Want to create interactive content? It’s easy in Genially!
Enzymes, Intro
clacardona
Created on August 9, 2020
Start designing with a free template
Discover more than 1500 professional designs like these:
View
Vaporwave presentation
View
Animated Sketch Presentation
View
Memories Presentation
View
Pechakucha Presentation
View
Decades Presentation
View
Color and Shapes Presentation
View
Historical Presentation
Transcript
Mis conocimientos...
- Actividad específica
- Apoenzima
- Centro catalítico
- Cinética enzimática
- Coenzima
- Constante de Michaelis
- Enzima limitante de la velocidad
- Grupo prostético Holoenzima
- Inhibición competitiva Katal
- Regulación alostérica
- Serina proteasa
http://www.kscience.co.uk/animations/anim_2.htm; https://www.abpischools.org.uk/topic/enzymes-16plus/5/1
Enzymes
An enzyme is a substance that acts as a catalyst in living organisms, regulating the rate at which chemical reactions proceed without itself being altered in the process. The biological processes that occur within all living organisms are chemical reactions, and most are regulated by enzymes.
Enzymes
Enzymes
Nomenclatura establecida por la Unión Internacional de Bioquímica
Okey, intentemos analizar el siguiente gráfico contestando y relacionando las siguientes preguntas con la imagen a continucaión: 1. Qué es una isoenzima? 2. Qué papel metabólico tiene la LDH? 3. Qué ilustra cada gráfica? 4. podrías explicar cómo este análisis se incorpora a la práctica médica?
- CK o glucoquinasa
+ CK o glucoquinasa
Análisis gráficos alternativos permiten determinar con mayor exactitud la Km y la Vmáx de una enzima
Esta ecuación proporciona una línea recta (y =mx + b)con y = 1/v x = 1/[S], m = pendiente, y b = intersección con y.
Esta ecuación proporciona una línea recta (y =mx + b)con y = 1/v x = 1/[S], m = pendiente, y b = intersección con y.
En este caso, la representación de v frente a v/[S] tiene un eje y (intersección de v) de Vmáx, una intersección del eje x (v/[S]) de Vmáx/Km y una pendiente de −Km.
Los inhibidores competitivos producen un aumento aparente de la Km sin modificar la Vmáx
- Competitive inhibition involves a molecule, other than the substrate, binding to the enzyme’s active site
- The molecule (inhibitor) is structurally and chemically similar to the substrate (hence able to bind to the active site)
- The competitive inhibitor blocks the active site and thus prevents substrate binding As the inhibitor is in competition with the substrate, its effects can be reduced by increasing substrate concentration
Los inhibidores no competitivos pueden unirse a sitios de unión fuera del centro activo y modificar tanto la Km como la Vmáx de la enzima
- Non-competitive inhibition involves a molecule binding to a site other than the active site (an allosteric site)
- The binding of the inhibitor to the allosteric site causes a conformational change to the enzyme’s active site
- As a result of this change, the active site and substrate no longer share specificity, meaning the substrate cannot bind
- As the inhibitor is not in direct competition with the substrate, increasing substrate levels cannot mitigate the inhibitor’s effect
pero....