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Tugas Amnalitik

The catalysis of amino acid hydrolysis by zinc carboxypeptidase can be inhibited by substances like β-phenylpropionic acid. Data is presented on the hydrolysis of benzoylglycylglycyl-L-phenylalanine with and without inhibition. This is an example of noncompetitive inhibition where the inhibitor does not bind to the enzyme's active site. Calculations using the Lineweaver-Burke equation show the inhibition constant K1 is 1.1 x 10-4 mol/L, the Michaelis constant Ks is 1.18 x 10-3 mol/L, and the rate constant k2 is 0.053 s-1.
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0% found this document useful (0 votes)
74 views4 pages

Tugas Amnalitik

The catalysis of amino acid hydrolysis by zinc carboxypeptidase can be inhibited by substances like β-phenylpropionic acid. Data is presented on the hydrolysis of benzoylglycylglycyl-L-phenylalanine with and without inhibition. This is an example of noncompetitive inhibition where the inhibitor does not bind to the enzyme's active site. Calculations using the Lineweaver-Burke equation show the inhibition constant K1 is 1.1 x 10-4 mol/L, the Michaelis constant Ks is 1.18 x 10-3 mol/L, and the rate constant k2 is 0.053 s-1.
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NAMA

: RENDI MAHARDIKA PINEM

NIM

: 130802042

FAKULTAS/JURUSAN : MIPA/KIMIA S-1


TUGAS KIMIA FISIKA IV
The catalysis of the hydrolysis of amino acids by various
metallocarboxypeptidases can be inhibited by various substances. Consider the
following data for the hydrolisis of benzoylglycylglycyl-L-phenylalanine (Bz-GlyGly-Pn) by 1.0 x 10-1 M zinc carboxypeptidase :
C(S)/(10-4 mol . L-1)
v(uninhibited)/(10-5 mol . L-1 .
s-1)
v(inhibited)/(10-5 mol . L-1 . s-1)

2.0

5.0

10.0

4.0
1.4

7.7
2.7

11.1
3.9

Where the inhibitor is 2.0 x 10-4 M, -phenylpropionic acid. Show that this is an
example of noncompetition inhibition.
In noncompetitive inhibition the inhibitor does not attack the active site of the
enzyme :
E+SXE+P
+
+
I
I
(13.30a)

EI + S XI
For this mechanism, the Lineweaver-Burke equation is :

1
v

[ ( ) ](

KS 1
C(1)
1
+
1+
V S C( S) V S
K1

(13.31a)
Where C(1) is the concentration of the inhibitor and K 1 is the equilibrium constant
for the inhibition process. The plots of 1/v against 1/C(S) for both the uninhibited
and inhibited processes are shown in Fig. 13-14. Comparison of (13.31a) with
(13.28a) indicates that both the slope and the intercept for the uninhibited
reaction will be increased by a factor of [1+C(1)/K 2]. The respective intercepts
are 5.00 x 103 L . s . mol -1 and 1.427 x 104 L . s . mol -1, and the respective slopes
are 4.00 s and 11.5 s, giving :

C (1 )
1+
=
K1

1.427 x 104 L. s . mol1


3
1
5.00 x 10 L . s . l mol

11.5 s
=2.86
4.00 s

Solving for K1 and substituting in the concentration of the inhibitor gives :

2.0 x 104 mol . L1


K 1=
2.861

= 1.1 x 10-4 mol . L-1

A plot of against v/C(GPNA) is shown in Fig. 13-13. From the


intercept,
Vs = intercept =

2.12 x 10-3 mol . L-1 . s-1

And from the slope,


Ks = -(slope) = -(-1.18

x 10-3 mol . L-1) = 1.18 x 10-3 mol . L-1

Solving (13.23) for k2 and substituting the data gives :

K 2=

2.12 x 107 mol . L1 . s1


4.0 x 105 mol . L1

= 0.053 s-1

Katalisis dari hidrolisis asam amino oleh berbagai metallocarboxypeptidases


dapat dihambat oleh berbagai zat. Perhatikan data berikut untuk hidrolisis dari
benzoylglycylglycyl-L-fenilalanin (Bz-Gly-Gly-Pn) sebesar 1,0 x 10-1 M seng
Carboxypeptidase:
C(S)/(10-4 mol . L-1)
v(uninhibited)/(10-5 mol . L-1 .
s-1)
v(inhibited)/(10-5 mol . L-1 . s-1)

2.0

5.0

10.0

4.0
1.4

7.7
2.7

11.1
3.9

Dimana inhibitor adalah 2,0 x 10-4 M, asam -fenilpropionat. Tunjukkan bahwa ini
adalah contoh dari penghambatan yang bersaing.
Dalam penghambatan nonkompetitif, inhibitor tidak menyerang situs aktif
enzim:
E+SXE+P
+
+
I
I
(13.30a)

EI + S XI
Untuk mekanisme ini, persamaan Lineweaver-Burke adalah:

1
v

[ ( ) ](

KS 1
C(1)
1
+
1+
V S C( S) V S
K1

(13.31a)
Dimana C (1) adalah konsentrasi inhibitor dan K 1 adalah konstanta
kesetimbangan untuk proses penghambatan. Plot dari 1 / v terhadap 1 / C (S)
untuk kedua proses tanpa hambatan dan menghambat ditunjukkan pada
Gambar. 13-14. Perbandingan (13.31a) dengan (13.28a) menunjukkan bahwa
kedua lereng dan intercept untuk reaksi tanpa hambatan akan meningkat
dengan faktor [1 + C (1) / K 2]. Penyadapan masing adalah 5,00 x 10 3 L. s. mol-1
dan 1,427 x 104 L. s. mol-1, dan lereng masing adalah 4,00 s dan 11,5 s,
memberikan:

C (1 )
1+
=
K1
Pemecahan untuk
memberikan:

K1

1.427 x 104 L. s . mol1


5.00 x 103 L . s . l mol1
dan

menggantikannya

K 1=

11.5 s
=2.86
4.00 s

dalam

konsentrasi

inhibitor

2.0 x 10 mol . L
2.861

= 1.1 x 10-4 mol . L-1

Sebuah plot terhadap v / C (GPNA) ditunjukkan pada Gambar. 13-13. Dari


mencegat,

Vs = intercept =

2.12 x 10-3 mol . L-1 . s-1

Dan dari slope,


Ks = -(slope) = -(-1.18

x 10-3 mol . L-1) = 1.18 x 10-3 mol . L-1

Pemecahan (13.23) untuk k2 dan mengganti data memberikan:

K 2=

2.12 x 107 mol . L1 . s1


5
1
4.0 x 10 mol . L

= 0.053 s-1

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