Answer:
you sniff it with ur nose
Answer: (1) Providing an optimized orientation of the substrate.
(2) Decreasing the ∆G in reaction.
(3) Excluding excess water.
Explanation: The active sites of enzymes increase the rate of reaction because they decrease the activation energy of the reaction,and the physical microenvironment provides an optimal orientation of the substrate relative to reactive functional groups while excluding excess solvent,such as water.
Although some active sites may have amino acids that form salt bridges with the amino acids from a substrate,not all do, so this is not a generic strategy of active site microenvironments
*Gotten directly from Quizlet*
Answer:
i think its vestigial, but if not then it is homologous.
hope that hepls!
The Sun provides energy for the plants (producers) to grow. Herbivores (primary consumers) then eat the producers for energy. Any animals that eat the herbivores are considered secondary consumers. As this cycle continues, energy is lost to the environment as heat.
Answer:
Enzymes are influenced by changes in pH. Enzymes are best dynamic at ideal pH. It is the most favorable pH value - where the compound is most dynamic. Above and beneath to this ideal pH influence enzyme action. Accordingly enzyme show catalytic action at ideal pH.
At the point when enzymes are st low or high pH. Hydrogen particles interface with amino corrosive present at dynamic site. In this way changes their state of amino acids, their legitimate direction and influence enzyme movement.
While estimating action of enolase . 2 phospho glyceraldehyde is a substrate for enolase included a response tube. After appropriate in hatching measure of item is estimated (PEP). Proportion of PEP to 2 phospho glyceraldehyde gives thought regarding enzyme action.
For negative control, we will take a response tube, without having any enzyme enolase in it. Along these lines we will ready to preclude any change of 2 phospho glyceraldehyde to PEP without enzyme.
All compound present in our body are adjusted to as per the earth where we are living. In this manner makes us effective in C. aurantiacus ideal temperature for enolase is 55 degrees. So this catalyst will consistently work best at 55 degrees than at 37 degree
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