Competitive Inhibition
Trending Questions
What is the allosteric inhibitor? Explain with an example.
An enzyme which increases the rate of permeability across the plasma membrane is
Amylase
Catalase
Gelatinase
Permease
- Decrease in Vmax and Km
- Unchanged Vmax and decrease in Km
- Unchanged Vmax and increase in Km
- Increase in Vmax and Km
Key and lock hypothesis of enzyme action was given by
Koshland
Kuhn
Fischer
Buchner
The 'lock and key' model of enzyme action illustrates that a particular enzyme molecule
Forms a permanent enzyme-substrate complex
Reacts at identical rates under all conditions
Interacts with a specific type of substrate molecule
May be destroyed and resynthesised several times
Change of active site, which prevents the binding of substrate to the enzyme and stops the reaction is called
Reverse inhibition
Competitive inhibition
Allosteric inhibition
Non-Competitive inhibition.
What does negative regulation mean?
A protein which lacks a metal is
Glycoprotein
Cytochrome
Ferredoxin
Haemoglobin
- α -ketoglutarte
- Malate
- Malonate
- Oxaloacetate
The passive absorption of minerals requires Ion channels which are proteinaceous in nature. The ion channels are
Transmembrane proteins
Extrinsic proteins
Intrinsic proteins
Both a & c are correct
what are steroids? What is the function of steroids?
Biocatalysts were found accidently in yeast extract by
Pasteur
Buchner
Kuhn
Sumner
- Inhibition of methanol by ethanol
- Inhibition of succinate by malonate
- Cyanide poisoning
- All of these
Statement A: Coenzyme or metal ion that is tightly bound to enzyme protein is called prosthetic group.
Statement B: Transition state structure of the substrate formed during an enzymatic reaction is transient but stable.