MED LEZ 2 ENZIMI 2016
Transcript of MED LEZ 2 ENZIMI 2016
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CATALISI ENZIMATICA
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REAZIONI CHIMICHE
A B
[B]Keq =
[A]
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REAZIONI CHIMICHE�SPONTANEITA’ DI REAZIONE
∆G = variazione di energia libera
= -RT ln Keq
= capacità di un sistema di compiere
lavoro utile
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REAZIONI CHIMICHE� ∆G = - ESOERGONICA
LA REAZIONE LIBERA ENERGIA
∆G = + ENDOERGONICA
LA REAZIONE HA BISOGNO DI ENERGIA
∆G = 0 EQUILIBRIO
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A
B
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H2O2 Acqua ossigenata
2H2O2 2H2O + O2
∆G = - ESOERGONICA
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REAZIONI CHIMICHE
� VELOCITA’ di reazione
1. Aumentando la temperatura
2. Usando dei catalizzatori
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ENZIMI
�GLI ENZIMI SONO CATALIZZATORI
BIOLOGICI IN GRADO DI
AUMENTARE LA VELOCITA’
DI UNA REAZIONE SENZA ALTERARE
L’EQUILIBRIO DELLA STESSA
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ENZIMI CLASSIFICAZIONE
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DEIDROGENASI
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DEIDROGENASI
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Transferasi
CHINASI
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Alcol deidrogenasi
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SITO CATALITICO
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EFFETTO DEL pH
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pH
� Perché p……. perché H …………..
�Il termine p (operatore) simboleggia due operazioni matematiche da effettuare sulla concentrazione idrogenionica [H+]. Le due
operazioni sono: il logaritmo in base 10 della concentrazione molare espressa in
moli/litro e il cambio di segno del risultato (moltiplicazione per -1).
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EFFETTO del pH
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EFFETTO TEMPERATURA
20 37 60 80
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REAZIONE NON CATALIZZATA
A + B
P + Q
∆G = -
ESOERGONICA
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REAZIONE CATALIZZATA
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http://www.youtube.com/watch?v=VbIaK6PLrRM&feature=related
MECCANISMO DELLA
CATALISI ENZIMATICA
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TEORIA CHIAVE-SERRATURA
P2
P1
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TEORIA dell’ ADATTAMENTO INDOTTO
P2
P1
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Modello catalisi enzimatica
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Funzione enzimi
http://www.youtube.com/watch?v=V4OPO6JQLOE
http://www.youtube.com/watch?v=VbIaK6PLrRM&NR=1http://www.youtube.com/watch?v=E-_r3omrnxw
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CINETICA ENZIMATICA
K1 K3
�S +E ES EP
P + E
K5K6
K4K2
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EQUAZIONE DI MICHAELIS-MENTEN
1913
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CINETICA ENZIMATICA
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PARAMETRI CINETICI
�Vmax = velocità d’idrolisi massima alla quale l’
enzima tende, a concentrazioni di substrato infinite
�Km = concentrazione di substrato alla quale la reazione va metà della velocità massima
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Km e affinità
1. Un valore alto di Km indica una bassa
affinità per il substrato
2 . Un valore basso di Km indica un
alta affinità per il substrato
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Kcat numero di turnover
K1 K3
♦S +E ES EP
K2 K5
P + E
K4
K6
Kcat
Kcat numero di molecole di S trasformate in 1 sec
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Efficienza dell’enzima
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REAZIONI A PING-PONG
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REAZIONI PING PONG
A + B C + DE
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INIBIZIONE ENZIMATICA
1. IRREVERSIBILE
2. REVERSIBILE a. COMPETITIVA
b. NON COMPETITIVA
c. INCOMPETITIVA
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COMPETITIVA
L’ INIBITORE COMPETE CON IL
SUBSTRATO PER IL SITO CATALITICO
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NON COMPETITIVA
L’ INIBITORE NON COMPETE PER IL SITO
CATALITICO E SI LEGA A UN SITO
DIVERSO
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INCOMPETITIVA
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INIBIZIONE INCOMPETITIVA
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REGOLAZIONE ENZIMATICA
1. Costitutivi /Induttivi
2. pH
3. Associazione / Dissociazione
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1. Costitutivi /Induttivi
�ESOCHINASI
�GLUCOCHINASI +3.3
-7.3
-4.0
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3. Associazione / Dissociazione
PKA
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4. Inibizione da Prodotto
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5. Precursori Inattivi
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Precursori Inattivi
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Precursori Inattivi
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6.MODIFICAZIONE COVALENTE
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ENZIMI ALLOSTERICI
� ENZIMI IN CUI SONO PRESENTI «ALTRI» ALLO SITI
� SITO CATALITICO
� SITO REGOLATORE
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ENZIMI ALLOSTERICI(aspartato transcarbamilasi)
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EFFETTORI
OMOTROPICI ligando = effettore, spesso è effettore positivo, il suo legame all’enzima è cooperativo perché stimola il legame di altre molecole di substrato
ETEROTROPICI molecole diverse dal substrato (spesso modulazione feedback)
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Cooperazione negativa o positiva
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CLASSE K modificazione Km
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CLASSE V modificazione Vmax
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ISOENZIMIGli isoenzimi sono enzimi esistenti in
forme molecolari diverse, catalizzanti la stessa reazione
LATTICO DEIDROGENASI LDH
E’ un tetramero formato da una diversa composizione di 2 subunita’
H = heart M= muscle
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LDH
4H
4M
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LDH
4H
4M