• Sonuç bulunamadı

BIO 435 BIO 435

N/A
N/A
Protected

Academic year: 2021

Share "BIO 435 BIO 435"

Copied!
12
0
0

Yükleniyor.... (view fulltext now)

Tam metin

(1)

BIO 435 BIO 435

ENZYMOLOGY ENZYMOLOGY

VI. WEEK

(2)

Enzyme

Kinetics

(3)

1. Enzymes affect reaction

rates, not equilibria

(4)

2. Reaction rates and equilibria

have precise thermodynamic

definitions

(5)

Substrate concentration affects the rate of enzyme-catalyzed

reactions.

(6)

Hyperbolic curves EQUATION

Sigmoidal feature

Michaelis-Menten Equation Michaelis-Menten Kinet

Michaelis-Menten Kinet ics ics

(7)

Michaelis-Menten Kinet

Michaelis-Menten Kinet ics ics

E + S k1 ES E + P

k-1

k2

E: enzyme

S: substrate

ES: Enzyme-Substrat komplex

P: product

(8)

Step 1:

Step 1:

Formation and

degradation of

the ES complex

(9)

Step 2:

Step 2:

Steady state

assumption

(10)

Step 3:

Step 3:

Solution of the

equation for ES

(11)

Step 4:

Step 4:

Vo EXPRESSION in

terms of ES

(12)

Referanslar

Benzer Belgeler

Allosteric enzymes exist in either exist in either an active or inactive state. an active or

mechanism involves the acylation and.. deacilation of the

Some regulatory enzymes undergo reversible

 1) Enzyme Technology, Martin Chaplin and Christopher Bucke, Cambridge University Press, 1990. Cox, Çeviri

 KİMOTRİPSİN: AROMATİK aminoasitlerin katıldığı peptid bağlarını KARBOKSİL uçtan keser... SUBSTRAT SPESİFİKLİĞİ SUBSTRAT SPESİFİKLİĞİ. 

 1) Enzyme Technology, Martin Chaplin and Christopher Bucke, Cambridge University Press, 1990. Cox, Çeviri

 ENZİMLERİN BAZILARI SUBSTRATI İLE STABİL OLMAYACAK ŞEKİLDE KOVALENT İNTERAKSİYONLAR. OLUŞTURABİLİR.  BU SON

 1) Enzyme Technology, Martin Chaplin and Christopher Bucke, Cambridge University Press, 1990. Cox, Çeviri