Answer:
use own words
Explanation:
In competitive inhibition, an inhibitor molecule is similar enough to a substrate that it can bind to the enzyme's active site to stop it from binding to the substrate. ... In noncompetitive inhibition, an inhibitor molecule binds to the enzyme at a location other than the active site (an allosteric site)
hat is the difference between competitive and non competitive inhibition?
The main difference is that in competitive inhibition, the inhibitor binds directly to the active site of the enzyme. ... Competitive inhibition can be overcome by increasing the concentration of the substrate. This cannot occur with non-competitive inhibition.
Answer:
4. I would choose Gel Electrophoresis because you can use it for DNA sequencing, southern blotting or PCR
Answer:
B. ensure the production of GTP in the case of succinyl-CoA
Explanation:
Succinyl CoA like acetyl-CoA has a thioester bond with very negative free energy of hydrolysis. In this reaction, hydrolysis of the thioester bond leads to the formation of phosphoester bond with inorganic phosphate. This phosphate is transferred to histidine residue of the enzyme and this high energy unstable phosphate is finall transferred to GDP resulting in generation of GTP.
Hence the answer is B. ensure the production of GTP in the case of succinyl-CoA.