Enhancers
Active site .
Yes, enzyme structure is important because the active site of an enzyme is specifically shaped to bind to the substrate. This specificity allows only certain substrates to fit into the active site and form an enzyme-substrate complex. The binding of the substrate to the enzyme is crucial for catalyzing the chemical reaction that the enzyme facilitates.
It will only bind with the enzymes active site of the shapes are complimentary and enzymes are very specific
it i called an active site
The binding of an enzyme and a substrate forms an enzyme-substrate complex. It lowers the activation energy of a chemical reaction
Enhancers
Active site .
Yes, enzyme structure is important because the active site of an enzyme is specifically shaped to bind to the substrate. This specificity allows only certain substrates to fit into the active site and form an enzyme-substrate complex. The binding of the substrate to the enzyme is crucial for catalyzing the chemical reaction that the enzyme facilitates.
It will only bind with the enzymes active site of the shapes are complimentary and enzymes are very specific
it i called an active site
After the NADH binds there the binding of pyruvate happens at the enzyme active site.
An enzyme's three dimension shape is important to the binding that occurs between the enzyme itself and its specific substrate, forming the enzyme-substrate complex. In order for the enzyme to create a reaction it is important that the shape of the enzyme binds the substrate to the active site where the chemical reaction occurs. One other thing to consider is the shape that the enzyme takes that allows only its specific substrate to bind and not any other molecule.
enzyme- substrate complex
Binding site is anywhere which something (such as a protein) can bind to. An example would be the upper flanking regions which contain binding sites thattranscription factors bond with during transcription. The active site is more specific to enzymes and refers to the site where the enzyme functions. It is the specific contours of this active site which give the enzyme its specific function (see how enzymes are substrate specific).
Competitive inhibition is where a inhibitor has a structural similarities of a substrate. Due this the inhibitor binds to the active site of the enzyme,where normally substrate binds. This binding of the inhibitor to the enzyme forms a EI complex instead of ES complex and thus inhibiting the catalytic activity of an enzyme. Non competitive inhibition is when inhibitor possessing same structure of substrate binds to the site other than the active site of an enzyme. The substrate binds to the active site of an enzyme. This binding of the inhibitor to the site other than an active site disturbs the normal structure of an enzyme. Thereby, lowering the catalytic activity of an enzyme.
No, diffusion of molecules across a cell membrane is a passive process, not active, and arguably the least complex.