Yes all enzymes have an active site where substance are temporarily bound. All enzymes have shape that may change during catalysis. The active site of an enzyme orients its substrate molecules, thereby promoting interaction of their reactive parts.
The simple answer is yes. However the shape of the active site resemble more the transition molecule then the original substrate.
All this means is the the substrate under goes some conformational change when binding. The active site more resemble the mid point (transition point) of that conformational change.
Yes two substrates can bind to an active site providing the are complementary in shape, size and charge
no
The active site
No, since the reaction reaches a max rate depending on the speed of which the Enzyme bonds to the substrate and the speed at which the enzyme catalyzes the reaction to produce enzyme and product (shown below). E + S --> ES (E - enzyme, S - substrate, P - products) ES --> E + P Thus, if each reaction rate is not equal to each other, the rate of the overall reaction is not only proportional to both the concentration of enzyme and substrate.
A given enzyme works on ONE TYPE of substrate
As the substrate concentration increases, so will the enzyme activity and hence there will be a quick reaction. however, only up to a certain point ( where, if you drew a graph of the reaction, the line will level off ) as all the active sites in the enzyme are occupied and the reaction cannot go any faster. Here more enzymes will be needed to speed up the reaction.
Very basically: * specificity - the better 'fit' the substrate, the higher the rate of catalysis. * temperature - higher temp = more kinetic energy = faster eaction. However, too high and the enzyme becomes irreversibly denatured and will not work at all. (denatured = the folding of the peptide chains are disrupted, meaning that the shape changes and the substrates no longer fit). The temperature at which the reaction occurs at the fastest rate is called the optimum temperature. * pH - enzymes have specific pH that they work best at (the optimum/optimal pH), as pH can also affect the bonds holding the tertiary structure together (especially ionic bonds), denaturing the enzyme. * concentration of enzyme and substrate - rate of reaction is proportional to the enzyme/substrate concentration. However, at a given enzyme concentration, substrate conc is proprtional to rate up to a point when the enzyme becomes saturated and the rate remains constant. * cofactors/coenzymes - some enzymes require interaction with other molecules to show full catalytic activity. * inhibitors - the presence of an inhibitor lowers the rate of catalysis. There are competitive, uncompetitive, non-competitive and mixed inhibitors, they can bind reversibly or irreversibly, at the active site or an allosteric site... That's a very simple, school textbook answer (and I may have forgotten a factor?). For more detail, any biochemistry textbook should be able to help.
The active site
An enzyme will alter its substrate although the specific substrate depends on the enzyme.
Generally in an enzyme-catalyzed reaction, the reactant is called the substrate, which in association with the enzyme forms the product.
One type of substrate
The reason why an enzyme fits a specific substrate is due to its 3rd dimensional shape. Enzymatic competition involves competition among several different available enzymes to combine with a given substrate material.
No, since the reaction reaches a max rate depending on the speed of which the Enzyme bonds to the substrate and the speed at which the enzyme catalyzes the reaction to produce enzyme and product (shown below). E + S --> ES (E - enzyme, S - substrate, P - products) ES --> E + P Thus, if each reaction rate is not equal to each other, the rate of the overall reaction is not only proportional to both the concentration of enzyme and substrate.
The lock is the enzyme and it's active site is where you put the key in. The key is like the substrate that comes and binds to the active site, or the key that fits into the lock.
A given enzyme works on ONE TYPE of substrate
Dunno. But this is pretty cool. But if i search the question, i obvioudly don't know it, so why would i be given an optionto answer it?
As the substrate concentration increases, so will the enzyme activity and hence there will be a quick reaction. however, only up to a certain point ( where, if you drew a graph of the reaction, the line will level off ) as all the active sites in the enzyme are occupied and the reaction cannot go any faster. Here more enzymes will be needed to speed up the reaction.
It means the highest (and best) temperature an enzyme can work until it gets denatured (active site is re-shaped therefore substrate is unable to fit into it anymore). Hope it helped :)
They do so because it is in theiq characteristics to. They are catalysts so they are generally protenious in nature(hence promote growth)or speed up the rate of chemical reactions. Nevertheless,some catalysts slow down Chemical reactions.