Biochemistry

P 'Yf-qV1~ -, Ajman University of Science a71dTechnology Network Faculty of Pharmacy & Health Sciences Biochemistry / Dentistry (700236) 1st Exam. - Semester 2008-9

k~ Q 1: a Name the followin Compound # 1

I

15

c1- D_ mCl/YfI1

Student!D:

MoM

Compound#3 k",GUI

Compound # 4 If",

/(11-1-

N-{I

B

\~-~' S-uc.rak

c.:. H"l-0 1+

0( - J)-.= (I'

bo fu ra.~

Compound # 8

H,

" ./ oU

,<,:1

z.ol+ ~ofL-rCVYl

Compound # 12 I

r-

Q-'J~ ~

~~

-_.---

,-~1o.P~

"-/

~_,

Compound # 16

oH

ce1£,Jo~

-=SCSi~

b Use the above chemical structures to Com lete the followin table: Compound # I) and Compound # ( ~) are air of imers /'Y\ 0...\'\\1\'; '. ~ V\ c' . . Comp~:)Und/ . and \Compo~d ~ ( q, ) are Pal! antlomers f\ '0",,,-, ~u.Y""w..- \ ~",).> Compoim ) is aKetOhexose

ill

Compo~d

-

. ..-'.

.-\ 0...(

(3 ) is non-reducmg f:,.u

.

{Y\ '" VI V1 D

alc·

.

Compound #

".'

Compound # (

\'

eox sugar

-.

=:-'0.

is an ornc a~,id

~,1-

)

ptSund # (15)

ill

IS:

,

•

IS an(aric

Compound #

ep'v' f'

•

5) Oneof the fimctionsof !,~~ycan;;

is:

~'

~e

source of lactase enzyme is:

~

~.

6?

~

. t7J'L.1Ae...a <;

(;1':-l

Y

;r~~

\to>e

1\v~-'--'<---

rfll\

2.~

0z 7..aA ·t./Y~

(~

~~

structures. -.

(7:::;

-+

N-r'

~.

~A-Y

f!.:::.1-~ _

..... +-. ......F- ..., I:=a

sugar

.....T....

~'.rU-Lt __

\...~

Q 3: Answer the following True o~se. r--) .... ~ .. 1) Glycogen has an a,(1-4/andlh,66-likages .,2 n.lactose the ic bond is f9rmed wi~ II se an .: lucose are anomers '-...... .;:::...'::4J· -e bond in celTulose is a, ~ . .. .q-::: 5) Sucrose is a nonreducing ....F 6) Galactose and mannose are epimers 7) Mannonic has a carboxyl group on C-6 8) Gluc~d F~e are enan!i~mers .... \:;-::' .. .,9) fructose IS a k~ose ~~ . 10) The reduction of glucose wi I produce sorbitol

.... F ....F

_

e globular protein is:

~r--

sucrose ~usin!C~~al

~7'

/l~A

afl uffi 0-/

~-~

Hef/f-!oO

-

1J£!3:f:;) \iiii? LAmf!J

7) Theendprodrn;tof~acto~dig~tioni±ias~ 8) The Eq~Xdrol~s~s.2f

rotein in water is.


~poLAA-'~~ ofam,~ICliSe~yamyJas .. e is:

f

,.\-,

c:l'-.J~V

~1o ~

o:-:~em

4) The end product ofc~digestlOn

' ,(

2) The name of one of the amino acids likely to be found in the outside of the g 3) The name of one of the amino acids likely to be fo~t~tside

acid

r~4'

<.

(-:---..,

fJ:-.~

thebloodgrou@s:

..

g!yco_~id~ bond

c.. t"'-z;>

QeoJuJ

Q 2: Complete the following: l)Theterminalmonosacch~eof

, ~(~

Compound # ( J c..7 ) has an a,1-4 glycosidic bond L- 'm,~ -h> -

sugar

(~L..

n170 ru,,fw"J'l.

0 ) is a

6\ v-;Z:Z 't'·"' ..•.\.c

has an {l,l-6 glycosidic bo.J.ld Compound # ( / / I ~r""' . ~~ '-f Compound # ( LJ-) is an aldopento~e c§) The number of ste

0<

YT9Y

~

Compound # ( r~)

Compound # (

0

I ) is an a

Compound # (.

(57C225

1 )i

#(

Compound # I ) and Compound ~ ( /0 ) ar paIr anome tt)'A """"'I,,. '-, P.l~ Compo un # 3 )has ~, 1-2 lycosidic bond

of glucose .

Give the name of the [o])owing amino acids and classify each as nonpolar, polar with no charge, polar with negative or sitive charge

~,i

.

/1-<:' s=-2.. I,

o

.

-Clf-.

C.

'.:-

.,

~

f1?

i"-c 001

_,

All-! --CI,j-Cc:a/_J 2-

\

( <:-112)

All '

I.,

\

?'

'3

.'\IN

CD:f"~-,

tl7-.JV /c.~tV H

y(;?"~--'(~~:-V~

po {Q)L

/ fIIo C

It Al-c:.H -<::.s::JoH L I

<;H2.~ ~~

(?~~lA/o
r\~

ci

,

11<-AJ -·LH - coo f-f I C. I

H?

~J L..

H 3.

--ntJLitJ. ~ oLtifL--

I,,::;

~

='.~._======.=::==~:::::===-..---~ )(/ \ . Dentistry Study questions - First

Quiz-

In case of sickness, medical report from a government hospital approved by University Physician and Dean o~~entistry ,is re,uired. Exa~ will not be , ,/) repeated. No make-ups ~. pfOv.ef/v-j 0'. ':Slfjh,!;,c.g.,,,,t e~
emU

UJ""\

-t 4- Draw the chemical structure of the following pairs: a) epimers .... / . c) anomer5\.. rel="nofollow"> e) Optical isomers : '+-

l'\

u

b) enantiomers~. d) functional isomers t'


e.- ~ '

L

c

eaoH

",0

~-, ~ l

~

J

(( LYUUfY\.\QC' A

•

0\1

b) uronic acid d) aric acid f) gluconic acid h) galactaric acid j) L-glyceraldehyde /1) deoxyribose

/

Give evidence that glucose is in a ring structure m lvtoJ 1"'0t-o....·h 0'" Draw the structure of a-D-fructofuranose in both Hawoth and Fisher projections ;;:f 10-For each of the following carbohydrates write the s.trnc.~s of the monomer(s) involved and the ~ of the bonds: -Ia) Isomaltose b) amylopectin c) Sucrose Jd) maltose ..e) cellobiose -If) Lactose g) amylose e) glycogen /

.l.

~ ;./"" 1; 9-

11) Calculate the number of ~s :)

/

40

2; ~6 \ 4 L

of a-D-fructofuranose

8 s\-<e.;"loi.s()~

l \)

i\' -.

f .N\-\~ c,

~

H'!c

cM-3

__Q;) Why the number of sterioisomers is different in open and ring structure ~

l'"

l_Alc}.\M.v.~.

'> _ -'".,

~,_.., a) hemiacetal ~l'l c) hemiketal ~. e) formation of a ~lycosidic bond 6- Draw the stnicture of: a) ~nic' .. c) Sugar alcohol e) Sorbitol g) mannitol i) mannuronic acid k) Ribose ..,/Ill) N-acetyl- galactosamine

-

~

5- Draw the structures of the following:

'*

}•.L,tJ

~-

b-

p,~"'\\r..~,

12) Draw the structure of the smallest aldose and ketose and give their names and j mark the asymmetric carbon atom in each. 13) What is meant by a) D- b) a and d) (+) in the compound a-D-(:::JJfructofuranose

;l

"

D~

~Draw

~~~\

~~In

loLy+- ob!- ,'"

~

the equation of hydrolysIs of sucrose usmg chemIcal structures

~'i~JlI~t.

+- a~~~c

IX!..', ..

~"'<>I.l..r

l..

~

\-<.,'\'~\CJ,

~~~drc

15) Draw the structure of O-glycosidic bond and N-glycosidic bond in glycoproteins

l-1 •

5...- 16) Give the structural difference between 0, A, B and AB blood groups /v ....-' _ y--~ e:, ~ f . ,17YFrom the study of :d4~t~' Ui~s_~ennst;Y o:sugar~} __ .. /'different compounds that can be used as natural sweetners for diabetic patients.

•

-'

f·'

Answer the following True or False. IX!. \-G .1) Glycogen has ana, 1-4 and ~,1-6likages ~c.-<4 ....... F. 2) In lactose the glycosidic bond is formed with 9'(of glucose . ....... E 3) L-Glucose and D-glucosi are an-pmefs eJv\.c.'-\A.~\~(Y\..~5 . ...... ~ .4) The bon~ in~ellul~se is a, 1-4 (3 <-lJ.,\C.~~~-,,~ .......f..: 5) Sucrose IS are\iucmg sugar. ni~ r',) l),JG-s~ ......f. 6) Galactose an d mannose are e~ I~C"":::...~e-y-.J ...... f. 7) MannQDlc has a carboxyl ......f: 8) Glucose and Fructose are enantiomers .~ b ~L ';3'\ IJ <:9-<; e . ...... f. 9) fructose is ~ aldMe&ose sug~ kd--v ~ ~)(P--Se • . .. • •. f-: ..•.•• 10) The reductIOn of ~\ ose WIll produce ,Ofbltol

..... f:

c

~.

Q,

~c<_,

u.

1i\C...:>~e.

•• Give the type of bonds (example a, 1-4) and the name of the sugar units involved in the following compounds: =1. Lactose: P II ~q) 8i\Ac.o.::.~T t\ \~c\..o .~~ \ ~~

0

2. Amylose: 3. Cellobiose:

c< li - 4 ) .

,1\ (~

-z.

d\

-t

\A. C. '-"

4. Isomaltose:

0<.

?-

U _c, )

5. Sucrose

r,i.~[I ~- Z.)}

6. Maltose

c< (

8~vtcv.s:..r-

.•

I-

LJ)

'i

-t

"

7. Cellulose

j»- G·

s.c...

) "'t

(J ( I -

4)

C 2)

~'-'\.c.<.>~<.. ) V\.

{YVI. c. .

G

4%~_;

h. -'<-' ,

\ II\. Co

.i-e...

f'

J

J..lcic t ..5
9 f~

,~

'~\

iJ S(

v:..J.-" , cte

fVSqU~l(/ :::::.---

j\'

,

~

2_

Pi (A."J (

S\-~'\(c-h <

co'·"'-fo~.L

ut-

0\.C1l0S~·

(\nY{

~) o --

A V\;\NV,-'\

\()~.

CU

r

I

~().,\\0 ".e. -\-

, 1- -

r-V\{ ~

; y'\ ~

a

eL

CJ.:>\-i l'\Z..

\

c ~

\\-<:::

S' ~ ,

e.()\-~uV\

•

, ,""

/ 2_b~Cd\J",~

.\'I\~~

<:DCY

o\l'j

~.~~~\\

("

~t

f\

~\,'L"~-(..

\",\-~~l~

-

,r

~

DIGESTION OFCARBOHYD TES ~ L What are the rincipa sites :WdfeiWvcarbohydrate digestion ~ ~\\~ 8-\~\lL~-\\'N.... ~'ll\~, 2, What are the e e 'neeo,edfbr degradation of most diet~ carbohydrates P'r;,'-.QI.~ el2J.Q~I\jCo·S3f,.C.~ (CIc'~{Qjt..'-d~lol"e J.,,.~\ c \\~ - cJ> s~cc'" What is the end product oftsa rY8! am las actmg bnefly on Cll"e't if 'J • kept long time in the ~ 1-._ 5. Why we are unable to digest cellulose t:Y--- d-.Y"1l~ ~\r 0(.. l .... l..\ , ~ - ~ \.9Ai~, ' f' 01'\\-\ ~ UI-·.• 6. Be,What is the en d pro d~ct 0, sahvary amylas acting on amylopectin and. lyco en Wli Carbohydrate digestion ts temorarily in th stomacFi 7. Where Further digestion of carboh drlites occurs ~ ~ \,C>.lo' ~'t:., jll.-~ 8 Why the procesS of starc~ digestion continGS ilit'he small intestine :J '\~\e,.y.J.i1\.{; 9. Wnere The fipal; ~gestive processes of disaccharides occur 10. How the e~es aisacc aridases are secreted \ 11. Where thebulk of the dietary sugars is ,absorbed J. ~o'~ & Vf(2& \J.D U I.MII IIV\ 12. What are the possi?le ause O.f-I estive enzyme deficien~ies~ ~'<>-_ ilA.~SL;\l(lll\~Q.re I' . List events associated With Lactose mtolerance ~ ~\..~. 1

,

\

j

--

What is the~eaSJfo~ Lactose lntoler?nce How do you diagnose, for the deficiency of a specific ~ enz~e_

i~

Chapter ~ ~~ ~ _ Amino acids study the overview of the chapter and you should be able to list the _ in the ~iologi~al system. . 1- You need to recognize all ammo aCids and to be able to clasSIfy each amino acid as non-polar, polar without charge, polar with charge ( - or +). 2- Know how to write the structure of one example from each class. 3- Know which amino acids are located on the surface and interior of proteins soluble in water and in the case of membrane proteins (Fig. f4). 4- Know how to compare between imino group of proline and amino groups of other amino acids (Fig. 1.5)' ./" 5- Know how to form a hydrogen b?nd between phenolic hydroxyl group and another teriary /7~" , , 6- Know the structure of sul:fi!ydyl group of cysteine all i hew te feRB ~ S eeBd ~y the QKigatigQ e+-2 e)steiftes t8 feHB eys~iRi, (gi;ve ~l:Nshgcm feaelt). ' . 7- Know the structure of the amide group in glutamine and aspargine 8- Know how to write D & L enantiomers of amino acids

J . H 10 H

;1] ~' ~,d),l ~

Q 1: Give the coIn lete ·~ameof the folio· . ( J)

'().)

Q

tLOt/

yL~

c- .

H

C). (6} '.

\

CIj)

g: Name the following amino acids a classify each one as non-polar, ::>Iarwith charge, polar with negatj e charge and polar with positive

no

:large

~HZ.-rCH-COO-

~HS CH~-CH

\

\

NH,·

coo-

LH,+ c~:::.\<:.-\\'\.e.-

,r.' \

c \ 0 --;rcii-z. -~H -c.o6'- ~ Jvt~~

:d

pl-o p~Y\.

Lc:'J

4 j' vtl~1J

rite the names of the following amiD. _ _ cA~ J. po lo---'1... L-U~_:t.f,.. '1i.c\ ~--'L) r-.r-) ~-€-)

_

/

~

-coo 1

~

+.

•.. CH-COO-

\

NH)+

.

5:eppy'l-ne .. ,

I)nd~,,"1.v fJ

J

.

cids lcu1-

~ W'l

8~v-e- ~. /""k.(-)

~Jy~d\i~.~6n-

etuv~e.. ~Pc.lo...h __/"Ul;U",

H I-CH-COO-

\

NH)+

H)C-S-CHz-CH

2

CH-COO-

I

NH) +

\I ,- CH,~lH-COO-. H1N-C-CH

-

H1N-C-CH; '-

."

CH-COO-

\

0

NH·+ •

I . /'~- /-C(-coo-

ti)N+ -CHz-CH-CH O·

H H

o

.

\\

'l+_N-C-e-oH \

6

.

I'

Od

. \l~

O''J''"- I J

yTJ

OH

I.

j'\

NH)+

NH 3 +

~

<-("'\0

'\

~~y I

~ll-L)

j

llA.L0.5.C

" +

-t-V..•.c.. \-'6(..-

I

~\A~ (3

t

i -i.1)

?I

<1 cllc\.c..k.:,

c

-/0

\v....c--->";' C

-: -*.

d rex

l, s+ ~ct y-bO~j

//

(j)

@ ~.3 l;;V

*G

iV~

0- s\~ "'~;

"-"-"'\-

tJllUJ ~ \

ex..\t\

~'r\l"-U 0'"

st rdJt

S-\;,~-VC\-U\f'ot

//1

oev-

Q.Q.

oJ" cqL

~~ "St~m :

;"oS±--"~«ht",,,,, .

6013 '

~'1J~ (

VLol

d"

u dit:J

a\-'dO\!rl\<:)~~

.~"r\aJfl~

G~

\:0 Uow I

-\-h ~

c>t

.'hcli.l- ~

eJzIIfj,j

,,~

G\>v\?
ex ~~ 'fA. ~

l' h +ht::.bi

'h<2f\dA '5

m €.-

~

~

t'hC

1.

.#

Bact, (elllJjtt~·

-\--v~AJ c.J-\J V'~):

c~

--------

I

81~ ce~~ deJ'lj'_d~ fA ..••.

Aldo pe.Vt-JQ~~

c "",-l

0

'

Q

.H

0

H

~

S~E'. ~

01-1

i

A lda hex QP~ rQU'lGS~

C -

c I--t 2. () H

cite

e-J''''

~l:GI4 ''~- c '.1-

rib

H -

l-

I

C Hz..

1+

\...81~coP~~cU'\ose. I

04Cft'20

H

I

C::=a

c\t

'2..0

H·

D~~\h e.:

~

\

-

\

"1G

\'Y\ G

f t 8 "S, ~ 0

cc

h ciIr\ d. €. (tM.

-j ~l~~ 'S ~ l ~s\d ll-e..

~Q\.~

". 0..re. ~c

': \uJ-1l\~lj ~i5'

\JO ~ \"\c

<s

<3\

~\~

'Sa.C

\~

c:.:~'-J..t -' ~\:Q. N-IA

c..\-o.rt ck J

k+ ~ ~

"'S~~~

\-

'S~c~

~\'Il,Jd

re

tr""cl.~(o~

{Q

~:1C>

~jluc.rI'c

CU2G#

N- aceJ3'-

3 OlIOlC+-os

c==o

\ c~~

c:x~\'Vl~

i *JG\\j~ ~'S\d~!r\c~ becd-\JSE:

\\~ 0 ~

ca(~C9S~

WlAI..Wt

•

~ w~ t~~~c~\\

\-\\L <~::J.~\j ~-\~V"'~

*cH2.o~\~h~1r l-l ,

c::.o

C H 'LoH

IS

\\f\

rowie"" .

Q

\f'\\AJ

~\--\nIJ~-\-\l\r~,

I So ""'-d \ +os. e : ~ 'U Csl se + d' \I CbS ~ ~/~-

~~)~,6~ .. ,

I

~~cro$e

~\

q ~'?

I

J, ~JroXJ ~ns r)

\,


Gv- bo

Q]0~oL>r

G\. -

D-

0(

'\ S

C+) ~

+- ~

fu - 6)

t~

- ~'r VC+o.\l\f~1A cL\r-ec\ I

D ~

-t. .

\"NLCU/,-

.

lJ)I...

'S.\-

~cV'

0

<:.~

0

0

\+

~i.JY\.

S

\~\'

\1

\~

t'\

PJL.P'r'JL

~

t

h.cl S

OJ'\

d

h


k ~'\

il \+-) ~~ 4~e

~(?lJ~

S~

'---.-/ J

0(

",,$;1~"'"

M~

Cl

l+(\~~tr~

S ~

r~r-",~,<-~~~ !'

1M..~

?-e ) \ t- t ~

CO\Jr '" G lI\

\~

CJ"'9'\.Vy. __ ,

\. \ U\

cLVJV\.

~I}

,,~,iJ d '<;;(\.-~_ •

\ 6)

b reA VJ -\\'\iL ~~\) ~\) N-

3 l~ G '?:ll'cl; ,

C

boVt d

\r-'~

i'~

L N_~l~

(J)'!oiJ.i

~w.

0 _')A)

1(;,

I '-((-'C

(~

y•• ' , .,.

8

It

fk

'bo~cl.). Ae b&,cd

~19'

\\.....,...--

r' I.,.,

.,

Ajman University of Science and Technology Network Faculty of Pharmacy & Heath Sciences Fi rst Exam BiochemistrylDentistry - (700236) 151 Semester 2007-8

:&tltel

~~~_~~~_~~~ ~_e_:_

JjQft{(:LL~

~~~~~~_t_~~ ~~

_

Q 1: Name the following Carbohydrates:

~~

C\-hdJl-

80 rb

,~ioI J

&~ fOil

{

IP'

COOl..(

~ooH

::'

/l V\

lAt.i!{P

"CJ"

A..-0 n \..0 ~-

n

1

,4

\

F(L'(O?LlC

v/

lt~.

X

UCA.

r

cl

I

o..u'c! I

. I !

i

I --~---------~-------~_

__

1

@- The

function of carbohydrates

etttwJY

(V The glycosidic

(~s

in the ~t

is: ~

o~~

~'a

ir(§nyJopectii1)are:

~, 1-4 ~ ~-G, J ---

@The

glycosidic bond in@lulQS"? is:

(3, ,

(§) The

-l+

complete digestion of amyl os with amylase \vi II produce:: ,~'{-CT~lO-

@ in galacwronic

the carboxylic group is on carbon #: 2

0

rnal-toge

Q 3: a) DraW the chemical structural of the following carbohydrates:

a-N-acetylglucosamine

~~~.-= ~

r

~~

C ~+f-

SL~c)~ 10-l-l- 3..

Mannuronic acid ---

C

(!)

0

.~

~l~/I

1-1

_

Enzvmes ~- .i

Give rea~on (8) " 1. ~Yelin~off of the,rWrla I Onrate \IIbs r- a.:r-e. 'Q r. ~ ,QtI~suhs!ra~, -"5\ I'l

I

.

fL' (\

.

'01

coneentratlOnsx& \e.cJ-s--\-h e <scJ-\A ,cJ ,0 _ ~ \ I -'lol t> ,.rpS 0 o4+j c., -e t:l"2.-~me.... t"y)0 \. '(.uJe..qD~~ 2. e rea hon velOCl mcreases 1 empera urelmtl1 a-peak velOcIty IS .reached and furth%~elf~n Q.:tthe ~m~~;tum~s~ ~,. ~r~se }~~!i.0E .¥~ociry .£3.s~xtt~mes ofij:If¥an leatl to aecrease or CtsSitt1b1I,orenZY~111creaetlO~~PI he '- l\

~~t.;t~6\ ~~1~2-~

,

~e yYl'

r t:llll S'L. ~Y\..e.. ~\-r

'€.- \~V\

o~

IAL t\-U't:....

'Ie.... C-"'~mlL\--.er o~

..fh e.-

~'d

4-h'€..0IY!"\

now The following rJ.JV\ Enzymes are highly ~

h

V\oCILid

L .. ~.'.. . v'v-€..J ~ '\0 \-e b Icle-ChO\.\Y\s ,

I ()

yY) 0 ~ u.J.

e.cle.-p etldl

OSCI\

.... _.... __ "~

and i .. ·thspecifi?SiiQ.strates"'-the- • Enzyme a al zes" ne type of ch .on. -z..,~Y\')t-.. A plot of reactIOn ve .QE~ (vO; against subst"rat€ncentrati§0 [S], has (hyp~ ~~

slIaj5e'J

>

.--------

------

~losteric enzymes frequently show sigmoidal urve similar in shape • Th;-MichaeHs:::NIenten equa ion escn how reaction velocity varies with substrate ~ \n\ ------.concentrati~ __ • The Mi~~~~l~~§starlBs characteristic of an_~--_..... -e-a-n-d-a-p-art-i-cu-l-ar-su-b-s-t-ra-0• The Michaelis constant reflects the affinity of the enzyme for that substrate. -~------. • Kmis"numerically equal to the s~bstrate concentration at which the reaction velocity is equal to Vmax. • Km does no v with the concentration of enzyme. • X"numerically small {to reflects a ig a Illi • tar e : A numerically large (hig .. a low aftini _.-------sustrate • The rate of the reaction is directly proportional to the eJ;gyme concentration at all substr.].kconcentr"atiQ..us. --• Noncompetitive inhibitio~s "Yl1eJl!~einhibitor a~QJ;E..!?~tr'!te bindat different sites .........

~n *~~e:~~:;etitive i~~~or_~~b;D~lth~ en~~'-~~£]iS~~~~~~~~\therebY preven.tiniilie-reactlon..liilIIloeeming -...• -N~ompe!itiv~ __inhibit~~ cannot be overcome b . cre_asin~!~ con_~Etration of substrate. Thus, noncompetItIve 1 .. ltors decreas~ th ax 0 ~ --- -,---• ---N~~competiiiY~jIJ.hibif()rsd.6 nOi-inte..rfere with the binding gi§~bs~rate to enzyme. Thus, the enzyfu..... cshows the sameKminJ@ presence or absence of!he ~Q.t:l~ompetitiveillhffi"itor. E~zYn;einhibit€!~~_asdrug~ -... -- . .. • lactam antibiotics such au>enicmiE-and amox~act by inhibitin one or more 0 the enzymes 0 acte' al eel all s thes' s. --== --- ~. DrugS_mayalSO ad-oy ---iIili.IbItmge,~!..rClc~lUlar~reactloIfs:-l11~is-lTlijSIrnfed=bY---- ...-.-..------.~ angiotensin-conve!!ing enzyme (ACE) inhibitofsJhat JQ~~r~l??~2!ess!!re by blocking the enzyme that cleaves angiotensin I to form the potent vCl~()~<:>l!s!riC:!QI:,_an.giotensinJl. • Theseclrugs,wIiich include captopril, enalapril, and lisinoPIiJ._s::aus~_Y..aSilililC:l:!i.Q~Ll:I11d a 2 resultaiiired.uction-iiiblo-oa-pre-ssure. . ---~-----_.~,._ ~_.-...

.. ..

REGULATION OF ENZYME ACTIVITY • CBlc:hang~.s_msubs!t:.'!t..~_C:QI}.C:~~ • Covalent modification: Phosphorylation-dephosphorylation • Altered rates of ~nzyme synthesis whenl'hysi.QlQgicc;~ditions are ~~ge~l. • Effectors that inhibIt enzYII!~activity ar~JeI'!!!edn~gat~'y¢effecto.r:s, • wh~r~~sth~se that.._--.--_.---------_ increa~~enzyme activity ar~~i:;tiledp9~!!iY~_df~~tors. -----,... ,_ ..--,-"----_ .._... _-----_._-_ ... __ ._-~~-_.----._-... _--,,=..-.::---

• Allosteric enzymes usually contain multiple subunits and frequently catalyze the committed step e-arl-y-ln a-pathway. • Most often an allosteric substrate functions as a positive effector. In such a case the presence of a substrate molecule at one site on the enzyme enhances the catalytic properties of the other substrate-binding sites-that is, their sites exhibit cooperativity. • These enzymes show a sigmoidal curve when reaction velocity (Vo) is plotted against substrate concentration, [S]. • Feedback inhibition serves to coordinate the flow of substrate molecules through a series of reactions with the needs of the cell for the product of that particular pathway. • Regulation of enzymes by covalent modification --• Many enzymes may be regulated by covalent modification, most frequently by the ):,i .. • The presence of elevated enzyme activity in the plasma may indicate tissue damage accompanied by increased release of intracellular enzymes. [Note: Plasma is the fluid, noncellular part of blood. Laborat()ry assays of enzyme activity most often use serum, which is obtained by centrifugation of whole blood after it has been allowed to coagulate. ~.j

Alteration

of plasma

oi.\~.~f.-Jv...,,:,~

enzyme levels in disease diagnosis

-:..~~if.;ib..~-' ye-_

~""-

0...

The lack of tissue specificity limits the diagnostic value of many plasma enzymes. ~:~~~ Many isoenzymes contain different subunits in various combinations. -:::. '\ l~ ~,-~::5 . The appearance of the hybrid isoenzyme, CK2, in plasma is virtually specific for infarction of the myocardium. Following an acute myocardial infarction, CK2 isoenzyme appears in plasma approximately 4 to 8 hours following onset of chest pain, and reaches a peak in activity at approximately 24 hours. Troponin concentration is also elevated in plasma following an infarction, eakint~ 3 . L. ,It- ~ e '" k-.p~ 'l ' r1C\chVO'J1D"\ days after the onset 0 f symptoms. ~ I ~ r rj f' n.\.W''\l- J ~ 'L i I.A r'\.e' ~

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Answer the followlllg uestlOns. \l 0 •••I "Jo i nl: a) List the names of enzyme classe gI en -(f:thtem~ional UI)fC . c €mistry i.eW\.~~ I Molecular Biology (IUBMB).mC)'XiOO'(e.otuC~)e.. \:b) 1wtnSfLfQSQ.S h~Viro \CA~ f'S 'tD~ CY'2: a~d\agrams show how enzyme activity is affected by: ® L~(»)Y1e'lq Se...S'® I ~qS-eJ' " 'n, h""~~ z:. - H \ 2) S :?,,J,,<"'f 1) P . "3 S II . temperatur~ ... ~ <.i -z,.ef'J ~ - --- - -thve-rea~uns-tcJex-pl-am-=the~ffeets-{)f-oneof-these-factors-on-enzyme-actlvItI. - --- , \••..-:s~ffi . " -(;\ e\..~~ :a) Using a diagram show how the enzyme concentration affects the,rate of-cataly~i~ ~ ~- ~ ~",),.)I \ b d' d . . ~\ '1--\ ~ \v-v-~ \_ \-'y \ 0>.~t7 List conditions t~~~~~~Imng~mes .D \, , L 'Y 0 .r\\.~'r\ ~ 'fe
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i

th~ following Questions: a) Define: Isozyme.

~~S'lt~st~oup :

~

i.. ~':f

D - :

, \~

'<>'

\

6~':-'

_et~

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True or false Michaelis constant, KIn, is: 1- numerically t:gua1te> 1/2 Vm~ D( F2- Dependent on the enzyme concen~r~tion·X ,3- characteristic of an enzyme anQa particular substrate ~ 7' 4- the rat~ of ~ e'?zyIDe-catalyzed reaction mea~ured~~lc~_~i.~ concentratIOn. ~ -

v:::

Independent ---

L--

True or false the presence of ~oilll2etitjye inhibitor: ~ 1- leads to ~ decr.ease in~s~erved¥maxT f= 2-leads to a decrease i~d Vmaxw=')(.. --r 3- Does not affect substrateaffi~!ty to the enzyme ~V4- the.it1l}ililiorandsi}Pstratebina at diff~~nt~~s on the enzyme:r4..-5- inhibitor can b~ to free e~e b~ )1otto the E~ complex. "'P

.--r

r

\X

of enzyme

Nucierc Acids Ql: Name the following com ounds and the name of the bonds involved: o II

NH2

I

-",C,

C

N

HN/

c"'" ~ II CH

N""

I

I

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l

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H 2'

OH

0

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.' HOCrg20 .OH 4'

H

H 3'

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H

H

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H

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I'

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•

Y11-uDse, @.~~~ .0\4

'~S~~

u.Yt·~

t

~H

(J

-----_.-

-----~~-

~

!-"" _.~

N,aIEe~h~di~ereotr~~:ol~~Il~dt~e!:;~ctio~~p~e--'\V\~.9~fYJ l-:C f\ N H ',r ot~Y{0 pI 'O'-J V rr ,/ 'C»' '\.:J:.S~ 2- rRrJA C r~ bbSorn~R.JVft:)~ I~~h 3-

,

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- Using Diagrams define therollowmg: bN'A ReplIcatIOn,TranscnptIOn,and TrlfnslatiO¥l::rv"e..s~~ \ ~ Draw the structure: of guanosine-5'-triphosphate . ~ ~ ~~ .•O\.••.. ~ethefunctionsofrRNA,tRNA,mRNAandD~

.f

+-~

.~~"S~~

~2j\'+D0 ~~

Draw the chemical structure ofp1)pIpp and on the structure give the followin 1- The names of tbe nuc1eosidesinvolved 2- The 5'-end and the 3' end 3- The name or type of bonds involved

.

~'1~I'nL.h

1. Draw the che mical structure of Thymidine triphosphate (TTP)

2. Draw a diagram showing the flow of information in the biological system. Label its components and the name of the processes involved.

I

You should be able to draw the structure of: I-The base pairs AT & GC . 2- Any dinucleotide 3- Nucleoside 4-Nucleotide

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G.lycolysis' ' The end product of.w.l.aerobicglycoly~

.

is: - ...

"-'-oC_=":""

/0 di:C .CJucJ/

.

Cells pro~UCII~&pYt;Iv~t~reqUlres the presence of:'

1-

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The number of reactions in~:?bic

2 .'$'-~

glycolysis is:

,. _

.

. . . /." ~ \. 1.21 ·r, ~~-oxi~a~o~?_ f the NADH during Aerobic glyc~lysis: \,-~'\ '~'

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Re-oxidation of the NADH during Anaerobic glycolysis: Example of tissue lacking mitochondria:

-eue

yl

LA

.00

J

The first five reactions of glycolysi~ correspond to: 9.

~\ (.:C.

cie r-

uJJ

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The number of molecules ofNADH produced with pyruvate formation from glucose: AT[/) ,4/Jr Give the reaction catalyzed by hexokinase: G !t..«c-3f _ GfE-fiery

f:jU!f' g. /2

Write the reaction of isomerization of glucose 6-phosphate including the naIne of the enzyme:

00{1))

"'-..2_>

Write the reaction catalyzed by phosphoctokinase-1 Draw the reaction catalyzed by Aldolase A

\(;)0

(PFK-I):

/00

6-f

/6 )

(

(/6 ) Iou (16 )

Draw the reaction catalyzed by Triose phosphate isomerase

II I

Draw the reaction catalyzed by glyceraldehyde 3-phosphate dehydrogenase What is the first oxidation-reduction

04· (

reaction of glycolysis'!

,

z/

Name the first high energy compound produced in glycolysis

I)

5

v

Draw the reaction catalyzed by phosphoglycerate kinase

1<:'2 (( ') )

Draw the reaction catalyzed by phosphoglycerate mutase

(I" L

b

1.:5 -

r(;f?~rf,'l(::'?-T'; /7'cJc. {/

/

) [ I C) )

Draw the reaction catalyzed by enolase lu 2 ( 19) Draw the reaction catalyzed by pyruvate kinase

i0 2 (~I '))

Give reason Reduction of pyruvate to lactate under anaerobic conditions Explain: Intense exercise poten~lly res~ts i~ cramps. ~ J)

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c.Yln.vrr-vl~tX76L

af'

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a

./ l r°j;r( tJYCdIA',{

How many molecules of ATP are generated for each molecule of glucose converted molecules oflactate? 10 j

to two

True or false there is no net production or consumption o~~uring

glycolysis. T

-...r~ ,,~

)

-

Anaerobic

/

-

I

.)1

List conditions favoring

"

/

What is the net gain

e u c f,

2ATp hf

anaerobic glycolysis

of moles ATP per mole of glucose under aerobic or anaerobic

(;

glycolysis?

How NAD i§ regene, 'rateq ,und,qr ~_othaer?bic ~d aJ15lerobic.~ycolysis? ~A c _To ../! O{ 'Ciic tho ~ re~lt~ /VA YJ ~ +1.\).Ijfj Dr~w the reactions that convert pyruvate to ethanol and give the names of the enzymes and coenzymes involved. \() {;

rJ

DfWj

;;t'c;

t1I'CClrho

Review questions on TeA cycle ooJ cJdl (J{ A yet.) --U'J-rIC G
c/ui1

Give The Other two names for Kreb's cycle and the reason for the names. Show how to calculate the number of moles of ATP produced by the metabolism of pyruvic and AcetylCoA in Kreb's cycle Give the reaction catalyzed by citrate synthetase. List the different functions of Kreb's cycle. Give the reactions in TCA cycle that results in production ofNADH during the metabolism of AcetylCoA in Kreb's cycle. Give the reaction catalyzed by pyruvic dehydrogenase. The number of moles ofFADH2 produced by the metabolism of AcetylCoA in Kreb's cycle is:---and is produced by the following reactions 8The reaction catalyzed by aconitase is as follows: 9The number of moles ofGTP produced by the metabolism of AcetylCoA in Kreb's cycle is: and is produced by the following reactions , . ,,-It. 10The reaction c~talyzed by isocitric dehyqrogenase is as follows: t 'jeo/fic .l U ri _k6/-0 '(u;flt-~If:. 11The number of moles of CO2 produced by the metabolism of Acetyl CoA in Kreb's cycle is: and is produced by the following reactions 12The reaction catalyzed by alpha ketoglutarate dehydrogenase is as follows: 13The number of moles of ATP produced by the metabolism of Pyruvic in Kreb's cycle is: 15 and is calculated as follows: fit T(,'? c 1 1,/II;r4J-l-, ~ ~4 II + l' lQ), .~ - -:)' 14The reaction catalyzed by S"ucc~n~lthiokinase IS as .follows:'----,r, '2 15The reaction catalyzed by succmIC dehydrogenase ISas follows --.:.- ~(A.[C/n...J-~ri:' fL-tJ t ~ 16The reaction catalyzed by malic deh~drogenase is ~s follow~ AJI t'.J-, '1tU.( u, t 17The reaction catalyzed by fumarase IS as follows t"Lf.tYlUJcJf',~ /VI&-{c. e " 18Give.the key enzymes and their reactions that regulates the TCA cycle It4 (9 ·9 )

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Review Questions on ... 1. Give one of the tissues that require a continuous supply 9f glucose ~ a metabolic fuel. / ',A-e\~' ' I -. ? ',""'i " / • ./1 ' J J ~ , I" J "'11 2. WhatarethePl!curs2!"~ fiorguconeogenesI.s. G;~gf~e~''.J''~ __ Ci~lI~e~ r;;, ..•.f~fr(i.'J CAC,N:•.4 - 'ch-'c.Jf" 3. During pro,longed faA~mg, what organ( s) IS the SIte of the newly synthesIzed glucose ~ c~ If [of J[,{,{J;to molecules? !-I/JnYT- ---0 v(f ~"",' , U . '7 'rrf'm"S,'~f:4. DiagrammaticallyshowthefunctionofC.oricycle JiJf;.,M' Ie';, (ifS). . efCdi"\~ h'1fUre 5. Why Acetyl CoA and compo~ds that~Ive ~se ~o!i~;~I/~oA .~annot gIve rIse to a net Ol U Co fl 'synthesis of glucose. 11IYCDI~,h' 1((..1 V",; ,Alf It''lffl '-..t [" t( ?" ~ /nf'lflfl ~{( ')l.-i(l1ve.de 6.How many reversible atld UI.eversible reactions are in glycolysisY h 1/ y 7. Show how i~ible reactions in glycolysis c~ be reversed du~~g glu7?neo~enesis ,/ / t) /Cf ':i'8'. Where in the ce.l1the enzy~es of gluconeogenesIs are loc~ted. M,'fIJ[ }1"'-'(,LI{) ~€P c;7t9;!d:. ((,{ 'CJ!"" 9. Write the equatIOn of reactIOn catalyzed by fructose 1,6-biSphosphatase.« y~

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PI

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1

CC,.f1Vflr)

rJ'1 ~(dp C'

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bvoasses the irreversible hexokinase reaction

ii: H~w Glu~~gon ~affects gluconeogenesis fI l' 1

I 2 2. () () Ii [), ,r / . O-OU'f'r.-Se- ( "uv'€...---( c'---t U,L&r/, f 12 What is the elect 0 nsu m on g uconeogenesls ,. .- 'f /. 17' J' 13' What is the source of acetyl CoA d)Jl'ingfasting. 0 '1:-J . h c-- r-- C'm ill. cJ-Y-. ." ilt- '. u.---e \ \ I-€ :.1.2. 'n J''Vf " ;Vl~ r:6 ro",{ u ¥. (HO '/'v4 " ~.~_,J-J: _e::-~~~I./ ~ {}! 'j,~/;:-:!-'''f I i1 i26 (j11ccr-..Rc
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, Glycogen is storedinlhr followjp.g_~jssues: ~ /(efe)ujl11uscLt::~e ~c/..t'i/ff '7 ~o ot~y ce16. Z Glycogenesis is: ~~(lffwsl~ "f cr.yr0(f-l?n. G~l~VI ,'~ '.?JVrt'!l~~'7.£J!. j)rvvy/ mole c-Je of , "3,The substrate ~or g ycogen synthase IS: GI'(Le'rbY - I[rd-~ _ Am, rf;OCJu oZ- f)Ff IV! (~. 0 cce-:r in 4 Draw the reactIon catalyzed. by glycogen ph?sp?orylase \\' + { 'c ;:,--1080./' ~ tf''7U1 rt 5 Compare between the functIOn of glycogen In lIver and muscles (! ey~' 7.; i AT er" True or false: 1. Glycogen synthase can only elongate already existing chains of glucose. 2. In the presence of a glycogen fragment, a protein, called glycogenin, can serve as an acceptor of glucose residues f 3. The degradative pathway that mobilizes stored glycogen is a rev~t-sal of the synthetic . C t7 I p1 reactIOns. ,--{--«J>"C/( 4. When glycogen is de~~ed, the primary product is glucose 6-phosphate, F 5. phosphorolysis until fl,Xeglucosyl units remain on each chain before a branch point 6. phosphorylase cannot degrade limit dextrin any further } 7. In the liver, glycogen synthesis accelerates during periods when the body has been well fed, whereas glycogen degradation accelerates during periods of fasting. f 8. In skeletal muscle, glycogen degradation occurs during active exercise, and synthesis begins as soon as the muscle is again at rest. I . 9. glycogen synthesis and degradation are hormonally regulated. -J~ 10. glycogen degradation is increased when e~rgy levels and available &!.UCOSl; supplies are

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Give two examples of Hemeproteins VVlvp ~ \~~\ '" / "'eV(\~o:>\''<:>\'" List the function of myoglobin Yc..s!>\vo/ o~ C!>~ & C)~ C""VY\'(.'C What is the function of hemoglobin '\v •••",~~~y\ ()~ f'l'"O'-' \\.l."\j'~ \0 c_~i \\r+~ Answer the following true or false and correct the false statement The iron in heme is ferric ion (Fe3+) F 2. In heme the iron is held in the center of the heme molecule by bonds to the two nitrogen atoms of the porphyrin ring. r-l\)3. Myoglobin, a hemeprotein present in heart and skeletal muscles, F ~. Myoglobin consists of two polypeptide chains. 1...\)5. Hemoglobin is found exclusively in red blood cells \ F --6. ' Hemoglobin A, is composed of one single polypeptide \... \) 7. The hemoglobin is tetramer T <. 'o(CI ..\l~ 'J06'~ '" ".) flll.lY ~ \'"oh .•."'- ,"",0 \u~\t.\\ \..~ ') 8. (a~) dimer are held tightly together, primarily by hydrophobic interactions (t) l~ ) 9. Ionic and hydrogen bonds do not occur between the members of the dimer. lV') ~ ) 10. The two dimers are held together primarily by ionic bonds . .,\.'Tl 11. The deoxy form of hemoglobin is called the "T," form. '\ 12. The T form is the high oxygen-affinity form ofhemoglobin.f \...\) 13. The binding of oxygen to hemoglobin causes the rupture of some of the ionic bonds and hydrogen bonds between the a~ dimers. -'\ \..~ '\14. "R," or relaxed form, which is the low oxygen-affinity form ofhemoglobin.r\..r) 15. Myoglobin can bind only two molecules of oxygen (02), because it contains two heme groups. \.~) 16. Hemoglobin can bind four oxygen molecules, one at each of its four-heme groups. '\ \...f) 17. Myoglobin has a lower oxygen affinity than does hemoglobin. ~ (\) 18. The oxygen dissociation curve for myoglobin has a hyperbolic shapeT (.0 •••• t 19. Myoglobin is designed to bind oxygen released by hemoglobin at the ~ p02 found in muscle. Myoglobin, in turn, releases oxygen within the muscle cell in response to oxygen demand. t=" \T;20. The oxygen dissociation curve for hemoglobin is sigmoidal in shapw r; 21. the subunits of hemoglobin do not cooperate in binding oxygen. ~ ~ '122. Cooperative binding of oxygen by the four subupits of hemoglobin means that the \. ~ '''' l..••. ~"h binding of an oxygen molecule at one heme group decreases the oxygen affinity of the remaining heme groups in the same hemoglobin molecule d=., (\) 23. The sigmoidal oxygen-binding curve reflects specific structural changes that are initiated at one heme group and transmitted to other heme groups in the hemoglobin tetramer.' 30C \..~) 24. The affinity of hemoglobin for the last oxygen bound is approximately 3 times greater than its affinity for the first oxygen boundt l 25. The cooperative binding ofJ.xxgen allows hemoglobin to deliver more oxygen to the tis'sues in response to relatively l~rg~r changes in the partial pressure of oxygen. ~ ,26. In the lung, the concentration of oxygen is high and hemoglobin becomes virtually saturated (or "loaded") with oxygen. '\ '" 27. In the peripheral tissues, oxyhemoglobin releases (or "unloads") much of its oxygen for use in the oxidative metabolism of the tissues "'\ \" 28. Most of the carbon dioxide produced in metabolism is hydrated and transported as bicarbonate ion '\ 29. Carbon monoxide (CO) binds tightly (but reversibly) to the hemoglobin iron, forming carbon monoxyhemoglobin (HbCO). T

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When carbon monoxide binds to one \or more of the four-heme sites, causing the remaining heme sites to bind oxygen with l~ci affini~ ~ 31. Carbon monoxide poisoning is treated with 10 p~~cent oxygen therapy, which facilitates the dissociation of CO from the hemoglobin. ~ \" 32. HbF, ~e normally synthesized only during fetal development. "' 33. The lo~~'~xygen affinity of HbF facilitates the transfer of oxygen from the maternal circulation across the placenta to the red blood cells of the fetus. ~ '\ 34. Increa~d amounts of HbAlc are found in red blood cells of patients with diabetes mellitus. \ ":je"'~c... ~ 35. Sickle cell disease (also called sickle cell anemia) is a nongenetic disorder of the bloodt= r 36. Sickle cell disease is caused by a single nucleotide alteration (a point mutation) in the globin gene. \" 37. An infant does not begin showing symptoms of the disease until sufficient HbF has been replaced by HbS':\ T 38. Sickle cell disease is characterized by chronic hemolytic anemia, and increased susceptibility to infections, usually beginning in early childhood. ""'\ c!9 [; 39. The lifetime of an erythrocyte homozygous for HbS is approximately 90 days, compared with 120 days for normal red blood cells. "'\"40. Amino acid substitution in HbS P chains in which glutamate at position six has been replaced with valine '\41. Sickling causes tissue anoxia T '\ 42. At low oxygen tension, HbS polymerizes inside the red blood cells, first forming a gel, then subsequently assembling into a network of fibrous polymers that stiffen and distort the cell, producing rigid, misshapen erythrocytes. 143. Such sickle cells frequently block the flow of blood in the narrow capillaries. =( 44. This interruption in the supply-of oxygen leads to localized anoxia (oxygen deprivation) in the tissue, causing pain and eventually death (infarction) of cells in the vicinity of the blockage. " T45. HbC is a hemoglobin v~t that has a single amino acid substitution in the sixth position of the p-globin chain 1 '"t"46. In this case ofHbC a lysine is substituted for the glutamate-:-\ Patients homozygous for hemoglobin C generally db>silltsufferfrom infarctive cri~' \48. Oxidation of the heme component of hemoglobin to the ferric (Fe3+) state forms methemoglobin \ 49. methemoglobin cannot bind oxygen:\, ~ 50. In p-Thalassemias the synthesis of a-globin chains is decreased or absent, \51. a -Globin chains cannot form stable tetramers and, therefore, precipitate, causing the premature death of cells initially destined to become mature red blood cells~ '\ 52. a- Thalassemias are defects in which the synthesis of a-globin chains is decreased or abseIif:'1""" ~ \53. In a-Thalassemias the subunits show no heme-heme interaction. I _ 54. In a-Thalassemias Tetramers have very high oxygen affinities. This makes them ~ essentially useless as oxygen deliverers to the tissues. \'

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