Flashcards in Biochemistry Deck (16):

1

## Vmax

### The maximal velocity of a reaction

2

## Km

### The substrate concentration that brings about half Vmax

3

## How can you experimentally determine Vmax?

### Taking the initial velocities of reactions using known substrate concentrations. Then plot the initial velocities against substrate concentration. The point they plataue off at is almost Vmax.

4

## Why is experimentally determing Vmax not effective?

### No matter the substrate concentration- the reactions will never reach Vmax.

5

## What is the original equation for V and what does it get transformed into?

###
V= Vmax[S]/km + [S]

1/V = Km+ [S]/ Vmax[S]

1/v= Km/Vmax[S] + [S]/Vmax[S]

1/v= km/Vmax x 1/{S] + 1/Vmax

y= m x + c

6

## What is the gradient of the lineweaver Burke plot?

### Km/Vmax

7

## What is the y interception?

### Vmax

8

## What is the x interception?

### Km

9

## In competitive antagonism- what changes on the Lineweaver Burke plot

###
Vmax stays the same

Km varies

10

## In non-competitive antagonism- what changes on the lineweaver burke plot?

###
Vmax changes

Km stays the same.

11

## Enzymes can have the same Vmax but different Km's?

### True

12

## A low Km means

### Little substrate is needed to get a half maximal response.

13

## A high Km means

### Lots of substrate is needed to get a half maximal response.

14

## Allosteric enzymes follow the michaelis menten kinetics. True or false

### False

15

## What sort of curve do allosteric enzymes create?

### Sigmoidal

16