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PRIMERA CLASE DE ENZIMAS DEFINICION ENERGIA DE … · PRIMERA CLASE DE ENZIMAS ... Cuando la concentración de GAP es 0.05 mM, ... desarrollo del metabolismo intermediario se

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Page 1: PRIMERA CLASE DE ENZIMAS DEFINICION ENERGIA DE … · PRIMERA CLASE DE ENZIMAS ... Cuando la concentración de GAP es 0.05 mM, ... desarrollo del metabolismo intermediario se

Página 1 clases83.jimdo.com 096437814

PRIMERA CLASE DE ENZIMAS DEFINICION

ENERGIA DE ACTIVACION

CONCENTRACION EN FUNCION DE

TIEMPO

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Febrero 2017

Diciembre 2016

Diciembre 2015

Febrero 2015

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ENERGIA DE ACTIVACION

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PREGUNTA 21 DE DICIEMBRE 2015

Las enzimas aceleran las reacciones que catalizan

de la siguiente manera (señale la opción correcta):

a) Disminuyendo el ∆G real de la reacción.

b) Disminuyendo el ∆G'0 de la reacción.

c) Disminuyendo la energía de activación de la

reacción.

d) Aumentando la energía del estado de

transición.

e) Desplazando el equilibrio de la reacción

hacia la formación de productos.

Respuestas: c.

PREGUNTA 4 DE FEBRERO 2015

Indique la opción correcta respecto a la actividad

de la enzima:

a) La presencia de la enzima aumenta la

energía de activación de la reacción

b) La presencia de la enzima aumenta la

energía libre de la reacción

c) La presencia de la enzima disminuye la

energía de activación de la reacción.

d) La presencia de la enzima disminuye la

energía libre de la reacción.

Respuestas: c.

PREGUNTA 12 DE DIEMBRE 2014

Teniendo en cuenta sus conocimientos sobre las

enzimas, señale la afirmación correcta.

a) Una enzima permite que la reacción ocurra

cuando el ΔG es mayor a 0.

b) Durante el trascurso de la catálisis la

velocidad aumenta hasta alcanzar la Vmáx.

c) Una enzima cataliza la reacción

disminuyendo su constante de equilibrio

(Keq).

d) Una enzima cataliza la reacción sin afectar su

constante de equilibrio (Keq).

Respuestas: d.

PREGUNTA 5 DE FEBRERO 2014

¿Qué efecto tiene la catálisis enzimática sobre la

termodinámica de una reacción?

a) Disminuye la energía libre de Gibbs del

sustrato.

b) Disminuye la energía libre de Gibbs del

producto.

c) Disminuye la diferencia de energía libre de

Gibss entre reactivos y productos.

d) Disminuye la energía libre de activación de

la reacción.

Respuestas: d.

PREGUNTA 1 DE DICIEMBRE 2013:

Las enzimas aceleran las reacciones que catalizan

disminuyendo:

a) La diferencia de energía libre estándar de la

reacción.

b) La diferencia de energía libre real de la

reacción.

c) La diferencia de energía libre de activación

de la reacción.

d) La diferencia de energía libre en el equilibrio

de la reacción.

Respuestas: c.

PREGUNTA FEBRERO 2017

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CONCENTRACION EN

FUNCION DEL TIEMPO

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PREGUNTA 1 PRIMER PARCIAL 2015

La trehalosa es un disacárido NO reductor formado

por 2 moléculas de glucosa.

En el intestino es hidrolizado por la enzima

TREHALASA.

Trehalosa Glucosa

Se midió la actividad de la de enzima

TREHALASA (5 µM) con diferentes

concentraciones de su sustrato, trehalosa (0‐32

mM), midiendo la velocidad de formación de

glucosa en el tiempo.

Para determinar la velocidad inicial de formación

de glucosa se usa el Dinitrosalicilato (DNS)

midiendo la absorbancia (570 nm) luego de

distintos tiempos para cada concentración de

sustrato. Los resultados obtenidos se muestran en

el siguiente gráfico:

Tiempo (min)

Del análisis de los datos representados en la figura

podemos afirmar que la velocidad inicial de

formación de glucosa por la trehalasa para una

concentración de trehalosa de 2 mM es:

a) 0,5 mM/min.

b) 1 mM/min.

c) 2 mM/min.

d) 2,5 mM/min.

e) 5 mM/min.

Respuestas: b.

PREGUNTA 17 EXAMEN JULIO 2012

Un estudiante está midiendo la velocidad de la

enzima invertasa que cataliza la siguiente reacción:

Sacarosa + H2O ------------- glucosa + fructosa

El estudiante sigue la concentración de sacarosa y

glucosa en función del tiempo a una concentración

inicial de 0,10 M de sacarosa. El KM para la

sacarosa es 0,010 M y la concentración de enzima

es de 1M. A continuación se muestra el ensayo.

De acuerdo al gráfico podemos afirmar que:

a) La velocidad máxima se aproxima a 0,025

M/min.

b) La velocidad máxima correspondería a la

tangente en el punto de la flecha de la gráfica.

c) Es imposible calcular la velocidad máxima

en estas condiciones.

d) La velocidad máxima aumenta durante los

primeros 4 minutos.

Respuestas: a.

0 1 2 3 4 5 6 7 8 9 10 0

1

2

3

4

5

6

7

8

9

10

1 mM 2 mM 4 mM 8 mM 16 mM 32 mM

Trehalosa )

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SEGUNDA CLASE DE ENZIMAS VELOCIDAD EN FUNCION DEL

TIEMPO

VELODICAD EN FUNCION DEL

SUSTRATO

DOBLE RECIPROCA

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Vo EN FUNCION DE SUSTRATO

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PREGUNTA 11 DICIEMBRE 2014:

La enzima gliceraldehído-3-P deshidrogenasa

(GAPDH) presenta un Km para el gliceraldehído-

3-P (GAP) de 0.1 mM. La concentración

intracelular de gliceraldehido3-P varía entre 0.04 y

0.1 mM. Teniendo en cuenta estos datos indique

cual de las opciones sobre la actividad intracelular

de la GAPDH es correcta.

a) Cuando la concentración de GAP es 0.01

mM, la velocidad inicial corresponde a

0.9Vmax.

b) Cuando la concentración de GAP es 0.04

mM, la velocidad inicial corresponde a

0.28Vmax.

c) Cuando la concentración de GAP es 0.05

mM, la velocidad inicial corresponde a

0.5Vmax.

d) Cuando la concentración de GAP es 0.1 mM,

la velocidad inicial corresponde a Vmax.

e) Cuando la concentración de GAP es 0.5 mM,

la velocidad inicial corresponde a Vmax.

Respuestas: b.

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PREGUNTA 43 FEBRERO 2012

La mayoría de las reacciones fundamentales para el

desarrollo del metabolismo intermediario se

encuentran catalizadas por enzimas.

Muchas de estas enzimas presentan un

comportamiento del tipo de michaelis menten en

relación a su comportamiento frente a distintas

concentraciones de sustrato.

Con respecto a este tipo de cinética enzimática

indique la opción correcta:

a) Si la concentración de enzima pasa de 0,05

mM el valor de Km se duplica.

b) Si cambiamos el valor de PH del medio de

reacción, la curva de velocidad den función

de la concentración de sustrato no varía.

c) La velocidad máxima a la que llega una

enzima depende de la concentración de

enzima.

d) A una concentración de sustrato igual al

doble del Km la enzima está trabajando a

velocidad máxima.

Respuestas: c.

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DOBLE RECIPROCA

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PREGUNTA 16 DEL PRIMER PARCIAL 2014

Teniendo en cuenta los datos representados en la

gráfica indique cuál de las siguientes opciones

representa la ecuación de michaelis menten para

este preparado enzimático.

a) Vo = 3,06 [S]

59,2+S

b) Vo = 0,3 [S]

5,35+S

c) Vo = 3,06 [S]

59,2S

d) Vo = 3,06 [S]

1+S

Respuestas: a.

PREGUNTA 2 DEL PRIMER PARCIAL 2015

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TERCERA CLASE DE ENZIMAS ORDENES DE REACCION

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CONSTANTE CINETICAS

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INHIBIDORES

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PREGUNTA 15 DEL EXAMEN DE JULIO DE

2012

Se estudia la velocidad inicial de una enzima y el

efecto de un compuesto denominado X. A

continuación se muestra el gráfico de doble

recíprocas (1/v versus 1/[s]), en línea continua se

representa la enzima sola y en línea cortada la

misma enzima bajo similares condiciones en

presencia del compuesto X.

Teniendo en cuenta el gráfico de doble recíproca de

la enzima sola podemos afirmar que:

a) El Km de la enzima por el sustrato

corresponde a 2 mM.

b) El Km de la enzima por el sustrato

corresponde a -2 mM.

c) El Km de la enzima por el sustrato

corresponde a 0,5 mM.

d) La Vm corresponde a 0,1 moles/min.

e) La enzima presenta una cinética de tipo

alostérico o cooperativo.

Respuestas: c.

PREGUNTA 16 DEL EXAMEN DE JULIO

2012

Comparando ambas gráficas podemos afirmar:

a) El compuesto X actúa como un activador de

la enzima.

b) El compuesto X actúa como un inhibidor no

competitivo.

c) El compuesto X actúa como un inhibidor

acompetitivo.

d) El compuesto X actúa como un inhibidor

competitivo.

e) El compuesto X disminuye el Km aparente

de la enzima por su sustrato.

Respuestas: d.

PREGUNTA 3 DEL EXAMEN DICIEMBRE

2013

El siguiente gráfico se obtuvo al representar 1/Vo

en función de 1/S para la enzima invertasa en

ausencia (I) y en presencia de una sustancia A (II).

Indique la opción correcta respecto a los

parámetros cinéticos de la enzima en las

condiciones ensayadas.

a) El Km en (II) es menor que en (I).

b) El Km es el mismo en ambas situaciones.

c) El Km en (II) es mayor que en (I).

Respuestas: c.

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PREGUNTA 3 DEL EXAMEN DICIEMBRE

2013

En el ensayo representado en la figura anterior la

concentración de enzima es la misma en la gráfica

(I) que en la (II). Sabiendo esto, indique la relación

entre las constantes catalíticas (Kcat) para ambos

casos:

a) Kcat (II) es menor que Kcat (I).

b) Kcat (II) es igual a Kcat (I).

c) Kcat (II) es mayor que Kcat (I).

d) La relación entre ambas Kcat varía durante el

ensayo.

Respuestas: b.

PREGUNTA 1 A 6 CORRESPONDEN AL

SIGUIENTE ENUNCIADO

Se analiza la cinética de la hexoquinasa frente a dos

sustratos distintos, la D glucosa y la D fructosa.

A continuación se muestra los gráficos de

velocidad inicial (Vo) en función de la

concentración de cada sustrato(S)

Se realiza el ajuste de los datos experimentales

(curvas) a una ecuación del tipo:

Donde S es la concentración de sustrato y

corresponde a los valores de velocidad inicial y A

y B son constantes que surgen del ajuste.

Para glucosa A=1 y B=0,025

Para fructosa A = 1,8 y B = 1

Pregunta 1:

El comportamiento cinético observado en los

gráficos nos permite afirmar que la hexoquinasa:

a) Presenta cooperatividad en la unión de la D

glucosa.

b) Presenta cooperatividad en la unión de la D

fructosa.

c) Presenta mayor velocidad inicial para todas

las concentraciones de sustrato cuando el

sustrato es la D glucosa

d) Presenta una cinética de michaelis menten

para ambos sustratos.

Respuestas: d.

Pregunta 2:

De acuerdo a los datos podemos afirmar que el Km

de la hexoquinasa:

a) Para la D glucosa y la D fructosa son

iguales.

b) Para la D glucosa es de 0,025 mM.

c) Para la D glucosa es de 1 mM.

d) Para la D fructosa es de 1,8 mM.

e) Par la D fructosa es de 0,9 mM.

Respuestas: b.

Pregunta 3:

De acuerdo a los datos podemos determinar cual es

la afirmación correcta respecto a la velocidad

máxima (Vmax) de la hexoquinasa para la D

fructosa y para la D glucosa.

a) Vmáx para D fructosa es de 0,025

mol/min.

b) Vmáx para D fructosa es de 1 mol/min.

c) Vmáx para D glucosa es de 1 mol/min.

d) Vmáx para D glucosa es de 1 mM.

Respuestas: c.

Pregunta 4:

En el ensayo se utiliza un inhibidor en la reacción

de fosforilación de la D glucosa. Cuando se

analizan los resultados se observa que el valor de

Vmáx no cambia y el valor de Km para la glucosa

aumenta. Indique cual es el tipo de inhibición

obtenida:

a) Inhibición competitiva.

b) Inhibición acompetitiva.

c) Inhibición no competitiva.

d) Inhibición irreversible.

e) Modulación alostérica negativa.

Respuesta: a.

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EFICIENCIA CATALITICA,

DEPENDENCIA DEL PH Y DE

LA TEMPERATURA

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REGULACION

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DEFINICION DE ENERGIA

LIBRE

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VARIACION DE ENERGIA

LIBRE Y ACOPLAMIENTO

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DICIEMBRE 2016

JULIO 2017

FEBRERO 2015

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RELACION P/R Y Keq

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G°´ Y G´

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ECUACION DE ENERGIA LIBRE

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Pregunta 42:

En relación a la energía libre de Gibbs, indique cuál de las siguientes afirmaciones

es correcta:

a) En el equilibrio la relación de concentraciones entre productos y reactivos

tiene un valor de 1.

b) Si el S de una reacción es positivo su G también será positivo.

c) El G estándar de una reacción (G°´) es el G de la reacción cuando la

misma está en equilibrio.

d) El G de una reacción es una constante.

e) Toda reacción exergónica se produce espontáneamente.

Respuestas: e.

Pregunta 5:

¿Cuáles son las condiciones termodinámicas de la siguiente reacción en

equilibrio?:

a) G = Gº`

b) G = 0

c) Keq = 0

d) Keq = 1

e) [A] = [B]

Respuestas: b.

Teniendo en cuenta las siguientes reacciones y sus respectivos Gº`indique el

valor del Gº`de la síntesis de glucosa 1P a partir de glucosa y ATP.

Glucosa + Pi ------ Glucosa 6 P Gº`= + 13,8 Kjoul/mol

ADP + Pi ---- ATP + H2O Gº`= + 30,5 Kjoul/mol

Glucosa 6P -- glucosa 1P Gº`= + 6,7 Kjoul/mol

a) – 51,0 Kjoul/mol.

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b) – 10,0 Kjoul/mol.

c) + 10,0 Kjoul/mol.

d) + 20,5 Kjoul/mol.

e) + 51,0 Kjoul/mol.

Respuestas: b.

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GLUCOLISIS

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PRIMERA REACCION DE LA

GLUCOLISIS

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Página 55 clases83.jimdo.com 096437814

PREGUNTA 46:

En cuando a la regulación de la hexoquinasa y la glucoquinasa (hepática) es

correcto afirmar que:

a) La glucoquinasa es inhibida por la fructosa 1,6 BPF.

b) La hexoquinasa es inhibida por la fructusa 6 fosfato.

c) La hexoquinasa es inhibida por la glucoas 6 fosfato.

d) La hexoquinasa es inhibida por la glucosa 1, 6 bi fosfato.

Respuestas: c.

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SEGUNDA REACCION DE LA

GLUCOLISIS

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Página 57 clases83.jimdo.com 096437814

TERCERA REACCION DE LA

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Página 60 clases83.jimdo.com 096437814

CUARTA REACCION DE LA

GLUCOLISIS

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Página 61 clases83.jimdo.com 096437814

QUINTA REACCION DE LA

GLUCOLISIS

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Página 62 clases83.jimdo.com 096437814

BALANCE DE LA PRIMERA

ETAPA

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Página 63 clases83.jimdo.com 096437814

NAD+ Y NADH

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Página 64 clases83.jimdo.com 096437814

SEXTA SEMANA

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Página 66 clases83.jimdo.com 096437814

SEPTIMA REACCION

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OCTAVA Y NOVENA

REACCION

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DECIMA REACCION

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DESTINOS AEROBIOS Y

ANAEROBIOS DEL PIRUVATO

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EXAMEN JULIO 2017

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EXAMEN FEBRERO 2017

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EXAMEN DICIEMBRE 2016

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BALANCE DE LA GLUCOLISIS

AEROBIA Y ANAEROBIA

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EXAMEN JULIO 2017

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EXAMEN JULIO 2017

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FERMENTACION LACTICA

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FERMENTACION

ALCOHOLICA

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ENTRADA DEL PIRUVATO A

LA MITOCONDRIA

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DESCARBOXILACION

OXIDATIVA DEL PIRUVATO

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EXAMEN JULIO 2017

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EXAMEN JULIO 2017

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EXAMEN DE JULIO 2017

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RELACION ENTRE CICLO DE

KREBS Y METABOLISMO

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PRIMERA REACCION

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SEGUNDA REACCION

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TERCERA REACCION

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CUARTA REACCION

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QUINTA A OCTAVA

REACCION

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BALANCE

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TRANSFERENCIA DE

ELECTRONES

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POTENCIALES DE REDUCCION

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