki/Catalytic_triad

    A catalytic triad is a set of three coordinated amino acid residues that can be found in the active site of some enzymes. [ 1 ] [ 2 ] Catalytic triads are most commonly found in hydrolase and transferase enzymes (e.g. proteases , amidases , esterases , acylases , lipases and β-lactamases ).

  8. Aspartate carbamoyltransferase - Wikipedia

    en.wikipedia.org/wiki/Aspartate_carbamoyltransferase

    Aspartate carbamoyltransferase (also known as aspartate transcarbamoylase or ATCase) catalyzes the first step in the pyrimidine biosynthetic pathway (EC 2.1.3.2). [1]In E. coli, the enzyme is a multi-subunit protein complex composed of 12 subunits (300 kDa in total). [2]

  9. Metabolic pathway - Wikipedia

    en.wikipedia.org/wiki/Metabolic_pathway

    In biochemistry, a metabolic pathway is a linked series of chemical reactions occurring within a cell.The reactants, products, and intermediates of an enzymatic reaction are known as metabolites, which are modified by a sequence of chemical reactions catalyzed by enzymes.