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Active site information


Lysozyme displayed as an opaque globular surface with a pronounced cleft which the substrate depicted as a stick diagram snuggly fits into.
Organisation of enzyme structure and lysozyme example. Binding sites in blue, catalytic site in red and peptidoglycan substrate in black. (PDB: 9LYZ​)

In biology and biochemistry, the active site is the region of an enzyme where substrate molecules bind and undergo a chemical reaction. 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 reaction. It usually consists of three to four amino acids, while other amino acids within the protein are required to maintain the tertiary structure of the enzymes.[2]

Each active site is evolved to be optimised to bind a particular substrate and catalyse a particular reaction, resulting in high specificity. This specificity is determined by the arrangement of amino acids within the active site and the structure of the substrates. Sometimes enzymes also need to bind with some cofactors to fulfil their function. The active site is usually a groove or pocket of the enzyme which can be located in a deep tunnel within the enzyme,[3] or between the interfaces of multimeric enzymes. An active site can catalyse a reaction repeatedly as residues are not altered at the end of the reaction (they may change during the reaction, but are regenerated by the end).[4] This process is achieved by lowering the activation energy of the reaction, so more substrates have enough energy to undergo reaction.

  1. ^ Bugg TD (2004). Introduction to Enzyme and Coenzyme Chemistry (PDF) (2nd ed.). Blackwell Publishing Limited. ISBN 9781405114523. Archived from the original (PDF) on 22 March 2018.
  2. ^ Shanmugam S (2009). Enzyme Technology. I K International Publishing House. p. 48. ISBN 9789380026053.
  3. ^ Pravda L, Berka K, Svobodová Vařeková R, et al. (2014). "Anatomy of Enzyme Channels". BMC Bioinformatics. 15 (1): 379. doi:10.1186/s12859-014-0379-x. PMC 4245731. PMID 25403510.
  4. ^ Alberts B (2010). Essential Cell Biology. Garland Science. p. 91. ISBN 9780815341291.

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facilitates a specific chemical reaction by binding the substrate to its active site, a specialized area on the enzyme that accelerates the most difficult...

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make glucose-6-phosphate. Active site residues of hexokinase allow for stabilization of the glucose molecule in the active site and spur the onset of an...

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Mg2+ in the active site of the enzyme involves addition of an "activating" carbon dioxide molecule (CO2) to a lysine in the active site (forming a carbamate)...

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repeating α-β subunits, each coupled pair of subunits has an active site, for a total of 12 active sites. It plays an essential function for survival, neutralizing...

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tissues of the body but are at the highest concentration in the liver. The active site of the aldehyde dehydrogenase enzyme is largely conserved throughout...

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into one of several families based on their active site mechanism. Enzymes that use a metal in the active site are called "metallo-carboxypeptidases" (EC...

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dissociated ions of carbonic acid (i.e. bicarbonate and hydrogen ions). The active site of most carbonic anhydrases contains a zinc ion. They are therefore classified...

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(not shown here) in the active site. The amino acids are shown as wires, and the TPP is in ball and stick form. The active site also aids in the transfer...

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requirement for L-DOPA as cofactor. The two copper atoms within the active site of tyrosinase enzymes interact with dioxygen to form a highly reactive...

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newer class of medication, directly inhibit thrombin by binding to its active site. Recombinant thrombin is available as a powder for reconstitution into...

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while within the active site (e.g. hydrogen bonding or van der Waals forces). Specific and favorable bonding occurs within the active site until the substrate...

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Competitive inhibition

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substrate. This is accomplished by blocking the binding site of the substrate – the active site – by some means. The Vmax indicates the maximum velocity...

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heterogeneous catalyst has active sites, which are the atoms or crystal faces where the substrate actually binds. Active sites are atoms but are often described...

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Eflornithine

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the natural substrate ornithine from accessing the active site (Figure 1). Within the active site of ODC, eflornithine undergoes decarboxylation with...

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Alcohol dehydrogenase

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has two zinc atoms per subunit. One is the active site, which is involved in catalysis. In the active site, the ligands are Cys-46, Cys-174, His-67, and...

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Cre does not form a shared active site between separate subunits and all the residues that contribute to the active site are found on a single subunit...

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Ribosome

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work has shown that there are no ribosomal proteins close to the reaction site for polypeptide synthesis. This suggests that the protein components of ribosomes...

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attack the C-2 cation which will leave behind a fructose molecule. The active-site carboxylate anion will take action to help keep the unequal balance of...

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acetyl-CoA. Pyruvate decarboxylase occurs as a dimer of dimers with two active sites shared between the monomers of each dimer. The enzyme contains a beta-alpha-beta...

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group of the amino acid substrate displaces the ε-amino group of the active-site lysine residue in a process known as transaldimination. The resulting...

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made of seven β subunits that contain three to seven protease active sites. These sites are located on the interior surface of the rings, so that the...

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Hemocyanin

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at the active site. Partial denaturation actually improves hemocyanin's phenol oxidase activity by providing greater access to the active site. Spectroscopy...

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