[Answer] what kind of bonds are involved in the initial binding of substrates to the active site?

Answer: non covalent bonds
what kind of bonds are involved in the initial binding of substrates to the active site?

In biology the active site is 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 (binding site) and residues that catalyse a reaction of that substrate (catalytic site). Although the active site occupies only ~10–20% of the volume of an enzyme it is the most important part as it dire…

In biology the active site is region of an enzyme where substrate molecules bind and undergo a chemical reaction. The active site consists of amino acid residues that form temporary bond s with the substrate (binding site) and residues that catalyse a reaction of that substrate (catalytic site). Although the active site occupies only ~10–20% of the volume of an enzyme 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. 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 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). This process is achieved by lowering the activation energy of the reaction so more substrates have enough energy to undergo reaction.

Usually an enzyme molecule has only two active sites and the active sites fit with one specific type of substrate. An active site contains a binding site that binds the substrate and orients it for catalysis. The orientation of the substrate and the close proximity between it and the active site is so important that in some cases the enzyme can still function properly even though all other parts are mut…

Usually an enzyme molecule has only two active sites and the active sites fit with one specific type of substrate. An active site contains a binding site that binds the substrate and orients it for catalysis. The orientation of the substrate and the close proximity between it and the active site is so important that in some cases the enzyme can still function properly even though all other parts are mutated and lose function. Initially the interaction between the active site and the substrate is non-covalent and transient. There are four important types of interaction that hold the substrate in a defined orientation and form an enzyme-substrate complex (ES complex): hydrogen bonds van der Waals interactions hydrophobic interactions and electrostatic force interactions. The charge distribution on the substrate and active site must be complementary which means all positive and negative charges must be cancelled out. Otherwise there will be a repulsive force pushing them apart. The active site usually contains non-polar amino acids although sometimes polar amino acids may also occur. The binding of substrate to the binding site requires at least three contact points in order to achieve stereo- regio- and enantioselectivity. For example alcohol dehydrogenase which catalyses the transfer of a hydride ion from ethanol to NAD interacts with the substrate methyl group hydroxyl group and the pro-(R) hydrogen that will be abstracted during the reaction. In order to exert their function enzymes need to assume their correct protein fold (native fold) a…

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