Help, please! We did an experiment on enzymes, and it showed that as substrate concentration went up...?
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http://www.biologymad.com/master.html?http://www.biologymad.com/Enzymes/enzymes.htm\n\nhttp://www.tvdsb.on.ca/westmin/science/sbi3a1/digest/enzymes.htm\n\nhttp://www.activescience-gsk.com/miniweb/content/enzymes/how_do.htm\n\nI use these websites with my students...it has some basic enzyme info.\n\nAn enzyme is active only when there is substrate present. So therefore, the rate of activity will increase when thre is "something to do!"
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well... sorry I can't help more specifically with your compounds...\n\n\na co-factor would be something that aids in the enzymatic process\n\na co-subtrate would be something that is required in addition to another subtrate which is ALSO altered by the enzymatic process\n\nThats my understanding of the matter... a substrate is acted upon by the process, whereas a factor is an additional required component but isn't acted on.
380887
lol, last minute lab write ups. afaik enzymes dont change colour, as they are not supposed to change so id bet there is something else that the enzyme works on. better put up the other reagents to get a better answer
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Sounds like somebody is working on a biochem lab. :) \n\nDenaturation lowers enzyme activity because it changes the shape of the protein. Heat disrupts the tertiary structure by breaking covalent, non-covalent and van der waals interations between side chains of the protein. Proteins must be in the right conformation in order to perform their functions correctly. When they are denatured substrates can no longer bind to the active site, key amino acids are no longer in the correct position. \n\npH affects enzyme activity in the following ways: 1-enzyme binding to the active site 2-catalytic activity 3-ionization of the substrate 4-variation of protein structure. This is because pH will change the ionization state of certain side chains. (H+ ions will interact with \n\nOptimum conditions for alpha amylase (ptyalin) from wikipedia.com:\n Optimum pH-5.6 - 6.9\n Room temperatue- 37 degrees Celsius
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I know this! I did a problem like this a while ago! It's an exponential equation. It can be used to predict exponential increases or decreases, like bacteria or double/triple/quadrupled information.
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SURFACE AREA INCREASES\n\nIT'S VICE VERSA
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1. Well, so far as I know enzymes are not changed by their reactions. \n2. There are also special molecules called "substrates" which specifically bind to an enzyme's "active site" (kinda like a key fitting into a hole) and is changed and then released by the enzyme.
1030022
the induced theory states that an enzyme will change shape in order to embrace the substrate
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The effects of temperature may be explained on the basis of kinetic theory - increased temperature increases the speed of molecular movement and thus the chances of molecular collisions, so within a narrow range (often 0-45 °C), the rate of reaction is proportional to the temperature. It is often said that an enzyme's rate of reaction doubles for every10° C rise in temperature. In this respect, the biochemistry of enzymes is similar to chemistry as studied elsewhere, However, the interaction between this positive effect of increased temperature and the negative effect described below results in a different situation, so that enzymes may be said to have an optimum temperature for their action. \n 4 Above normal temperatures (say 60 °C), heat alters irreversibly the enzyme molecule. This denaturation is due to molecular vibrations (caused by heat) which change the shape of the protein, altering the folding and internal cross-linkages in its polypeptide chains. These changes - especially in the region of the active site - mean that the enzyme is inactivated, even when returned to normal temperature. \nIt would be wrong to say that an enzyme is KILLED by heat, since it is only a molecule, not an organism. \nHowever, misconceptions of this sort are easily spread (see the BASC enzymes booklet!) \n\n\n\nThe higher the temperature to which the enzyme is subjected and the longer the heating is continued, the greater the proportion of damaged enzyme molecules and the result is that the conversion process becomes less and less efficient.\n\n\n\n\n\nBelow normal temperatures, enzymes become less and less active, due to reductions in speed of molecular movement, but this is reversible, so enzymes work effectively when returned to normal temperature.
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Enzymes have specificity which means they work on specific substrates. if you add ions to the substrate this will change the substrate slightly enough so that the enzyme will either not work on the substrate or will slow down.
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My guess would be that the larger the particle, the slower the reaction, as the particle would have to achieve an orientation that would fit within the active site of the enzyme, and the larger the particle, the longer it would take for it to orient itself to fit in.
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Well I don't know much about it but look at it this way: what happens normally when starch reacts with amylase? I'm guessing that sugar is produced. If so, I would be willing to bet that when you increase the amount of starch, the rate that sugar is produced increases (enzyme makes contact with starch molecules more frequently, as there is more of it to hit). Of course this will only happen up to a point. Once a certain amount has been added, the amylase will be at its maxium speed of sugar converting, so the speed will stay the same.\n\nI hope this helps, good luck!
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Well, there really isn't one answer to this. You have to think about the function of your enzyme and why it might or might not need multiple substrate/pH combinations.\n\nBear in mind that organisms often have different responses as a result of different stresses. Your enzyme could very well be sensing pH and using that to select a particular cell signalling pathway to deal with a particular stress. \n\nWork it out and you should have a nice paper.
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http://en.wikipedia.org/wiki/Glycolysis\n\nJust scroll down and look at reaction number 8 for the mechanism.
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Peroxidase is a catalyst...catalysts speed up a reaction.\n\nIncreasing surface area of a substrate increases the rate of a reaction. The enzyme can bind on more places of the substrate to catalyze the reaction. The only limiting factor is the amount of enzyme versus the amount of substrate.
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It is more of a regulator enzyme than a catalyst. When there is a high concentration of ATP, the production of pyruvate is low, hence the slowing down of glycolysis (no more energy is needed).
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increased ionic concentration generally means increased acidity which acts the same way as increased temperature on an enzyme causing breakdown of the structure and function.