Question

___________ cuts most pro-proteases into proteases.

___________ cuts most pro-proteases into proteases.

Homework Answers

Answer #1

Active protease cuts most pro-proteases into proteases.

Protease is an enzyme that cuts a protein into smaller pieces. It catalyzes proteolysis the breakdown of proteins into smaller polypeptides or single amino acids. There are many proteases that exist in inactive precursor, that is proprotease forms until another protease clips off part of their structure. This removal of a peptide takes place, where upon they often cleave additional proteases activating other proteases is a recurring one in biology; examples include the complement pathway of the immune system, blood clotting, and digestion of proteins.

Know the answer?
Your Answer:

Post as a guest

Your Name:

What's your source?

Earn Coins

Coins can be redeemed for fabulous gifts.

Not the answer you're looking for?
Ask your own homework help question
Similar Questions
Why it is more difficult to inhibit aspartyl proteases than serine proteases?
Why it is more difficult to inhibit aspartyl proteases than serine proteases?
Compare and contrast serine proteases and aspartic proteases. Not all answers will be used. Serine protease...
Compare and contrast serine proteases and aspartic proteases. Not all answers will be used. Serine protease Both Aspartic protease
1. Proteins are degraded by lipases, proteases, amylases, or DNases? 2. Sugar is broken down by...
1. Proteins are degraded by lipases, proteases, amylases, or DNases? 2. Sugar is broken down by lipases, proteases, amylases, or DNases? 3. Fats are broken down by lipases, proteases, amylases, or DNases? 4. DNA is degraded by lipases, proteases, amylases, or DNases?   5. Carbohydrates are broken down by lipases, proteases, amylases, or DNases?
Explain why proteases are first selected in an inactive state and describe the means by which...
Explain why proteases are first selected in an inactive state and describe the means by which proteases are activated in the stomach and small intestine
Proteolytic enzymes such as trypsin and chymotrypsin are produced by the pancreas. These proteases are very...
Proteolytic enzymes such as trypsin and chymotrypsin are produced by the pancreas. These proteases are very efficient at digesting protein and will even digest tissues. However, there is a mechanism, which activates these enzymes and prevents them from digesting the tissues. What are the mechanisms by which these proteases are activated? ( please give the answer with complete reference)
EDTA is a widely used food preservative. One reason that food spoils is that proteases begin...
EDTA is a widely used food preservative. One reason that food spoils is that proteases begin to break down proteins within the food. Often proteases rely on metal ions to function properly. Hypothesize why EDTA is used as a preservative instead of another ligand such as a monodentate ligand.
A major difficulty in studying the properties of pancreatic serine proteases is that these enzymes are...
A major difficulty in studying the properties of pancreatic serine proteases is that these enzymes are self-digesting. Provide a detailed rationale for the observation that the problem is less severe for solutions of chymotrypsin than it is for solutions of trypsin.
SOC 1111-34 general sociology Chapter 14 Discussion Pro Con Link Look over the Pro/Con debate on...
SOC 1111-34 general sociology Chapter 14 Discussion Pro Con Link Look over the Pro/Con debate on Medicare for All (Universal Healthcare) and identify a talking point form each perspective. What perspective makes the most sense to you?
Compare trump’s tax cuts with Reagan’s and George W. Bush’s cuts in taxes?
Compare trump’s tax cuts with Reagan’s and George W. Bush’s cuts in taxes?
Which of the following statements about the catalytic mechanism of serine proteases is TRUE? a. The...
Which of the following statements about the catalytic mechanism of serine proteases is TRUE? a. The side chain of the catalytic triad aspartate residue directly engages in base catalysis to remove a proton from the side chain of the catalytic triad serine residue. b. Cleavage of peptide bonds by a serine protease is likely to be insensitive to large changes in pH. c. Mutation of the three catalytic triad residues to alanine would have no effect on the rate of...
ADVERTISEMENT
Need Online Homework Help?

Get Answers For Free
Most questions answered within 1 hours.

Ask a Question
ADVERTISEMENT