Review4 -...

Info iconThis preview shows page 1. Sign up to view the full content.

View Full Document Right Arrow Icon
This is the end of the preview. Sign up to access the rest of the document.

Unformatted text preview: The
greater
the
ac*va*on
barrier
for
a
reac*on
 A.  B.  C.  D.  E.  The
slower
the
reac*on
goes
 The
faster
a
reac*on
goes
 The
less
favorable
a
reac*on
is
 A
and
C
 None
of
the
above
 For
alcohol
dehydrogenase,
EtOH
has
a
kcat/Km
=
 10,000
M‐1
s‐1
,
MeOH
has
a
kcat/Km
=
1000
M‐1
s‐1
.
 A.  B.  C.  D.  E.  EtOH
is
a
beJer
substrate
 MeOH
is
a
beJer
substrate
 Need
to
know
the
Km’s
to
decide
 Need
to
know
the
Vmax’s
to
decide
 C
and
D
 The
diffusion
limit
is
 A.  B.  C.  D.  1
M‐1
s‐1

 1000
M‐1
s‐1

 100,000
M‐1
s‐1

 100,000,000
M‐1
s‐1

 The
Michaelis
constant
for
a
substrate
 A.  Can
be
used
to
determine
the
Kd
 B.  Defines
how
well
a
substrate
is
recognized
 C.  Is
the
substrate
concentra*on
at
which
the
enzyme
is
 running
at
0.5
x
Vmax
 D.  All
of
the
above
 E.  None
of
the
above
 In
chymotrypsin,
Ser195
contributes
to
the
rate
 enhancement
via
 A.  B.  C.  D.  Intrinsic
binding
energy
 Acid/base
catalysis
 Covalent
catalysis
 Electrosta*c
catalysis
 In
a
well‐behaved
enzymology
experiment,
substrate
 u*liza*on
is
_______
with
respect
to
*me
 A.  B.  C.  D.  Linear
 Hyperbolic
 Sigmoidal
 Exponen*al
 In
a
serine
protease,
Asp
performs
____
catalysis
 A.  B.  C.  D.  Covalent
 Electrosta*c
 Acid/base
 Intrinsic
binding
 Enzymes
bind
most
*ghtly
to
 A.  B.  C.  D.  Substrate
 Products
 Transi*on
states
 Depends
on
the
enzyme
 The
following
are
all
serine
proteases
 A.  B.  C.  D.  E.  Trypsin
 Chymotrypsin
 Elastase
 A
and
B
 A,
B,
and
C
 The
role
of
the
specificity
pocket
in
a
serine
protease
 is
to

 A.  B.  C.  D.  E.  Provide
electrosta*c
stabiliza*on
 Provide
intrinsic
binding
energy
 Provide
a
substrate
binding
pocket
 B
and
C
above
 A,
B
and
C
above
 At
low
concentra*ons
of
substrate
(compared
to
the
 Km),
doubling
the
substrate
 A.  Doubles
the
apparent
rate
 B.  Makes
the
apparent
rate
go
to
Vmax
 C.  Leaves
the
apparent
rate
unchanged
 Intrinsic
binding
energy
cannot
use:
 A.  B.  C.  D.  Electrosta*c
interac*ons
 Protona*on
of
substrate
 Aroma*c
stacking
 Hydrophobic
interac*ons
 A
rate
constant
of
3
s‐1
could
describe
the
 A.  B.  C.  D.  Specificity
constant
 kcat
 Km
 Insufficient
data
given
 ...
View Full Document

This note was uploaded on 02/25/2010 for the course CHEM 4611 at Colorado.

Ask a homework question - tutors are online