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Shape of substrate, shape of the enzyme, Competitive, noncompetitive and allosteric inhibitors.
Enzyme will catalyse when the substrate come close enough to interact with enzyme's active site (proximity and orientation). The rate of enzymatic reactions is influenced by the condition such as temperature or pH that favors the chemical environment, and when a co-factor is already bound (not for all enzymes).
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.
Enzymes are biological catalysts. They speed up metabolic reactions in the body but remain chemically unchanged themselves. Enzymes contain an active site. This is a region to which another molecule may bind. This molecule is known as the substrate, and is usually specific to the active site of the particular enzyme, which breaks it down. Substrates will not usually fit into any other active sites other than that of the enzyme it is specified to. This can be explained as a lock and key model, where the lock and key are specific to each other, only, that there are many of the same kinds of lock and key when it come to the enzymes. The higher the temperature, the higher the rate of reaction up to a certain point. This is due to the fact that the particles gain kinetic energy and subsequently move around more vigorously. Thus, the chance of there being a successful collision between the enzyme and substrate molecule increases as reacting particles with collide more frequently with increased kinetic energy. Enzymes have a very specific three-dimensional shape, held together by ionic and hydrogen bonds. If the amino acids are too vigorous in their motion, then, these bonds will brake. Once the bonds have been broken, the enzyme is said to have become denatured. As a result of becoming denatured, the enzymes' rate of activity becomes less because the enzyme loses its specific three-dimensional shape. The enzyme will start to become denatured after around 40ºC as enzyme activity is usually at its optimum at this temperature. After this, the rate of reaction will probably deteriorate. After 60ºC, there is likely to be no reaction, as the enzymes would probably be completely denatured by then.
What is the relationship between substrates and enzymes in a chemical reaction?Enzymes bind with chemical reactants called substrates. There may be one or more substrates for each type of enzyme, depending on the particular chemical reaction. In some reactions, a single-reactant substrate is broken down into multiple products. In others, two substrates may come together to create one larger molecule. Two reactants might also enter a reaction, both become modified, and leave the reaction as two products.The substrate binds to the enzyme at the active site. Since enzymes are proteins, this site is composed of a unique combination of amino acid residues (side chains or R groups). Each amino acid residue can be large or small; weakly acidic or basic; hydrophilic or hydrophobic; and positively-charged, negatively-charged, or neutral. The positions, sequences, structures, and properties of these residues create a very specific chemical environment within the active site. A specific chemical substrate matches this site like a jigsaw puzzle piece and makes the enzyme specific to its substrate.
They come together at the active site
The binding of an enzyme and a substrate forms an enzyme-substrate complex. It lowers the activation energy of a chemical reaction
Shape of substrate, shape of the enzyme, Competitive, noncompetitive and allosteric inhibitors.
Induced fit: is a more recent theory which suggests that the substrate attaches to the enzyme in a relatively accurate fit, then the enzyme moulds around it, then continues the chemically complex reaction. Lock and Key Mechanism: As obvious as the name states, the lock and key model is simply the substrate fitting acutely into the enzyme with no adjustments required to the enzyme. K.G. ;)
Enzyme will catalyse when the substrate come close enough to interact with enzyme's active site (proximity and orientation). The rate of enzymatic reactions is influenced by the condition such as temperature or pH that favors the chemical environment, and when a co-factor is already bound (not for all enzymes).
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.
Enzymes are biological catalysts. They speed up metabolic reactions in the body but remain chemically unchanged themselves. Enzymes contain an active site. This is a region to which another molecule may bind. This molecule is known as the substrate, and is usually specific to the active site of the particular enzyme, which breaks it down. Substrates will not usually fit into any other active sites other than that of the enzyme it is specified to. This can be explained as a lock and key model, where the lock and key are specific to each other, only, that there are many of the same kinds of lock and key when it come to the enzymes. The higher the temperature, the higher the rate of reaction up to a certain point. This is due to the fact that the particles gain kinetic energy and subsequently move around more vigorously. Thus, the chance of there being a successful collision between the enzyme and substrate molecule increases as reacting particles with collide more frequently with increased kinetic energy. Enzymes have a very specific three-dimensional shape, held together by ionic and hydrogen bonds. If the amino acids are too vigorous in their motion, then, these bonds will brake. Once the bonds have been broken, the enzyme is said to have become denatured. As a result of becoming denatured, the enzymes' rate of activity becomes less because the enzyme loses its specific three-dimensional shape. The enzyme will start to become denatured after around 40ºC as enzyme activity is usually at its optimum at this temperature. After this, the rate of reaction will probably deteriorate. After 60ºC, there is likely to be no reaction, as the enzymes would probably be completely denatured by then.
What is the relationship between substrates and enzymes in a chemical reaction?Enzymes bind with chemical reactants called substrates. There may be one or more substrates for each type of enzyme, depending on the particular chemical reaction. In some reactions, a single-reactant substrate is broken down into multiple products. In others, two substrates may come together to create one larger molecule. Two reactants might also enter a reaction, both become modified, and leave the reaction as two products.The substrate binds to the enzyme at the active site. Since enzymes are proteins, this site is composed of a unique combination of amino acid residues (side chains or R groups). Each amino acid residue can be large or small; weakly acidic or basic; hydrophilic or hydrophobic; and positively-charged, negatively-charged, or neutral. The positions, sequences, structures, and properties of these residues create a very specific chemical environment within the active site. A specific chemical substrate matches this site like a jigsaw puzzle piece and makes the enzyme specific to its substrate.
The enzyme complex in the ETC and the H come together to produce H2O: Water.
Reptile mites can come from the reptile its self if it is new or bad substrate that already has mite
Lowering the body temperature would lower the temperature in the cells, this causes the substrates to slow down, in a sense be less hyperactive, thus lowering the chance that the substrate will come in contact with its given enzyme. This will lower the overall Cellular Metabolism
Temperature And Enzyme Activity: Increasing temperature means the molecules gain more kinetic energy and move faster resulting in more chances of successful collisions of enzymes and substrates forming enzyme-substrate molecules.