How could you modify a reaction to reduce the effects of a c

How could you modify a reaction to reduce the effects of a competitive inhibitor? Why would bacterial production of B lactate result in drug resistance? What is the stock concentration of Nitrocefin in uM used in lab today?

Solution

2) A competitive inhibitor has structural similarity to the original substrate and it binds to the active site of enzyme but don’t not produce product. It competes with the substrate to bind the active site of enzyme and that’s why named so. It decreases the free active sites of enzymes and reduces the ultimate rate of product formation. But enzyme still able to catalyse the reaction on substrate molecules that come in contact with an active site.

A more substrate to inhibitor ratio can reduce the effect of completive inhibition effect. More substrate will compete with inhibitor to get the active site and the effect of inhibitor to be reduced.

3) Beta-lactamases are enzymes also known as penicillinase are produces by certain bacterial species. Certain antibiotics contain beta-lactam ring (eg. penicillins, cephamycins, and carbapenems etc.) are degraded by beta-lactamases. Such bacteria survive in presence of antibiotics and leads to antibiotic resistance.

4) Nitrocefin is used to detect beta-lactamase enzymes produced by beta-lactam resistant bacteria. Nitrocefin is soluble in DMSO. Stock solution used in labs is 10.0 mg/mL

10mg/ ml =19361 micromoles (µM)

[Solution:

Molecular weight of Nitrocefin =516.5

Mass (g) = Concentration (mol/L) x Volume (L) x Molecular Weight (g/mol)

10mg = Concentration (mol/L) x 1ml x 516.5

Concentration (mol/L)= 10mg/ 516.5 x 1ml

Concentration (mol/L)= 10mg/ 516.5

Concentration (micromole/L)= 10*10⁶/516.5

Concentration (micromole/L)= 19361 ]