Description : The chemical forces that bind most coenzymes and substrates to enzymes such as LDH are (A) Hydrogen bonds (B) Peptide bonds (C) Coordinate bonds (D) Covalent bonds
Last Answer : Answer : D
Description : Give some examples of co-enzymes involved in oxidoreductases.
Last Answer : NAD, NADP, FAD.
Description : Which of the following is not true regarding enzymes? (A) They catalyze only a particular type of reaction (B) They remain active even after separation from the source (C) They are destroyed ... They are irreversibly destroyed at high temperature (E) Their activity depends on the pH of the solution
Last Answer : Answer : C
Description : Isoenzymes can be characterized by (A) Proteins lacking enzymatic activity that are necessary for the activation of enzymes (B) Proteolytic enzymes activated by hydrolysis (C) Enzymes with identical primary structure (D) Similar enzymes that catalyse different reaction
Last Answer : Answer : B
Description : Hydrolytic enzymes which act on low pH are called as (a) proteases (b) α-amylases (c) hydrolases (d) peroxidases.
Last Answer : (a) proteases
Description : Enzymes leading to the high energy phosphorylation of substrates during glycolysis include which of the following? (A) Phosphoglycerate kinase (B) Enolase (C) Pyruvate Kinase (D) Glyceraldehyde-3-phosphate dehydrogenase
Description : Identify the wrong statement with regard to restriction enzymes. (a) Each restriction enzyme functions by inspecting the length of a DNA sequence. (b) They cut the strand of DNA at palindromic sites. (c) They are useful in genetic engineering. (d) Sticky ends can be joined by using DNA ligases.
Last Answer : d) Sticky ends can be joined by using DNA ligases.
Description : The cutting of DNA at specific locations became possible with the discovery of (a) selectable markers (b) ligases (c) restriction enzymes (d) probes.
Last Answer : (c) restriction enzymes
Description : Explain enzymes with the type of reaction they catalyse. -Biology
Last Answer : answer:
Description : Write the enzymes which catalyse the conversion of pyruvic acid to `CO_(2)` and enthanol
Last Answer : Write the enzymes which catalyse the conversion of pyruvic acid to `CO_(2)` and enthanol
Description : An example of lyases is (A) Glutamine synthetase (B) Fumarase (C) Cholinesterase (D) Amylase
Description : What is the function of lyases?
Last Answer : Cleave bond without adding water.
Description : Hexokinase (Glucose + ATP → Glucose-6– P + ADP) belongs to the category: (A) Transferases (B) Lysases (C) Oxidoreductases (D) Isomerases
Description : What is the function of oxidoreductases?
Last Answer : Transfer of hydrogen.
Description : Pick out the wrong statement. (A) Catalytic activity of enzyme catalysed reactions which is affected by temperature, pH value & chemical agents, is maximum at a temperature of about 45°C ... in enzyme catalysed reactions can be calculated by using the thermodynamic properties of substrates & prod
Last Answer : (C) Enzymes help in increasing the activation energy of the reaction
Description : Digestive enzymes along with their substrates and products. -Biology
Description : Mechanical digestion is the fragmentation of food aided by specialized physical structures, such as teeth, previous to extracellullar digestion. The mechanical fragmentation of food helps digestive ... there are mandibles and chewing muscles to triturate food previous to the chemical digestion.
Last Answer : Concerning extracellular digestion what is meant by chemical digestion?
Description : Organic molecules that increase the rate of metabolic reactions with themselveschangingareknown as A- coenzymes B- enzymes C- substrates D- .reactants
Last Answer : enzymes
Description : An enzyme catalyzes the conversion of an aldose sugar to a ketose sugar would be classified as one of the (A) Transferases (B) Isomerases (C) Oxido reductases (D) Hydrolases
Description : What is the function of hydrolases?
Last Answer : Cleave bond after adding water.
Description : Conversion of pepsinogen to pepsin is (A) Intra molecular rearrangement (B) Breaking of hydrogen bonds (C) Covalent modification (D) Polymerisation
Description : In quaternary structure, subunits are linked by (A) Peptide bonds (B) Disulphide bonds (C) Covalent bonds (D) Non-covalent bonds
Description : An example of ligases is (A) Succinate thiokinase (B) Alanine racemase (C) Fumarase (D) Aldolase
Last Answer : Answer : A
Description : What is the function of ligases?
Last Answer : ATP dependent condensation of two molecules.
Description : Regulation of some enzymes by covalent modification involves addition or removal of (A) Acetate (B) Sulphate (C) Phosphate (D) Coenzyme
Description : Activation or inactivation of certain key regulatory enzymes is accomplished by covalent modification of the amino acid: (A) Tyrosine (B) Phenylalanine (C) Lysine (D) Serine
Description : In biotin-containing enzymes, the biotin is bound to the enzyme by (A) An amide linkage to carboxyl group of glutamine (B) A covalent bond with CO2 (C) An amide linkage to an amino group of lysine (D) An amide linkage to α-carboxyl group of protein
Description : In the process of transcription in bacterial cells (A) Initiation requires rho protein (B) RNA polymerase incorporates methylated bases in correct sequence (C) Both the sigma unit and core ... RNA polymerase are required for accurate promotor site binding (D) Primase is necessary for initiation
Description : Which one of the following statements is not characteristic of allosteric enzymes? (A) They frequently catalyze a committed step early in a metabolic pathway (B) They are often composed of subunits (C) They follow Michaelis-Menten kinetics (D) They frequently show cooperativity for substrate binding
Description : 3-β-Hydroxysteroid dehydrogenase and ∆5,4 isomerase catalyse the conversion of the weak androgen DHEA to (A) Androstenedione (B) Testosterone (C) Progesterone (D) Estrone
Description : Bonds formed by the sharing of an electron pair between two atoms are known as - (1) Covalent bonds (2) Ionic bonds (3) Weak bonds (4) None of the above
Last Answer : (1) Covalent bonds Explanation: Bonds which are formed by the sharing of an electron pair between two atoms are known as covalent bonds.
Description : Name the organelle that contains high levels of hydrolases and is responsible for digestion of proteins, sugars, nucleic acids and lipids.
Last Answer : Lysosomes
Description : Enzyme involved in joining together two substrates is (A) Glutamine synthetase (B) Aldolase (C) Gunaine deaminase (D) Arginase
Description : All of the following statements about thioredoxin reductase are true except: (A) It requires NADH as a coenzyme (B) Its substrates are ADP, GDP, CDP and UDP (C) It is activated by ATP (D) It is inhibited by dADP
Description : Lock' and Key' model of enzyme action proposed by Fisher implies that (A) The active site is flexible and adjusts to substrate (B) The active site requires removal of PO4 group ( ... complementary in shape to that of the substrate (D) Substrates change conformation prior to active site interaction
Description : If curve X in the graph (below) represents no inhibition for the reaction of the enzyme with its substrates, the curve representing the competitive inhibition, of the same reaction is (A) A (B) B (C) C (D) D
Description : Fischer's lock and key' model of the enzyme action implies that (A) The active site is complementary in shape to that of substance only after interaction. (B) The active site is ... change conformation prior to active site interaction (D) The active site is flexible and adjusts to substrate
Description : Most amino acids are substrates for transamination except (A) Alanine (B) Threonine (C) Serine (D) Valine
Description : What are those non-carbohydrate sources? (What are the substrates for gluconeogenesis?).
Last Answer : Glucogenic amino acids and lactate.
Description : The active site of an enzyme is formed by a few of the enzymes: (A) R groups of the amino acids (B) Amino groups of the amino acids (C) Carboxyl group of the amino acids (D) Exposed sulfur bonds
Description : If the difference in electronegativity values between two atoms is more than 2.0 non-polar covalent bonds generally form?
Last Answer : At this value an ionic bond is formed.
Description : If the difference in electronegativity values between two atoms is less than 0.4 nonpolar covalent bonds generally form?
Last Answer : True apex:)
Description : The two polypeptides of human insulin are linked together by (a) covalent bond (b) disulphide bridges (c) hydrogen bonds (d) phosphodiester bond.
Last Answer : (b) disulphide bridges
Description : How many covalent bonds does P have?
Last Answer : Need answer
Description : How many electrons in covalent bonds are attracted to the nucleus of just one atom?
Last Answer : No electrons are "attached" to the nucleus of either atom. In acovalent bond one electron from each atom is shared with the otheratom.
Description : Is it true both ionic and covalent bonds between molecules are very strong?
Last Answer : Both ionic and covalent bonds are between atoms.
Description : What combination of atoms form by covalent bonds is called?
Description : Is PCl3 ionic or covalent bonds?
Description : How do covalent bonds and ionic bonds compare?
Last Answer : Covalent bonding involves the sharing of electrons. Ionic bonding involves the transfer of electrons.