BIOLOGY M.C.Q (1 Marks)

Lactose is a disaccharide made up of glucose and galactose.

Antibiotics which contain enzymes do contain protein but many antibiotics may not contain enzymes or protein. Pigments are not proteins.

Iron is found in haemoglobin, sodium and magnesium play important role in some metabolic activities.

Dehydrogenases catalyze dehydrogenation reactions, which involve addition or removal of electrons.
Addition or removal of electrons will lead to reduction or oxidation of substrates.
Dehydrogenases are a type of oxidoreductases.

Esterases are the enzyme which hydrolyse ester linkage.
Hence, esterases belong to class Hydrolase.
Hydrolases are the enzymes catalysing hydrolysis.

Proteins are body building molecules and provide the structural framework for cells.
They are biopolymers of amino acids.
They are the largest physical and chemical components of a cell.
No other biomolecule possesses such immense structural and physiological diversity as proteins.

Erucic acid.

Amylase

Glycogen.

Amino acid sequences within the protein molecule.

Peptidase, amylase, rennin.

Proteins are a very versatile biomolecules performing a variety of structural and functional roles.
Pepsin is a proteolytic enzyme secreted as pepsinogen in the stomach.
Myosin is a protein found in muscle tissue.
Lactogen is milk sugar and casein is milk protein.

Extraction.

Primary structure of a protein is simply the amino acid sequence of it which has two ends the carboxyl and amino terminals.

Purine.

Nucleic acids are long chain polymers of nucleotides.
The nucleotides, in turn, are phosphoric acid esters of nucleosides which mainly consists of a nitrogenous base, Sugar, and phosphate.
The nitrogenous base includes purines and pyrimidines while the sugar contains ribose and deoxyribose sugar. phosphate is formed of phosphoric acid.

Proteins

Guanine is a purine.

Nucleoside.

Fats that are generally liquid at room temperature.

Hydrogen bonds.

Alkaloids.

Succinic dehydrogenase by malonate.

Nucleoside.

Primary structure.

Metabolism.

In cytoplasm as well as in mitochondria.

Carbon, hydrogen, oxygen, nitrogen

Nitrogenase.

Uracil.

End product.

Euchromatin.

End products

Oxygen.

Competitive inhibition is seen when the substrate and the inhibitor compete for the active site on the enzyme.

Deoxyribonucleotides.

Glucose

This question relates to the industrial applications of enzymes.
Alcohol is not produced by the use of nitrogenase.
Nitrogenase performs complex functions of nitrogen fixation by bacteria.
Alcohol is produced by the fermentation process of sugars carried out by Yeast.

Regulating metabolism.

Viruses.

Most of the enzymes are proteins.Proteins are biological macromolecules made up of amino acids joined together by peptide bonds.
Peptidases are enzymes, which cleave or break peptide bonds.
The action of peptidase enzymes will cleave or break peptide bonds, thus breaking the primary structure of enzymes or digestion of enzyme.

Lyases.

Glycosidic bonds are the bonds formed between hemiacetal or hemiketal group of carbohydrates and hydroxyl group of another molecule.
It is a condensation reaction which leads to release of water molecules.

Starch, glycogen, cellulose.

The function of enzymes in the living system is to catalysed biochemical reactions without involving in the reaction.
It means enzymes speed up the rate of reaction by lowering activation energy, so the reaction proceeds faster and at the end same enzymes can are obtained without any changes in it.

Vitamin.

Reduction in activation energy.

Cellulose.

Feedback allosteric inhibition.

Inulin is a polysaccharide made up of glucose and fructose.

Phosphodiester bond.

Ghee.

Insulin is a polysaccharide made up of glucose and fructose.

Glycerol

Basic proteins.

End product

Guanine.

Are polymers of nucleotides.

It is a coloured cell.

Cellulose, Starch, Glycogen.

Glycoproteins.

The minimum amount of energy required to initiate a chemical reaction is called activation energy.

Transamination reaction is the transfer of amino groups from an amino acid to a keto acid.
The enzyme is transaminase.
It helps in formation of different amino acids which are not formed by reductive amination.

Papain is the only protein that is not found in humans.
It is found in plants like papaya and the main function of papain is breakdown of peptide bonds in protein.

One of the common methods of protein denaturation is heat.
For example, boiling of egg denatures egg white.
A denatured protein can no longer perform its normal biological role.

Phosphodiester bonds.

Nitrogen base, sugar and phosphate.

Loosely attached organic part.

When a phosphate group is added to a nucleoside, it becomes a nucleotide.

When substrate binds to the active site of the enzyme, it completes the. reaction. When inhibitor binds to the active site of the enzyme, it blocks the reaction.

Benzene.

All of these.

Proteins.

Myosin

Amino acids and glucose.

These are all proteins.

The term 'zwitterion' comes from a German word which means a neutral molecule with positive and negative charges.

Proteins are polypeptide macromolecules.
They are composed of amino acids joined together with the help of peptide bonds.
If peptide bonds of a protein are cleaved amino acids will be released.
This is exactly what happens during digestion of dietary proteins.
The proteins are hydrolyzed by breaking of peptide bonds and resulting amino acids are absorbed.

Proteinaceous centre and starchy sheath.

Thymidine.

Enzymes are proteins. Enzymes are in general globular proteins.
Like all proteins, enzymes are long, linear chains of amino acids that fold to produce a three-dimensional product.
Most enzymes can be denatured-that is, unfolded and inactivatedby heating or chemical denaturants, which disrupt the three dimensional structure of the protein.
Depending on the enzyme, denaturation may be reversible or irreversible.

Both Assertion and Reason are false.

Cellulose.

In cytoplasm as well as in mitochondria.

Mitochondria and Chloroplast

Glucose.

Succinic dehydrogenase by malonic acid.

Lecithin is a phospholipid.

Nucleotide.

Isoenzymes.

Starch, glycogen, cellulose.

Lowering the activation energy of the reaction.

Reserve materials.

Proteins are body building molecules and provide the structural framework for cells.
They are biopolymers of amino acids.

Phenylalanine.

Lysine.

Lyases.

Arginine.

Enzymes increase the rate of reaction by decreasing the activation energy.

Nucleotide.