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11 Cards in this Set

  • Front
  • Back
Name the general catalytic mechanism or process in which binding of substrate
to enzyme promotes structural changes (a different conformation) of either the
enzyme or the substrate, facilitating catalysis.
Induced Fit
Name the general catalytic mechanism or process in which enzyme groups
donate or accept a proton to increase the reaction rate.
General Acid-Base Catalysis
Briefly describe the overall reaction catalyzed by chymotrypsin. (For example, if
it were hexokinase, you could say "transfers a phosphate group from ATP to glucose" or
write "ATP + glucose ® ADP + glucose-6-phosphate".)
HYDROLYSIS OF PEPTIDE BONDS
What type of amino acid residue provides the R group that is the potent
nucleophile generated in the first phase of the chymotrypsin-catalyzed reaction?
Serine
Which of the amino acid R groups below could most reasonably be expected to serve
in the form shown as a general base catalyst?
conjugate base form of His imidazole
The nucleophile in the deacylation half-reaction of the chymotrypsin-catalyzed
reaction is
H2O (OH– )
The "oxyanion hole" in chymotrypsin is an area in the enzyme tertiary structure that
makes an additional hydrogen bond to the oxyanion of the tetrahedral intermediates,
presumably involved in tight transition state binding.
One of the substrates for aspartate transcarbamoylase (ATCase) is the amino acid
aspartate. A plot of Vo vs. [substrate (Asp)] for ATCase is
sigmoid
The 3 amino acid residues in the catalytic triad of serine proteases like
chymotrypsin are serine, aspartate, and ___ .
__histidine (or His, or H)_ .
What is the prosthetic group responsible for O2 binding in hemoglobin and
myoglobin?
___HEME____
What is the general name given to enzymes that catalyze phosphoryl group transfer
between trinucleotides like ATP and another compound (or a protein)?
kinases