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Chapter 5 -- Part 2: Metabolism
An example of enzymatic specifity can be found at the active site.
The example shows theProtein.
The ability to accelerate a reaction without the AB molecule that gives enough activation energy to react is an enzyme's ability.
The sub Enzymes have specificity for certain things.
A position that increases the probability of reac a specific enzyme may allow it to hydrolyze a peptide bond.
The unique configuration of each enzyme allows it to find the substrate molecule.
Substrate changes shape as they fit together more tightly.
The fate of a compound depends on how the en zymes act on it.
Each reaction will yield a different product because the holenzymes act on different parts of the molecule.
Enzymes are very efficient.
They can make reactions at rates of up to 10 bil per hour under optimum conditions.
The cofactor can be a metal ion, or if it is an organic lion times, it is called a coenzyme.
The reactant acted upon by the enzyme is the molecule that converts to product.
The activation is reduced as 500,000 by the enzyme-substrate complex.
Most of the forms of the enzymes are composed of the same thing.
Cofactors include iron, zinc, magnesium, and calcium.
Apoenzymes must be activated by cofactors.
The major apoenzymes won't function.
Involves with oxidation-reduction reactions.
You have the enzyme and the molecule.
Most trace elements are needed to see later, but living cells may be used in some way to create specific names for dehydrogenase and oxidase enzymes.
As the temperature increases, the rate of most chemical reactions increases.
Some coenzymes act as electron carriers.
Molecules move more slowly at lower temperatures than they do at higher temperatures because they don't have enough energy to cause a reaction.
There are many coenzymes.
35degC and 40degC are derivatives of both compounds.
The breakdown of aprotein involves energy-requiring reactions.
The coenzyme plays an imporidase to lose its ability.
In some cases, denaturation plays a role in the synthesis and breakdown of fats.
If denaturation continues it will lead to the Krebs cycle.
metabolism zyme cannot regain its original properties if it has lost its solubility and coagulates.
Later in the chapter, there can be Enzymes.
Cells are subject to various controls.
There is how active it is if it is above or below the pH value.
There are several factors that influence the activity of an enzyme.
The more important are temperature, pH, and the three-dimensional structure of the medium.
The rate of reaction is catalyzed by the enzyme.
At this point, the reaction rate falls steeply.
The cells stop working.
The active site can get this maximum rate.
When the concentration is high, a competitive inhibitor can do this.
It is similar to this condition in that it has a shape and chemical structure that is similar.
The sub doesn't affect the reaction rate because all active sites are already in the area.
Under normal cellular conditions, competitive inhibitors bind to amino acids in the not saturated with substrate(s).
At any given time, many of the active site, preventing any further interactions with the sub enzyme molecules are inactive for lack of substrate.
The rate of reaction is likely to be influenced by others bind reversibly occupying and leaving concentration.
Increasing the concentration can overcome competitive inhibition.
As active sites become available, more substrate molecule than competitive molecule are available to attach to the active sites.
Breakage of the noncovalent bonds renders the denatured protein nonfunctional.
Altered noncompetitive inhibitor causes allosteric inhibition.
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