Enzyme: Serine Proteases

What is a protease

an enzyme that hydrolyzes peptide bonds that link amino acids together protein
what are the two general types of proteases
- endoprotease: cleaves specific peptide bonds within the protein
- exoprotease: cleaves only terminal amino acid residue
what are proenzymes (zymogens) and name an example
- an enzyme synthesized initially in an inactive form but are present and ready to react when needed.
- Serine protease
what are the two physiological roles for proenzyme
- digestion of proteins in small intestine
- blood coagulation
what is a chymotrypsin
- a zymogen that catalyzes the hydrolysis of peptide bonds, on the carboxyl side of aromatic chains
- tyr, phe, trp
what are the active sites involved in the catalytic triad
- serine: where substrate binds
- histidine: ability to donate and accept protons
- aspartate: ability to accept protons and is the final link necessary for chymotrypsin action
are all the active sites of chymotrpsin polar/ nonpolar, where are they found on the protein
- polar
- deprotonated
- found on exterior of protein
what are the active sites for trypsin (serine protease)
- lysine
- arginine
what are the active sites of elastase (serine protease)
- alanine
- valine
- threonine

Author

tanyalequang

343027

Card Set

Enzyme: Serine Proteases

Description

enzymes that are involved with serine proteases such as chymotrpsin, trpsin and elastase

Updated

2018-10-17T05:00:00Z

Show Answers