True

False

Temperature is 37 Celsius

Substrate in excess

Presence of activators

Optimum pH

Bind to the active site and inhibit the enzyme

Bind to the allosteric site and inhibit the enzyme

Losing the enzyme-substrate complex by binding at the active site

Product bind with the substrate to reduce the reaction

Increased

Decreased or slowed

Stopped

Reversed

60°C

25°C

37°C

100°C

Increase the mobility of molecules to move faster.

Increase the number of molecules to have sufficient energy to pass over the energy barrier

Lower the activation value to form product faster

Change in the ionization state of substrate or enzyme

True

False

Alkaline phosphatase

Trypsin

Salivary amylase

Phenylethanolamine-N-methyl transferase (PNMT)

It is the Michaelis-Menten Constant

Measure the affinity of the enzyme

towards the substrate

The unit is Moles/Litre same with [Substrate]

Low Km, High affinity of the enzyme towards the substrate and vice versa

True

False

The y-intercept shows the value of V_max

The gradient shows the

enzyme concentration

The x-intercept shows the value of K_m

This graph is also called the Double Reciprocal plot graph.

It is converted to a straight line graph.

$V_o\ =\ \frac{V_{\max\ }+\ \left[S\right]}{K_m\ +\ \left[S\right]}$

$V_o\ =\ \frac{V_{\max\ }\left[S\right]}{K_m\ +\ \left[S\right]}$

$V_o\ =\ \frac{V_{\max\ }\left[S\right]}{K_{m\ }\left[S\right]}$

The rate breakdown of ES equals the rate formation of the ES complex.

[S] is very high compared to [E]. So all enzymes can bound to substrate and form ES complex.

Little accumulation of product [P]. So the formation of ES from E+P is negligible.

The enzyme must have a low K_m value. So the enzyme can bind to the substrate easily.

Total [E] in the system

Initial reaction activity of the enzyme

The number of substrate molecules converted to product per unit time.

The affinity of the enzyme throughout the reaction.

Because low [S] means little amount so it is easier for the enzyme to bind with the substrate.

Because low K_m shows high affinity towards substrate so even [S] is low, it still can be activated.

Because low K_m means low [E], so low [E] can easily bind with low [S].

Because enzyme with high [E] need is activated only when there is high [S] in the system.

High [S] is used so that the initial reaction rate is proportional to the [E]

The appearance of P or the disappearance of S is often measured by the change in absorbance using a spectrophotometer.

Low K_m of the enzyme is used so that the initial reaction can be activated easily.

The enzyme reaction is measured under the optimal pH and temperature condition per unit time.

Hexokinase and Amylase

G6PD and G6P

Hexokinase and Aldolase

G6P and Hexokinase