By changing the amino acids, you may have also changed the pH of them and enzymes will only work at a certain pH level. This level is different for different enzymes. So the amino acids may well have denatured the enzymes.
That one amino acid could be located in a critical position for the protein to fold properly. In biochemistry, structure is everything. If the amino acid is wrong due to size, polarity or any number of other chemical or physical characteristics, the entire fold can ruin the enzyme. Proteins and enzymes rely on their structure to function.
It will change the function of the enzyme.
An enzyme is a catalyst for chemical reactions. Three variables that can cause an enzyme to lose its ability to function are temperature, pH level and concentration.
There are many possibilities. If the mutations occurs but it does not change the amino acid sequence due to the redundancy (codon degeneracy) of the genetic code, then the mutation is silent and no effect is observed. If the mutation occurs and the amino acid sequence is changed, but the new amino acid has similar properties to the original amino acid (e.g. aspartic acid -> glutamic acid) and the position of the mutation is far away from the active site, then the mutation will likely have minimal effects on the structure and function of the protein. However, if the mutation changes the amino acid sequence such that the new amino acid has a very different property to the original (lysine -> valine) or if the mutation occured close to the acitive site, then it is very likely that the structure and function of the protein will be compromised. Lastly, there is also the marginal chance that the last type of mutation described above actually increases the effectiveness of the protein. Though this is exceedingly rare, it is the driving force behind evolution.
If shape of a protein is changed its function is altered. This might change or stop a particular biochemical pathway in which that enzyme was critical. Specific 3D shape of each protein is very essential for its function. Change in shape of proteins is caused by a mutation in the DNA.
It depends on the role of the amino acid that is altered. One amino acid might be replaced with no measurable effect on the protein's function; replacing another might cause a total loss of function.
So that when the substrate is added, the reaction between the enzyme and the substrate will cause a change in color
Enzymes work best at the optimum pH of 7.0. The addition of sulfuric acid causes the pH to become lower and this deactivating the enzyme. This change in pH can cause the side chains of an amino acid to change in its charge which can result in a change of protein. This can greatly alter the reaction that was to take place.
An enzyme is a catalyst for chemical reactions. Three variables that can cause an enzyme to lose its ability to function are temperature, pH level and concentration.
There are many possibilities. If the mutations occurs but it does not change the amino acid sequence due to the redundancy (codon degeneracy) of the genetic code, then the mutation is silent and no effect is observed. If the mutation occurs and the amino acid sequence is changed, but the new amino acid has similar properties to the original amino acid (e.g. aspartic acid -> glutamic acid) and the position of the mutation is far away from the active site, then the mutation will likely have minimal effects on the structure and function of the protein. However, if the mutation changes the amino acid sequence such that the new amino acid has a very different property to the original (lysine -> valine) or if the mutation occured close to the acitive site, then it is very likely that the structure and function of the protein will be compromised. Lastly, there is also the marginal chance that the last type of mutation described above actually increases the effectiveness of the protein. Though this is exceedingly rare, it is the driving force behind evolution.
Amino acid order is of great importance to a protein's function. Every amino acid has unique chemical properties that affect the function of a protein. In the case of an enzyme, those amino acids in the active site of the protein must be able to properly bond to the substrate, activate it chemically, and possibly put a certain amount of strain on the bonds within the substrate in order to make it more susceptible to a chemical reaction. And in the case of other functional proteins (such as receptors or muscle protein), the amino acids in the bonding site must similarly be of the right type so that bonding of various substrates can cause the right change in the shape of the protein. Additionally, the amino acids in the nonactive areas of the protein must be such that the protein folds properly.
Amino acid order is of great importance to a protein's function. Every amino acid has unique chemical properties that affect the function of a protein. In the case of an enzyme, those amino acids in the active site of the protein must be able to properly bond to the substrate, activate it chemically, and possibly put a certain amount of strain on the bonds within the substrate in order to make it more susceptible to a chemical reaction. And in the case of other functional proteins (such as receptors or muscle protein), the amino acids in the bonding site must similarly be of the right type so that bonding of various substrates can cause the right change in the shape of the protein. Additionally, the amino acids in the nonactive areas of the protein must be such that the protein folds properly.
If shape of a protein is changed its function is altered. This might change or stop a particular biochemical pathway in which that enzyme was critical. Specific 3D shape of each protein is very essential for its function. Change in shape of proteins is caused by a mutation in the DNA.
It depends on the role of the amino acid that is altered. One amino acid might be replaced with no measurable effect on the protein's function; replacing another might cause a total loss of function.
Enymes can change shape when it denatures. An enzyme can denature if it's not at the pH or temperature that it's used to. A denatured enzyme can no longer function (an enzyme's funcion: to speed up/cause chemical reactions fast enough for a living thing to survive).
ENZYMES
The primary function of the enzyme amylase is to break down starches in food so that they can be used by the body. Amylase testing is usually done to determine the cause of sudden abdominal pain.
an enzyme is a complex protein that cause a specific chemical change in other substances, without being changed themselves.
The amino acid sequence is shifted, and this kind of mutation is called a frame shift mutation. All of the amino acid sequence after the mutation will be changed, which will cause a change in shape of the protein, which will then probably result in a nonfunctional protein, since the shape of a protein determines its function.