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Which bonds are the last to break when an enzyme is heated 1 disulphide 2 hydrogen 3 hydrophobic interactions 4 ionic?
SandaruRukshalfb4610
disulphide since it is covalent
Wiki User
∙ 11y ago
Anonymous
ionic
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Which enzyme assists in the breakdown of hydrogen peroxide?
manganese dioxide
Which enzyme is responsible to the breakdown of hydrogen peroxide?
Manganese oxide is a catalyst which speeds up the decomposition of hydrogen peroxide.
What enzyme acts on hydrogen peroxide in living organisms?
Catalase Catalase
Why are bubbles produced when hydrogen peroxide reacts with catalase?
oxygen. catalase is an enzyme that breaks hydrogen peroxide down to form water and oxygen.
Which enzyme converts hydrogen peroxide to water and oxygen?
The peroxizome contains catalase, an enzyme which facilitates the decomposition of H2O2 to H2O and O.
How do factors such as temperature and pH affect enzyme activity?
By simply afecting the bonds ( hbonds . ionic bonds and hydrophobic interactions )
Why at the temperature 100C the rate of enzymes activity it is the lowest?
The heat at 100C disrupts the ionic bonds, hydrogen bonds and hydrophobic interactions between structural amino acids that make up the enzyme, causing it to be denatured and a loss of 3D conformation and loss of active site. The active site is no longer complementary in shape to the substrate molecules, hence there is no binding of substrate to enzyme.
Substrate attaches to what of an enzyme?
At the active site. The substrate is held in the active site by "weak interactions" such as hydrogen bonds and ionic bonds.
Why does molecules react with enzyme?
In order to do its work, an enzyme must unite - even if ever so briefly - with at least one of the reactants. In most cases, the forces that hold the enzyme and its substrate are noncovalent, an assortment of hydrogen bonds, ionic interactions and hydrophobic interactions. For more information, click the link on the left. Michaelis and MENTON have proposed a hypothesis called complex hypothesis the enzyme substrate compex is an intermediate or transiet complex and bonds involved H.bond vaner waals force sometimes 2 substrates can bind to an enzyme molecule and such reaction are callad as BISUBSTRATE REACTION.
When a substrate molecule comes in contact with the active site of an enzyme what happens?
Enzymes speed up the rate of reaction by lowering activation energy needed to begin a reaction. They are globular (spherical) proteins and are highly specific, with a shape maintained by hydrogen and ionic bonds, and hydrophobic interactions along the polypeptide chain. So, a substrate with a specific shape that exactly fits the shape of the enzyme's active site bonds to the site with noncovalent bonds, a mixture of ionic and hydrogen bonds. The enzyme will then increase the likelihood of bonding in the substrate molecule or conversely will weaken, stress and finally break bonds so that atoms can be rearranged into a product. An enzyme is NOT changed in a reaction. : )
Enzyme inhibitors disrupt normal interactions between an enzyme and its what?
substrate
How does temperature and pH effect the function of enzyme?
Raising the temperature will denature an enzyme so that it is no longer functional. Lowering the temperature will reduce the rate of the reaction so low as to make it seem non-functional. Altering the pH above or below its optimum pH will also reduce the enzyme's activity, and at extremes the enzyme may be permanently denatured. Here's why:* Proteins fold into particular shapes that are vital for (and determine) their function. * The shape a protein will fold into is determined by its amino acid sequence, since different amino acids have different properties. * Each amino acid has a 'side chain' sticking out of the main polypeptide chain, which will have specific chemical properties capable of forming certain interactions with other amino acids in the protein (as well as with water and other molecules).* It is these intramolecular forces (interactions between different amino acids within a protein) that are responsible for producing and maintaining the shape of the protein. The forces are:* Hydrogen bonds - weak bonds between slightly positively charged hydrogen and slightly negatively charged atoms (such as oxygen). * Electrostatic interactions - weak attractive forces between charged regions of the protein, including only small charges resulting from polar bonds. * Disulphide bridges * Hydrophobic interactions* Hydrophobic interactions are not sufficient to hold a protein in a particular shape, only to pull the protein into a ball to help it fold into the correct shape. * Hydrogen bonds and electrostatic interactions are dependent on interactions between charges. pH is a measure of the concentration of hydrogen ions, which are positively charged. If there were more hydrogen ions in the solution than the protein was designed for, these ions would compete for the interactions holding the protein together, as well as protonating groups that need to be deprotonated to form important intramolecular interactions (eg nitrogen). Equally, if there were too few hydrogen ions in the solution, the same interactions would disrupted by the relatively high concentration of hydroxide (OH) ions, and important protonated groups may become deprotonated.* Increasing the temperature increases the energy of the bonds and atoms in the protein, to the point at which there is enough energy to overcome the force of the intramolecular reactions, resulting in them breaking.* Disruption of the interactions in any case will lead to some of the protein losing its ability to be held in a certain shape, which then reduces it's catalytic activity (as catalytic activity relies on the shape). The loss of activity will be proportional to the extent of the disruptions, which will in turn be proportional to the extent of the change in pH or temperature. * Disulphide bonds would also be reduced (broken) at very low pH, and broken at extremely high temperatures (though other interactions will have already broken and destroyed activity before this temperature/pH is reached). * Therefore, all proteins have a pH and temperature at which they have been designed to work that they will work very well at. The further away from the pH the solution gets, the more of the proteins will be effected by the change, until eventually they are all completely denatured. This concept is similar to the collision theory, in that a small change in pH will reduce activity, but not significantly, because very few of the increased hydrogen/hydroxide ions will actually be competing for the intramolecular interactions at any one time. Typically, a protein will work best at about 40oC and pH 7. The activity approximately halves with every 10oC drop in temperature between 0 and 40. The activity with varying pH resembles a normal distribution curve.
Are enzymes hydrophilic?
Enzymes, being proteins, are made of many amino acids of which some are hydrophobic. These hydrophobic amino acids tend to shun water and fold into the interior of the protein enzyme. Enzymes are in solution so the hydrophobic sections would be away from the solution on the inside and the hydrophillic amino acids would tend to be on the outside of the enzyme. So, is a limited sense, you could say enzymes are hydrophyllic
What is hydrogen peroxidase?
It is an enzyme that breaks down Hydrogen Peroxide.
Substrate attaches to what part of an enzyme?
In the induced-fit model of enzymes, a substrate associates itself with which part of an enzyme?
What enzyme kills hydrogen peroxide?
This enzyme is called peroxidase and it is found in the peroxisome organelle.
Hydrogen is a substrate of the enzyme catalase?
Peroxide
