Answer:
c) Acetyl COA carboxylase; citrate
Explanation:
Citrate serves as an allosteric activator for fatty acid synthesis and diverts the cellular metabolism from the consumption of metabolic fuel to the storage of fuel as fatty acids. When the concentrations of mitochondrial acetyl-CoA and ATP increase, citrate is transported out of mitochondria into the cytosol. In the cytosol, citrate serves as the precursor of cytosolic acetyl-CoA and an allosteric activator of acetyl-CoA carboxylase.
The enzyme Acetyl-CoA carboxylase has three functional regions. Its biotin carboxylase activates CO2 and its transcarboxylase transfers activated CO2 from biotin to acetyl-CoA to produce malonyl-CoA.
Answer:
Polarity
Explanation:
Because of its polarity and ability to form hydrogen bonds, water makes a great solvent, resulting In the feat of dissolving many different kinds of molecules.
Answer: The information suggests that C. difficile is the leading cause of hospital-acquired infections usually as a result of antibiotics use.
Explanation: Antibiotics are employed to inhibit or kill bacteria. When used properly, they target aggressive bacteria that are causing infections. But sometimes healthy gut bacteria are killed in the process (normal healthy gut bacteria helps keep C. difficile in check) creating a vacuum which with increasing frequency, C. difficile seizes, and proliferates — especially in hospitalized patients, many of whom are not so strong to withstand the stress of diarrhea and fever.
Some of these antibiotics that most often lead to C. difficile infections include the quinolones, cephalosporines etc. including some proton-pump medications.
Answer:
Phosphofructokinase-1
Explanation:
Phosphofructokinase-1 catalyzes the phosphorylation of fructose 6-phosphate into fructose 1,6-bisphosphate. The reaction is exergonic with a large negative free energy change to make it essentially irreversible.
Phosphofructokinase-1 is an allosteric enzyme with regulatory sites. Higher ATP concentration serves to inhibit the phosphofructokinase-1 by binding to the allosteric site of the enzyme and thereby reducing its affinity for the substrate (fructose 6 phosphate).
