
The catalytic efficiency of two different enzymes is compared by their
(A) Product
(B) Molecular size
(C ) Km value
(D) pH optimum value
Answer
569.1k+ views
Hint: Proteins acting as biochemical catalysts are enzymes. Chemical reactions are accelerated by catalysts. The molecules that enzymes can work on are called substrates, and the enzyme transforms the substrates into multiple products known as molecules.
Complete answer:
To occur at speeds high enough to support life, nearly all metabolic processes in the cell require enzyme catalysis. To catalyse individual steps, metabolic pathways rely on enzymes. The study of enzymes is called enzymology, and a new area of pseudo-enzyme research has recently emerged, understanding that certain enzymes have lost the capacity to conduct biological catalysis during development, which is also reflected in their amino acid sequences and peculiar 'pseudo catalytic' properties.
Down proteins into smaller molecules, making the meat easier to chew. It is understood that enzymes catalyse more than 5,000 kinds of biochemical reactions. Some biocatalysts, or ribozymes, are catalytic RNA molecules. The specificity of enzymes derives from their distinctive three-dimensional architectures. Enzymes increase the reaction rate by lowering their activation energy, like all catalysts.
Some enzymes can make their substrate-to-product.
Conversions happen several millions of times faster. Enzymes are chemically like any catalyst and are not consumed in chemical reactions, nor do they change a reaction's equilibrium. By being much more precise, enzymes vary from most other catalysts. Other molecules can influence the function of enzymes: inhibitors are molecules that decrease the activity of enzymes and activators are molecules that increase activity. Enzyme antagonists are various therapeutic medications and toxins.
For practical purposes, Km is the substrate concentration that permits half Vmax to be reached by the enzyme. For its substrate, an enzyme with a high Km has a low affinity and needs a higher substrate concentration to attain Vmax.
Hence the correct answer is ‘option (C)’.
Note: The activity of an enzyme declines markedly above its optimum temperature and pH, and when subjected to extreme heat, many enzymes are (permanently) denatured, losing their structure and catalytic properties. For starters, in the synthesis of antibiotics, certain enzymes are used commercially. Some kitchen goods use enzymes to speed up chemical reactions: enzymes break down protein, starch or fat stains on clothes in biological washing powders, and enzymes break down in meat tenderizers.
Complete answer:
To occur at speeds high enough to support life, nearly all metabolic processes in the cell require enzyme catalysis. To catalyse individual steps, metabolic pathways rely on enzymes. The study of enzymes is called enzymology, and a new area of pseudo-enzyme research has recently emerged, understanding that certain enzymes have lost the capacity to conduct biological catalysis during development, which is also reflected in their amino acid sequences and peculiar 'pseudo catalytic' properties.
Down proteins into smaller molecules, making the meat easier to chew. It is understood that enzymes catalyse more than 5,000 kinds of biochemical reactions. Some biocatalysts, or ribozymes, are catalytic RNA molecules. The specificity of enzymes derives from their distinctive three-dimensional architectures. Enzymes increase the reaction rate by lowering their activation energy, like all catalysts.
Some enzymes can make their substrate-to-product.
Conversions happen several millions of times faster. Enzymes are chemically like any catalyst and are not consumed in chemical reactions, nor do they change a reaction's equilibrium. By being much more precise, enzymes vary from most other catalysts. Other molecules can influence the function of enzymes: inhibitors are molecules that decrease the activity of enzymes and activators are molecules that increase activity. Enzyme antagonists are various therapeutic medications and toxins.
For practical purposes, Km is the substrate concentration that permits half Vmax to be reached by the enzyme. For its substrate, an enzyme with a high Km has a low affinity and needs a higher substrate concentration to attain Vmax.
Hence the correct answer is ‘option (C)’.
Note: The activity of an enzyme declines markedly above its optimum temperature and pH, and when subjected to extreme heat, many enzymes are (permanently) denatured, losing their structure and catalytic properties. For starters, in the synthesis of antibiotics, certain enzymes are used commercially. Some kitchen goods use enzymes to speed up chemical reactions: enzymes break down protein, starch or fat stains on clothes in biological washing powders, and enzymes break down in meat tenderizers.
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