All of these components are reservoirs of carbon. The cycle is usually discussed as four main reservoirs of carbon interconnected by pathways of exchange. The reservoirs are the atmosphere, terrestrial biosphere (usually includes freshwater systems), oceans, and sediments (includes fossil fuels).
The answer is: The <span>exocrine structure that is involved in the digestion of fat is </span>liver.
<span>>The liver plays an vital role in the digestion and processing of proteins, fat and sugar.
</span><span>>The liver plays a significant role in fat digestion as well as the production of fats needed for the function of different organs of the body</span>
First, we need to solve for the common ratio from the data given by using the equation.
a(n) = a(1) r^(n-1)
1024 = 4 r^(9-1)
256 = r^8
r = 256^(1/8)
r = 2
Then, we can find the sum by the expression:
S(n) = a(1) ( 1 - r^n) / 1-r
S(9) = 4 (1 - 2^9) / 1-2
S(9) = 2044
Therefore, the correct answer from the choices listed above is option B.
Answer:
a) The response indicates that a pH below or above this range will most likely cause enolase to denature/change its shape and be less efficient or unable to catalyze the reaction.
b)The response indicates that the appropriate negative control is to measure the reaction rate (at the varying substrate concentrations) without any enzyme present.
c)The response indicated that the enolase has a more stable/functional/correct/normal protein structure at the higher temperature of 55°C than at 37°C because the enzyme is from an organism that is adapted to growth at 55°C.
Explanation:
Enolase catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate during both glycolysis and gluconeogenesis.In bacteria, enolases are highly conserved enzymes and commonly exist as homodimers.
The temperature optimum for enolase catalysis was 80°C, close to the measured thermal stability of the protein which was determined to be 75°C, while the pH optimum for enzyme activity was 6.5. The specific activities of purified enolase determined at 25 and 80°C were 147 and 300 U mg−1 of protein, respectively. Km values for the 2-phosphoglycerate/phosphoenolpyruvate reaction determined at 25 and 80°C were 0.16 and 0.03 mM, respectively. The Km values for Mg2+ binding at these temperatures were 2.5 and 1.9 mM, respectively.
Enolase-1 from Chloroflexus aurantiacus (EnoCa), a thermophilic green non-sulfur bacterium that grows photosynthetically under anaerobic conditions. The biochemical and structural properties of enolase from C. aurantiacus are consistent with this being thermally adapted.
