Unit 2 - BB450 questions with verified
answers A+ rated
A ____________ is an enzyme that cleaves peptide bonds - correct answer ✔✔protease
Serine, aspartic acid, and histidine make up a group
of residues in chymotrypsin known as a
of residues in chymotrypsin known as a - correct answer ✔✔catalytic triad
The ___________ is a specialized location in the
active site of serine proteases that helps to stabilize
active site of serine proteases that helps to stabilize
the negative charge of the otherwise unstable
the negative charge of the otherwise unstable
tetrahedral intermediates. - correct answer ✔✔oxyanion hole
Example of a protease that uses an oxyanion hole - correct answer ✔✔chymotrypsin
Chymotrypsin uses an active site serine to carry out
its chemistry. Name two other categories or major
classes of proteases. - correct answer ✔✔Cytesine protease (papain)
Aspartyl protease (renin)
Enzymes other than chymotrypsin, like trypsin and elastase,
use an active site serine and catalytic triad. Why do their
answers A+ rated
A ____________ is an enzyme that cleaves peptide bonds - correct answer ✔✔protease
Serine, aspartic acid, and histidine make up a group
of residues in chymotrypsin known as a
of residues in chymotrypsin known as a - correct answer ✔✔catalytic triad
The ___________ is a specialized location in the
active site of serine proteases that helps to stabilize
active site of serine proteases that helps to stabilize
the negative charge of the otherwise unstable
the negative charge of the otherwise unstable
tetrahedral intermediates. - correct answer ✔✔oxyanion hole
Example of a protease that uses an oxyanion hole - correct answer ✔✔chymotrypsin
Chymotrypsin uses an active site serine to carry out
its chemistry. Name two other categories or major
classes of proteases. - correct answer ✔✔Cytesine protease (papain)
Aspartyl protease (renin)
Enzymes other than chymotrypsin, like trypsin and elastase,
use an active site serine and catalytic triad. Why do their
