The active site is part of an enzyme where substrates bind and undergo a chemical reaction.
The shape of the active site is determined by its chemical structure which results from bonding between amino acids in the enzyme molecule.
Enzymatic reactions depend on the concentration of the substrate. Once all active sites become filled, the output of product obviously depends on something else. This could be the pH of the solution, the temperature of the solution, or many other factors. Usually, higher temperature means high kinetic energy (motion) of molecules and faster reaction times. However, too hot of a temperature can denature the enzymes active site. Also, different enzymes work more or less efficiently in different pH levels. Also, the overall affinity for the substrate by the enzyme influences the rate. Inhibitors can also affect rates.
Allosteric (noncompetitive) inhibition results from a change in the shape of the active site when an inhibitor binds to an allosteric site. When this occurs the substrate cannot bind to its active site due to the fact that the active site has changed shape and the substrate no longer fits. Allosteric activation results when the binding of an activator molecule to an allosteric site causes a change in the active site that makes it capable of binding substrate.
The shape of the active site is distorted.
The alteration of an amino acid on a site other than the active site will: change the shape of the protein.
Different Enzymes inhibit in different ways. Some are structural analogue of substrate and they compete the substrate in binding to the enzyme. Some inhibitors bind in the active site and prevent the binding of the enzyme. Some enzymes doesn't bind the active site but they change the active site properties that prevent the efficient binding of the substrate. some time substrate in large quantity may inhibit the enzyme, while other times the product formed may do so.
A permanent change in the shape of an enzyme's active site caused by high temperatures is called denaturation.
Shape of an enzyme specifically shape of its active site determines enzyme specificity .
shape of their active site make them specific for the substrates
The gene sequence determines the codon, which in turn determines the aminoacid, which in turn determines the tridimensional shape on the protein, which in turn determines the shape of the active site, which in turn determines what it'll be catalysing.
Active sites of enzymes (where the substrates fit in) are substrate specific, and are complementary to the shape of the molecule (substrate). In this way, enzymes can only act on a specific substrate, since that is the only shape that it will accommodate in the active site.
Yes all enzymes have an active site where substance are temporarily bound. All enzymes have shape that may change during catalysis. The active site of an enzyme orients its substrate molecules, thereby promoting interaction of their reactive parts.
Denatured refers to the loss of the 'native' active SHAPE of the enzyme - the Active Site included; this also causes the enzymes to lose their functions.
The bind in the active site.
Active site.
The structure of an enzymes and its active site determine which substrates will work for the enzyme. This is called the lock and key method. The active site is the lock and the substrate is the key.
The substrate binds to the active site.
The substrate binds to the active site.