-
used in stoichiometric
coenzymes do
or catalytic amount
coenzymes ~
what
they - - -
when to use
·
proteins provide coenzymes
sidechain for substrate
-
many &
are vitamins or are
NAD
*
NADH ( reverse) Vitamin B1 - thiamine TpP but who
3
.
>
- +
recognition formed from vitamins acyl group transfer
general acid/base hydride winvolved in
~ ~ source
metalions reduces carbonyls such as :
(thiamin pyrophosphate)
·
-
ketones TPP
cofactor
·
coenzyme is a
molecule
-
aldehydes ~ decarboxylation of pyruvate
that is an organic -
CA to acety-CoA
to
get
be metal FAD -
> FADH2 (+ reverse) carboxyl
S
cofactor this
gremoving
· can a & release CO2
group
molecule undergo add. to imine
organic pyruvate
-
O
ion or O
It
#In ord transfer
It of emboxylate -n + CO2
-
" + pp
acetaldehyde
reduction a oxidation pyruvate
>
- reduction is addition of is Catalytic
-
-
~ agent
LiAlHy
Ginn
metabolism
NaBHy & nucleophilic catalyst
or
H or
im
removal of Oxygen maker strong glucose >
- 2
Tires~
pyruvate
↳ converted
2 to
3
addition of can't do in solution
~
requires .
ent
a cetyl CoA
biotin-coenzyme
oxidation
-
>
- is kill & S
43-dehydrogenase
will cells coenz
enz
~ for carboxylase
.
.
- .
co-enz ~
spec. O
It
or removal of H2 -
> CO2
.
2 dihydrolipoyl transacetylase
C-COOM is added)
oxygen
CoASH- dihydrolipoyl dehydrogenase
H 3 HN ~H
.
-
NAD--NADH
·
L I POATE
of act CO2
acceptor carrier
.
~
-
> involved in
↓ + PP, Lipoate FAD
↓
In Roxidation
)
oxidative -
decarb .
WXn
~ allows the carboxyl group cook
like pyruvate dehydrogenase to be transferred biotin
~ use NADT-- NADH ~acts as a coenzyme by
CH12
44( ⑦
transferring acyl groups
added
Hi
:
acetyl CoA
To11
M
~ this will be used O
In
O
M n as hydride carboxylate < I
CHz ASCOA
a &
-
V + Hz reduction >
-
biotin GTS
13 -
CA
CH1z CHin CoA mg2
+
wa enzyme will Acetyl malonyl CoA
⑰ I
N know between
oxidized
⑬ I
Ha & Hp in
HCO3 + ATP
form nature's a
protein
· in
bioorganic chemistry , reduced borohydride a
-
cetyl CoA-CoA is thiol
PLP
be added z form equivalent
T ·
H2 ways
dependendent
can in setylated form
in vivo
PLP
1) add "M-S" ,
the H
+ >
-
unless
very
in
unreactive
bonding pocket enzymes Catalyze or
pyridoxal
a 2H)
in presence
of enzyme the following :
phosphase
2) ejt, ej H (giving Ze- Vit B6
PLP
pyridoxine m
a) decarboxylation
# 2
*
Coenzyme O
enzyme ①
PLP is covalenty linked
lysine side
chain
⑦
dehydrogenase
to
FADH 2
NHg WMz
* FAD - >
-
PLP cn
EvLyseNMyFE-LyS
+
derived from riboflavin (vi + B2)
↳ removing H
~
R
E
*
H becomes
CO2 n -
Y
* homoserine
b) racemization ~
inverting Stereochemistry
- -
phosphate
di
dehydrogenase ! # ility protonated
NH
~ acemization
..
FAD ⑦ enzyme G O
FADH2
in most cases
Nh
Of co-enz
50 %
Li reversible
diamine
is
>
-
enzyme is named diimine C = N 50 % R
R
for the reverse reaction -E
c) clearage
catabolism
Hugo
# O
all fatty acids
NM l ge
O
g succinate O
E BH enzyme are even length acyl adenylate
⑦0
H - 11- >
- t
O
don 0xc
dehydrogenase -
Go
I
PLP
FADH2
C-con
+ It
+
I
CH2-cz- - o- -OAd
-
pp ;
B
FAD u r R- Atr R -
>
-
oxidize to form takes
H activate it
fumerate in order to fatty acid G
C= C
toS
to form
form the
double bond oxidation tany CoASH a better LG
rxn
vitamin K CoA O
acyl Amp
Chemistry -ScoA hydrogenase
Mini
ATP c C SCoA
R
CH2 CHz
-
r
-
-
transfer =
-
-
~
formyl ~ &
CoA
needs to Michael FAD
Fatty acyl i
~
protonation enoy/ CoA FADM2
formaldense
hydration
A o
so there R-C SCoA
staggered hydratase
-
d be
B
N formyl - THF M are not 20-next to .
2 Hz0 L-hydroxyacy1CoA
O B
OM 3
ASH
-
O O a
-
R-ch-c2--scon >
-
dehydrogenase
n- - - -
Scot- T
i
-Adt
I It
adding
o- ATP
formyl
-SCoA
·
&
p
o -p p o
Mz
-
o NAD +
-
-
to
NH2
-
group
-
C 2
6
of
-NHe
starting
GAR i O
↓ no on ATP is better Oxidation rxn
-
·
pNA energy storage
transformylase E E
-
>
2002/0H of carbohydrates
~ catabolism
formyl
N"
iI
-
L
+ HF no on vS
A
·
bigger
net charge
rosidase glucose
polysacchride
+ other
ribose-s'-phosphate than ADP G Stagel &
&
O
key intermediate in II H20 Mono ,
ADP
glycinamide the synthesis of purines ·
p- o ATP ROH-RO-P-0Ot ADP Sac ,
·
0 o +
-p
- -
I 2 8
3 3 glucose ->
> pyruvate
-
2-
.
(GAR) I
Stage
no on of
-
decrease
.
overall
Of O net -
1 S
.
in net charge - O
(x2)
H
10 Steps OM
win
H2O will
""transfer
CH2
O
H no
n
Stabilize through
noun
If
19 S
~
-ors[0-p 0 bonding -0-H
-
E
ais
-
o P I
Ron t
-
O H
0
-
-o
H 0 -
H
de -o -H
glucose phosphorylationreceded Gircose-6-phosphate
J
i
PON
i thymidylate ↓& phosphoglucose
Removing -Mille
isomerize
m thymidine
sythesis - CH3 this isomerase
I
↓
or
- 6
6 8 pka
WSN-methylene d proton goes .
attached ATP ,
monophosphate harder
· when 2-phosphate is on
THF
Tmp
h bC . It is
generates Adenylate + Pi Cp frutose-6-phosphate
dump to remove (ppi) d ~ KetoSe
&
deoxyuridine O
o 000-
furanose
monophosphate * to
recycle DHF-
> WSN"-methylene THE Ato En Ro-p-0-Ad +
mechanism je in
DHFR
enolate
dihydrofolate
THE NSN-methylene ↓ 10
fructose 16 , -bisphosphate
-
generate
DHF
>
-
>
- THE aldolase Caldol rxe)
ring
↓
on
On ChopoCretro All
> attach
-
:sivEnz reductase enz
2
phosphate
key
.
enzymes are to ATP
next to acidic proton
↳ use double bond NAPH + H
+
activity within cells t
c = 0
of & attack
to attack one NV -
>
shyceraldehyde-in
-
the At on WSN-methylene DHFR inhibitors are
widely on
antibiotics
i
as
· 3-phosphate
used o Ad
DHAP
-
> use
- off
base to pluck · inhibitors wouldn't
johde (G3P)
acidic proton (to break bond) allow production
of THF -
Mgj
-reduces the neg
.
metal
swing down
>
- - on 0 to make bacteria >
- trimethoprim (f) on ATO will
reject N
by using
Cofactor
0 = C bond
> moves
-
double bond DHFR specific
>
- Su Enz breaks off
S3
malaria-parasite specific ->
pyrimethamine ,
final
programil
products ful
& in humans
"N
↳ methotrexate
+ MP
DHFR
>
- non-specific
inhibitor
>
- cytotoxic (kills
all cells) -> Cancer
therapy
used in stoichiometric
coenzymes do
or catalytic amount
coenzymes ~
what
they - - -
when to use
·
proteins provide coenzymes
sidechain for substrate
-
many &
are vitamins or are
NAD
*
NADH ( reverse) Vitamin B1 - thiamine TpP but who
3
.
>
- +
recognition formed from vitamins acyl group transfer
general acid/base hydride winvolved in
~ ~ source
metalions reduces carbonyls such as :
(thiamin pyrophosphate)
·
-
ketones TPP
cofactor
·
coenzyme is a
molecule
-
aldehydes ~ decarboxylation of pyruvate
that is an organic -
CA to acety-CoA
to
get
be metal FAD -
> FADH2 (+ reverse) carboxyl
S
cofactor this
gremoving
· can a & release CO2
group
molecule undergo add. to imine
organic pyruvate
-
O
ion or O
It
#In ord transfer
It of emboxylate -n + CO2
-
" + pp
acetaldehyde
reduction a oxidation pyruvate
>
- reduction is addition of is Catalytic
-
-
~ agent
LiAlHy
Ginn
metabolism
NaBHy & nucleophilic catalyst
or
H or
im
removal of Oxygen maker strong glucose >
- 2
Tires~
pyruvate
↳ converted
2 to
3
addition of can't do in solution
~
requires .
ent
a cetyl CoA
biotin-coenzyme
oxidation
-
>
- is kill & S
43-dehydrogenase
will cells coenz
enz
~ for carboxylase
.
.
- .
co-enz ~
spec. O
It
or removal of H2 -
> CO2
.
2 dihydrolipoyl transacetylase
C-COOM is added)
oxygen
CoASH- dihydrolipoyl dehydrogenase
H 3 HN ~H
.
-
NAD--NADH
·
L I POATE
of act CO2
acceptor carrier
.
~
-
> involved in
↓ + PP, Lipoate FAD
↓
In Roxidation
)
oxidative -
decarb .
WXn
~ allows the carboxyl group cook
like pyruvate dehydrogenase to be transferred biotin
~ use NADT-- NADH ~acts as a coenzyme by
CH12
44( ⑦
transferring acyl groups
added
Hi
:
acetyl CoA
To11
M
~ this will be used O
In
O
M n as hydride carboxylate < I
CHz ASCOA
a &
-
V + Hz reduction >
-
biotin GTS
13 -
CA
CH1z CHin CoA mg2
+
wa enzyme will Acetyl malonyl CoA
⑰ I
N know between
oxidized
⑬ I
Ha & Hp in
HCO3 + ATP
form nature's a
protein
· in
bioorganic chemistry , reduced borohydride a
-
cetyl CoA-CoA is thiol
PLP
be added z form equivalent
T ·
H2 ways
dependendent
can in setylated form
in vivo
PLP
1) add "M-S" ,
the H
+ >
-
unless
very
in
unreactive
bonding pocket enzymes Catalyze or
pyridoxal
a 2H)
in presence
of enzyme the following :
phosphase
2) ejt, ej H (giving Ze- Vit B6
PLP
pyridoxine m
a) decarboxylation
# 2
*
Coenzyme O
enzyme ①
PLP is covalenty linked
lysine side
chain
⑦
dehydrogenase
to
FADH 2
NHg WMz
* FAD - >
-
PLP cn
EvLyseNMyFE-LyS
+
derived from riboflavin (vi + B2)
↳ removing H
~
R
E
*
H becomes
CO2 n -
Y
* homoserine
b) racemization ~
inverting Stereochemistry
- -
phosphate
di
dehydrogenase ! # ility protonated
NH
~ acemization
..
FAD ⑦ enzyme G O
FADH2
in most cases
Nh
Of co-enz
50 %
Li reversible
diamine
is
>
-
enzyme is named diimine C = N 50 % R
R
for the reverse reaction -E
c) clearage
catabolism
Hugo
# O
all fatty acids
NM l ge
O
g succinate O
E BH enzyme are even length acyl adenylate
⑦0
H - 11- >
- t
O
don 0xc
dehydrogenase -
Go
I
PLP
FADH2
C-con
+ It
+
I
CH2-cz- - o- -OAd
-
pp ;
B
FAD u r R- Atr R -
>
-
oxidize to form takes
H activate it
fumerate in order to fatty acid G
C= C
toS
to form
form the
double bond oxidation tany CoASH a better LG
rxn
vitamin K CoA O
acyl Amp
Chemistry -ScoA hydrogenase
Mini
ATP c C SCoA
R
CH2 CHz
-
r
-
-
transfer =
-
-
~
formyl ~ &
CoA
needs to Michael FAD
Fatty acyl i
~
protonation enoy/ CoA FADM2
formaldense
hydration
A o
so there R-C SCoA
staggered hydratase
-
d be
B
N formyl - THF M are not 20-next to .
2 Hz0 L-hydroxyacy1CoA
O B
OM 3
ASH
-
O O a
-
R-ch-c2--scon >
-
dehydrogenase
n- - - -
Scot- T
i
-Adt
I It
adding
o- ATP
formyl
-SCoA
·
&
p
o -p p o
Mz
-
o NAD +
-
-
to
NH2
-
group
-
C 2
6
of
-NHe
starting
GAR i O
↓ no on ATP is better Oxidation rxn
-
·
pNA energy storage
transformylase E E
-
>
2002/0H of carbohydrates
~ catabolism
formyl
N"
iI
-
L
+ HF no on vS
A
·
bigger
net charge
rosidase glucose
polysacchride
+ other
ribose-s'-phosphate than ADP G Stagel &
&
O
key intermediate in II H20 Mono ,
ADP
glycinamide the synthesis of purines ·
p- o ATP ROH-RO-P-0Ot ADP Sac ,
·
0 o +
-p
- -
I 2 8
3 3 glucose ->
> pyruvate
-
2-
.
(GAR) I
Stage
no on of
-
decrease
.
overall
Of O net -
1 S
.
in net charge - O
(x2)
H
10 Steps OM
win
H2O will
""transfer
CH2
O
H no
n
Stabilize through
noun
If
19 S
~
-ors[0-p 0 bonding -0-H
-
E
ais
-
o P I
Ron t
-
O H
0
-
-o
H 0 -
H
de -o -H
glucose phosphorylationreceded Gircose-6-phosphate
J
i
PON
i thymidylate ↓& phosphoglucose
Removing -Mille
isomerize
m thymidine
sythesis - CH3 this isomerase
I
↓
or
- 6
6 8 pka
WSN-methylene d proton goes .
attached ATP ,
monophosphate harder
· when 2-phosphate is on
THF
Tmp
h bC . It is
generates Adenylate + Pi Cp frutose-6-phosphate
dump to remove (ppi) d ~ KetoSe
&
deoxyuridine O
o 000-
furanose
monophosphate * to
recycle DHF-
> WSN"-methylene THE Ato En Ro-p-0-Ad +
mechanism je in
DHFR
enolate
dihydrofolate
THE NSN-methylene ↓ 10
fructose 16 , -bisphosphate
-
generate
DHF
>
-
>
- THE aldolase Caldol rxe)
ring
↓
on
On ChopoCretro All
> attach
-
:sivEnz reductase enz
2
phosphate
key
.
enzymes are to ATP
next to acidic proton
↳ use double bond NAPH + H
+
activity within cells t
c = 0
of & attack
to attack one NV -
>
shyceraldehyde-in
-
the At on WSN-methylene DHFR inhibitors are
widely on
antibiotics
i
as
· 3-phosphate
used o Ad
DHAP
-
> use
- off
base to pluck · inhibitors wouldn't
johde (G3P)
acidic proton (to break bond) allow production
of THF -
Mgj
-reduces the neg
.
metal
swing down
>
- - on 0 to make bacteria >
- trimethoprim (f) on ATO will
reject N
by using
Cofactor
0 = C bond
> moves
-
double bond DHFR specific
>
- Su Enz breaks off
S3
malaria-parasite specific ->
pyrimethamine ,
final
programil
products ful
& in humans
"N
↳ methotrexate
+ MP
DHFR
>
- non-specific
inhibitor
>
- cytotoxic (kills
all cells) -> Cancer
therapy
