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What is lock and key?
Lock and Key is one of the theories behind how enzymes fit together with substrates and act as biological catalysts that speed up a reaction in the body. The enzyme usually allows this to happen at much lower temperatures than normal and whithin the range of the animals body. The lock and key refers to the tight specific fitting of the substrate with the enzyme so that specific enzymes can target specific substrates.
What is better more substrates or more enzymes?
Depends on how much substrate the enzyme can process. Most enzymes can process more than one molecule of substrate without denaturing or becoming unusable. However, in the terms of your question. More substrate is better. Too many enzymes would mean the reaction would be cut short, because they would all react the substrate at once. So for a prolonged, efficient reaction more substrate would be proper.
What happens to the rate of enzyme reaction when you increase the enzyme concentration?
As the enzyme concentration increases, the rate of reaction will increase because there are many more enzymes present to aid break down the substrate. However, a point will be reached when no matter how much enzyme is present, the reaction will not occur any quicker. This is equilibrium. This happens because all the substrate is being broken down by the exact same amount of enzyme, so enzymes will be present which have no substrate to break down.
What temperature are most enzymes most effective?
37.5 centigrade. however results are pretty much the same in temperatures between 35 and 40
What is the difference between oceans and lakes?
Lakes are smaller and most are fresh water
What is lock and key?
Lock and Key is one of the theories behind how enzymes fit together with substrates and act as biological catalysts that speed up a reaction in the body. The enzyme usually allows this to happen at much lower temperatures than normal and whithin the range of the animals body. The lock and key refers to the tight specific fitting of the substrate with the enzyme so that specific enzymes can target specific substrates.
STATE the composition of most enzymes?
Enzymes are made of certain combinations of Amino Acids folded into a certain 3-D shape. Most Amino Acids are composed almost entirely of Hydrogen, Oxygen, Carbon and Nitrogen, though sulphur and some other elements are found in much much smaller amounts.
What is better more substrates or more enzymes?
Depends on how much substrate the enzyme can process. Most enzymes can process more than one molecule of substrate without denaturing or becoming unusable. However, in the terms of your question. More substrate is better. Too many enzymes would mean the reaction would be cut short, because they would all react the substrate at once. So for a prolonged, efficient reaction more substrate would be proper.
What is the effect of heat on enzymes?
To a certain point, heat will increase enzyme activity because more collisions will be taking place between the enzyme and substrates. However, if there is too much heat, an enzyme can denature (change its shape) and inactivate. This is caused because the increase in heat disrupts the bonds in the tertiary structure of the enzyme. Due to the disruption of bonds, the enzyme can no longer interact with the substrates.
Why do enzymes only work with the specific substrates?
Enzymes act only on a specific substrate due to the active site of the enzymes fits perfectly with the substrate. Like 2 puzzle pieces, they can only go together and not with anything else. Enzymes catalyze or help a reaction take place. They bind substrates and then help position them in order that the chemical reaction between these substrates can take place. If they bound things other than the substrates they would be much less efficient in catalyzing the reactions.
What are important factors in enzymes structure?
Enzymes are in general globular proteins and range from just 62 amino acid residues in size, for the monomer of 4-oxalocrotonate tautomerase, to over 2,500 residues in the animal fatty acid synthase. A small number of RNA-based biological catalysts exist, with the most common being the ribosome; these are referred to as either RNA-enzymes or ribozymes. The activities of enzymes are determined by their three-dimensional structure.However, although structure does determine function, predicting a novel enzyme's activity just from its structure is a very difficult problem that has not yet been solved. Most enzymes are much larger than the substrates they act on, and only a small portion of the enzyme (around 2-4 amino acids) is directly involved in catalysis. The region that contains these catalytic residues, binds the substrate, and then carries out the reaction is known as the active site. Enzymes can also contain sites that bind cofactors, which are needed for catalysis. Some enzymes also have binding sites for small molecules, which are often direct or indirect products or substrates of the reaction catalyzed. This binding can serve to increase or decrease the enzyme's activity, providing a means for feedback regulation. Like all proteins, enzymes are long, linear chains of amino acids that fold to produce a three-dimensional product. Each unique amino acid sequence produces a specific structure, which has unique properties. Individual protein chains may sometimes group together to form a protein complex. Most enzymes can be denatured-that is, unfolded and inactivated-by heating or chemical denaturants, which disrupt the three-dimensional structure of the protein. Depending on the enzyme, denaturation may be reversible or irreversible. Structures of enzymes with substrates or substrate analogs during a reaction may be obtained using Time resolved crystallography methods.
Does the stomach produce the most enzymes?
Your saliva produces enzymes to break down food and your stomach has them too, but I am pretty sure that your stomach doesn't produce as much as your saliva.
What important factors in enzyme structure?
Enzymes are in general globular proteins and range from just 62 amino acid residues in size, for the monomer of 4-oxalocrotonate tautomerase, to over 2,500 residues in the animal fatty acid synthase. A small number of RNA-based biological catalysts exist, with the most common being the ribosome; these are referred to as either RNA-enzymes or ribozymes. The activities of enzymes are determined by their three-dimensional structure.However, although structure does determine function, predicting a novel enzyme's activity just from its structure is a very difficult problem that has not yet been solved. Most enzymes are much larger than the substrates they act on, and only a small portion of the enzyme (around 2-4 amino acids) is directly involved in catalysis. The region that contains these catalytic residues, binds the substrate, and then carries out the reaction is known as the active site. Enzymes can also contain sites that bind cofactors, which are needed for catalysis. Some enzymes also have binding sites for small molecules, which are often direct or indirect products or substrates of the reaction catalyzed. This binding can serve to increase or decrease the enzyme's activity, providing a means for feedback regulation. Like all proteins, enzymes are long, linear chains of amino acids that fold to produce a three-dimensional product. Each unique amino acid sequence produces a specific structure, which has unique properties. Individual protein chains may sometimes group together to form a protein complex. Most enzymes can be denatured-that is, unfolded and inactivated-by heating or chemical denaturants, which disrupt the three-dimensional structure of the protein. Depending on the enzyme, denaturation may be reversible or irreversible. Structures of enzymes with substrates or substrate analogs during a reaction may be obtained using Time resolved crystallography methods.
What happens to the rate of enzyme reaction when you increase the enzyme concentration?
As the enzyme concentration increases, the rate of reaction will increase because there are many more enzymes present to aid break down the substrate. However, a point will be reached when no matter how much enzyme is present, the reaction will not occur any quicker. This is equilibrium. This happens because all the substrate is being broken down by the exact same amount of enzyme, so enzymes will be present which have no substrate to break down.
How enzyme catalyze chemical reaction?
Enzymes lower the activation energy of a reaction (that is, the amount of energy that is needed in order for the reaction to occur).Without an enzyme, a reaction may need so much energy that it is impossible to obtain in a normal biological timespan. With enzymes, reactions require much less energy, so that they can occur hundreds of times a second.Enzymes can achieve this catalysis in many ways - for instance, if a reaction involves two substances combining to form one, the enzyme can bind each substance in a specific site that forces them close together, making the reaction much more likely to occur and requiring much less energy for the substrates to locate and approach one another.
What temperature are most enzymes most effective?
37.5 centigrade. however results are pretty much the same in temperatures between 35 and 40
Is the non protein part of an enzyme will attach with enzyme after making product?
Enzymes are proteins that catalyze (i.e., increase the rates of) chemical reactions.[1][2] In enzymatic reactions, the molecules at the beginning of the process are called substrates, and the enzyme converts them into different molecules, called the products. Almost all processes in a biological cell need enzymes to occur at significant rates. Since enzymes are selective for their substrates and speed up only a few reactions from among many possibilities, the set of enzymes made in a cell determines which metabolic pathways occur in that cell.Like all catalysts, enzymes work by lowering the activation energy (Ea‡) for a reaction, thus dramatically increasing the rate of the reaction. Most enzyme reaction rates are millions of times faster than those of comparable un-catalyzed reactions. As with all catalysts, enzymes are not consumed by the reactions they catalyze, nor do they alter the equilibrium of these reactions. However, enzymes do differ from most other catalysts by being much more specific. Enzymes are known to catalyze about 4,000 biochemical reactions.[3] A few RNA molecules called ribozymes also catalyze reactions, with an important example being some parts of the ribosome.[4][5] Synthetic molecules called artificial enzymes also display enzyme-like catalysis.[6]Enzyme activity can be affected by other molecules. Inhibitors are molecules that decrease enzyme activity; activators are molecules that increase activity. Many drugs and poisons are enzyme inhibitors. Activity is also affected by temperature, chemical environment (e.g., pH), and the concentration of substrate. Some enzymes are used commercially, for example, in the synthesis of antibiotics. In addition, some household products use enzymes to speed up biochemical reactions (e.g., enzymes in biological washing powders break down protein or fat stains on clothes; enzymes in meat tenderizers break down proteins, making the meat easier to chew).
