Quiz

Front 1

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.

Back 1

Induced Fit

Front 2

Name the general catalytic mechanism or process in which enzyme groups
donate or accept a proton to increase the reaction rate.

Back 2

General Acid-Base Catalysis

Front 3

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".)

Back 3

HYDROLYSIS OF PEPTIDE BONDS

Front 4

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?

Back 4

Serine

Front 5

Which of the amino acid R groups below could most reasonably be expected to serve
in the form shown as a general base catalyst?

Back 5

conjugate base form of His imidazole

Front 6

The nucleophile in the deacylation half-reaction of the chymotrypsin-catalyzed
reaction is

Back 6

H2O (OH– )

Front 7

The "oxyanion hole" in chymotrypsin is an area in the enzyme tertiary structure that

Back 7

makes an additional hydrogen bond to the oxyanion of the tetrahedral intermediates,
presumably involved in tight transition state binding.

Front 8

One of the substrates for aspartate transcarbamoylase (ATCase) is the amino acid
aspartate. A plot of Vo vs. [substrate (Asp)] for ATCase is

Back 8

sigmoid

Front 9

The 3 amino acid residues in the catalytic triad of serine proteases like
chymotrypsin are serine, aspartate, and ___ .

Back 9

__histidine (or His, or H)_ .

Front 10

What is the prosthetic group responsible for O2 binding in hemoglobin and
myoglobin?

Back 10

___HEME____

Front 11

What is the general name given to enzymes that catalyze phosphoryl group transfer
between trinucleotides like ATP and another compound (or a protein)?

Back 11

kinases