At molecular level, how do acidity break the molecules of an enzyme?
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acidity, radiation, heat, etc. destroy the protein component of enzyme, it's denaturation.
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Proteins function between very narrow pH levels, and, depending on the protein, those levels vary. \nFor instance, the peptidase proteins in your stomach can only function in a pH level of around 2-2.5. That's why your stomach is so acidic.\nBut, on the other hand, the proteins that digest starch in your mouth function in rather neutral-basic pHs (say 5-7).\nIt depends on the molecular structure of the proteing.
742243
Dont you mean how a molecule of glucose releases energy in a cell....any which way you look at it...refer to Kreb's Cycle in your Biology textbook!
199728
Amylase is an enzyme, that is, it is a catalist for the reaction (eases and accelerates it) but does not participate in the reaction itself. Starch is a polysaccharide formed by molecules of glucose, and what happens is that starch breaks down, i.e. the bonds between these glucose molecules are hydrolized (destroyed by addition of water, H2O), resulting in smaller polysaccharids (maltose), disaccharids and eventually single glucoses (monosaccharides). This reaction releases energy, the energy that was previously stored in those chemical bonds during the synthesis of starch; thus, it's exergonic (in fact all breakdown reactions - catabolism- are exergonic/exothermic).
102190
Some enzymes will be destroyed. But most will still work. Remember every enzyme has has an optimum envornment that it works at i.e. temperature and pH. So when it gets to 112 a lot of enzymes are not working at their best to sustain life.
722596
If I remember my biology correction, an enzyme is essentially a protien. Protiens look like tangled up strings of spaghetti (and therefore, so do enzymes). Enzymes work by fitting exactly with another molecule. \n\nA denatured enzyme is an enzyme that has lost it's shape for one reason or another. Once an enzyme has lost its shape, it can no longer take whatever action it usually takes. \n\nEnzymes can be denatured by heat or chemically.\n\nHope that helps!
934354
Enzymes are proteins so when you heat them up they will denaturalize and stop being an enzyme.
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At too low a temp. an enzyme remains inactive.\n\nAt too high a temp. It is killed or ineffective or destroyed.
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it usually creates an acid  like HCl, HF, H2SO4
77658
Chemical digestion is accomplished using enzymes - chemicals that break down the structure of whatever food the amoeba is eating.  Mechanical digestion comes from movement - like chewing - using physical force to break apart the food, but not alter the food's chemical structure (that is what the enzymes do - alter the chemical structure)
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It is a type of inhibition that occurs when a molecule, of roughly the same shape of the substrate, enters the active site of an enzyme.  It blocks the active sight and hence prevents the substrate molecule to enter active site.\n\nThe reaction's rate is decreased as not all enzymes can metabolise the substrates, some of them being blocked by the inhibitor.
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If the Catalyst is inorganic the higher the temp the quicker it works, if the catalyst is organic(enzyme),it will reach a peak of activity,then further temp will destroy the catalyst
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Enzymes are typically large proteins which are structured specifically for the reaction they catalyse. Their size provide sites for action and stability of the overall structure.\n\nTwo identified sites within enzymes are:\n\nThe catalytic site, which is a region within the enzyme involved with catalysis, and the substrate binding site which is the specific area on the enzyme to which reactants called substrates bind to.\n\nThe catalytic site and substrate binding site are often close or overlapping1 and collectively they are called the active site. If the catalytic site is not near the substrate binding site it can move into position once the enzyme is bound to a substrate.\n\nOften enzymes require additional components to become active. These may be:\n\nco-factors - simple cations, or small organic or inorganic molecules that bind loosely to the enzyme,\n\nprosthetic groups – similar to co-factors but more tightly bound to the enzyme, or co-enzymes – which are more complex than co-factors and prosthetic groups, they often act as a second substrate or bind covalently with the enzyme to affect the active site.\n\nThe enzyme must have additional binding sites for the additional components. Enzymes lacking essential additional elements are called apoenzymes, whereas intact active enzymes are called holoenzymes.
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Acidity is a measure of ionization. An acid will dissociate to proton (H+) and the conjugate base (or anion). The more stable the anion is, the stronger the acid. In your example, phenol dissociates to phenoxide anion. This anion is resonance stabilized -ie- the negative charge is spread out from the oxygen to 3 of the ring carbons. In cyclohexanol anion, the charge is not resonance stabilized and the minus charge is firmly placed on the one oxygen atom.
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That all depends on the enzyme. It could denature a protein involved, making the enzyme useless, or it could speed up the enzyme's activity.
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The factors that affect enzyme activity are:pH, temperature, substrate concentration and even enzyme concentration, and inhibitors.\nThere a particular pH at the which the enzyme activity is maximum. This is called the pH optimum of the enzyme.A graph of pH versus enzyme activity shows a bell shape curve.\nThere is a temperature at which the enzyme activity is 100%. If the temperature is increased by 10 degrees Celsius then the enzyme activity becomes doubled. This is called Q10 of the enzyme. Further increase in the temperature lowers enzyme acivity and at higher temperature the activity is lowered further to become nil.\nSubstrate concentration is also important. At lower substrate concentration the enzyme activity is dependent on the substrate but at higher substrate concentration it becomes independent of substrate concentration.\nAt a very low enzyme concentration the enzymes suffer a kind of dilution and become inactivated.\nThere are substances that are called inhibitors.They impede enzyme or block enzyme activity.A competitive inhibitor binds the active site to block enzyme activity. A non-competitive inhibitor binds to enzyme at some other place to cause change in the three-dimensional structure of the enzyme in such a way that the configuration of the active site is changed and in this case the substrate won't fit in nicely to ensure catalysis.
870113
Glucose is broken down into pyravate with a net gain of 2 ATP during glyclolysis, pryravate is broken down into CO2 and acetyl CoA.   acetyl CoA is oxidized in the kerbs cycle or citric acid cycle to for NADH, CO2, FADH2.  NADH passes electrons to the electron transport chain where the electron is passed along a chain of electron acceptors lossing energy each time.  The electron transport chain drives the H+ ions across the membrane of the mitochondria which ends up producing ATP.  Oxygen is the final electron acceptor.  I know thats a lot of info but its not close to all of it. I hope this helps