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To find the maximum speed of an enzymatic reaction, the substrate concentration is increased until a constant rate of product formation is seen. This is shown in the saturation curve on the right. Saturation happens because, as substrate concentration increases, more and more of the free enzyme is converted into the substrate-bound ES complex.
Organisation of enzyme structure and lysozyme example. Binding sites in blue, catalytic site in red and peptidoglycan substrate in black. (In biology and biochemistry, the active site is the region of an enzyme where substrate molecules bind and undergo a chemical reaction.
A navigational box that can be placed at the bottom of articles. Template parameters [Edit template data] Parameter Description Type Status State state The initial visibility of the navbox Suggested values collapsed expanded autocollapse String suggested Template transclusions Transclusion maintenance Check completeness of transclusions The above documentation is transcluded from Template ...
Similarly, another crucial site for the functionality of an enzyme is the active-site, which should also be maintained while enzyme is being attached to a surface for immobilization, it is a must to have a selective method for the attachment of surface/material to not end up with an immobilized, but dysfunctional enzyme. [3]
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To change this template's initial visibility, the |state= parameter may be used: {{Lipid metabolism enzymes | state = collapsed}} will show the template collapsed, i.e. hidden apart from its title bar. {{Lipid metabolism enzymes | state = expanded}} will show the template expanded, i.e. fully visible.