UNIT#07 ENZYMES Flashcards
If enzymes stop their functions, then biochemical reactions would:
Be slowed downs
All of the following are true or an enzyme except:
Increase the energy of activation
Enzymes catalyze all of the following except:
Breathing
The lower the activation energy, the ____ the reaction will be:
Faster
Most of the enzymes are:
Attached wiht organelees
Enzymes related to fatty acids oxidation are present in/at:
Mitochondria
(Fatty acid metabolism)
Al enzymes are ____.
Globular proteins
The reactants on which enzymes work are:
Substrates
What is true about enzymes?
No effect on the end product
The main difference between catalysts and enzymes is:
Catalysts are inorganic while enzymes are organic in nature
The type of energy reduced by the enzymes for biological reactions to occur is called the:
Activation energy
It is false about enzymes:
➡All enzymes require a co-factor for proper functioning✅
➡Only a small amount of enzymes is required❌
➡THey work in vitro as well as in vivo conditions❌
➡They lower activation energy❌
Biochemically enzymes are:
(all enzymes are globular)
Proteins
All enzymes are proteins:
Globular
Three-dimensional globular protein is:
Enzymes
Which of the following is NOT a globular protein?
Increases the rate of reaction
Enzymes involved in cellular respiration are found in:
Mitochondria
Which of the following is an example/s of enzymes attached to membrane systems inside the cell in a specific and orderly arrangement?
➡Mitochondira
➡Chloroplast
The reaction will proceed faster if the activation energy is?
Low
The energy required to start a reaction is called?
Activation energy
An enzyme that requires a biological change in order to become active is called?
Zymogen
AN enzyme without its cofactor is called:
Apoenzyme
If the non-protein part of the enzyme is covalently bonded to the enzyme it is known as?
Prosthetic group
Small organic, the non-protein part that helps in enzyme reactions:
Co-factor
An activated enzyme made up of a polypeptide with its cofactor is:
Holoenzyme
Nicotinamide adenine dinucleotide is an example of:
Co-enzyme
Co-enzyme requires:
Vitamins
Which of the following form weak linkage with an enzyme?
Co-enzyme
Co-factors are divided into groups:
3
The substrate binds to a specific region of an enzyme called?
Active site
All enzymes are:
Globular proteins
What does the active site of the enzyme determine?
Determines by its structure the specificity of an enzyme
Enzymes showing substrate specificity are specific to how many substrates?
1
Which term is used to refer to an inactive enzyme precursor?
Zymogen
Catalysts that increase the rate of biological chemical reactions are called?
Enzymes
Which of the following best describes a co-enzyme?
Loosely bonded non-protein part of an enzyme
Which statement about enzymes is incorrect?
➡Some of them consist solely o protein with no non-protein part❌
➡They catalyze a chemical reaction without being utilized❌
➡They without their cofactor are called apoenzyme❌
➡All enzymes are fibrous proteins ✅
The active form of an enzyme:
holoenzyme
A cofactor made of inorganic on which is detachable is called
Activator
Enzymes are globular proteins because
They have a tertiary structure
A small organic, non-protein molecule that carries chemical groups between enzymes are:
Co-enzyme
Biological molecules which catalyze a biochemical reaction and remain unchanged after completion of the reaction are called:
Enzymes
Enzymes bind with chemical reactants known as:
Substrate
Which of the following vitamin acts as a coenzyme
➡Vitamin B
➡Vitamin B2
If the non-protein part of the enzyme is covalently bonded to the enzyme it is known as?
Prosthetic group
The enzyme reacts with the substrate to form:
Product
Enzymes are ____ in nature:
Proteins
Which type of bond is never formed when the substrate fits into the active site of the enzyme
Hydrophobic interaction
The mechanism of enzyme activation is referred to as:
Catalysis
The specificity of enzyme structure depends upon:
Active site
The catalytic activity takes place at:
Active site
Which statement about the active sites is not true?
➡Acitve site is a spherical shape❌
➡Active site is non-specific✅
➡Active site contains few amino acids❌
➡Active site converts the substrate into product❌
Type of bond present between enzyme and prosthetic group:
Covalent
Which one forms the raw material for coenzymes?
Vitamins
The reaction takes place in a small part of the enzyme is called:
Active site
Coenzymes are closely related to;
Vitamins
The atoms, groups of atoms and molecules that join with enzymes that alter their shape and make them functional
Co-factors
If the cofactor is a non-protein like a metallic ion, it is referred to as a:
Activator
(Metallic ion)
The non-protein part which is organic in nature and detachable is called:
Coenzyme
The function of succinate dehydrogenase is aided by:
FAD+
Prosthetic groups are:
Organic molecules
All coenzymes are derived from:
Vitamins
A co-factor tightly bound to the enzyme on a permanent basis is called:
Prosthetic Group
An enzyme is required Mg+2 to catalyze the substrate. The Mg+2 is the best identified as:
Activator
Which of the following comprises inorganic ions?
Activators
A non-protein part essential for the proper functioning of the enzyme is called:
Co-factor
An enzyme that is non-protein in nature:
Peptidyl transferase
➡Ribozyme(made up of RNA)
An enzyme and substrate react through definite charge-bearing sites.
Active site
The active site of an enzyme:
Determine by its structure, the specificity of the enzyme
The specificity of the enzyme is due to its _____.
Configuration
The lock and key model was proposed by:
Emil Fischer
According to the Lock and Key model, the active site is:
Rigid structure
The lock and key model of enzyme action were proposed by:
Emil Fischer
The complex that forms when a substrate binds to the enzyme is called;
Enzyme-substrate complex
Who proposed the lock and key model of enzyme activity?
Emil Fischer
In the lock and key model of enzyme activity, the substrate acts as the;
Lock
Do enzymes work by which of the following?
Reducing the activation energy
How many models are present for enzyme-substrate complex or reaction?
2
Which statement is incorrect about the lock and key model?
➡Specific enzyme can transform only a specific substrate❌
➡Ative site of an enzyme is a non-flexible structure❌
➡Active site does not change before during or even after reaction❌
➡It explains the mechanism of every chemical reaction✅
Which types are never formed when a substrate fits into the active site of an enzyme?
Covalent linkages
Koshland in 1959 proposed the modified form of which the following?
Induced fit model
The induced fit model was introduced by Koshland in which of the following year?
1959
The lock and key model was proposed by:
Fischer
Which of the following is false concerning enzymes?
Enzymes increase both the forward rate and reverse rate of a reaction
A number of substrate molecules converted into the product by one molecule of enzyme active site per unit time is called:
Turnover number
According to the induced fit model, what happens when an enzyme-substrate complex is formed?
The contact between the substrate and the enzyme causes a change in the shape of the active site
What effect do enzymes have on the activation energy of a reaction?
Decrease
While bound to the active site, the substrate is converted into which of the following?
Product of reaction
The primary function of co-factors is to?
Assist in enzyme activity
In enzyme catalytic reaction the substrate is first converted to a high energy state called?
Transition state
Allosteric enzymes consist of multiple:
Polypeptide chains
The function of enzymes includes all of the following:
Shifting substrates into more favourable positions in the active site
ES complex is converted into the product by:
Catalytic site
____ suggested that each enzyme had a particular shape into which the substrate fits exactly.
Amil Fischer
Allosteric enzymes have ____ major sites.
2
According to the ____ model, the active site of the enzyme is modified as the substrate interacts with the enzyme.
Induced fit model
A modified form of the Lock and model was proposed by:
Koshland
According to Lock and Key model, the enzymes acts as:
Key
The working of sucrase and maltase can be explained by:
Lock and Key Model
With the increase of enzyme concentration in a reaction, more ____ is/are available for the substrate.
Binding sites
The lock and key model for enzyme action proposed by Emil Fischer suggest that:
Enzymes are restricted to one reaction type
The effect of a reversible competitive inhibitor can be neutralized by increasing the concentration of:
Substrate
If the concentration of the substrate molecule is higher than the enzymes then the rate of reaction would be:
Remain constant
Optimum pH of enterokinase is:
Slightly acidic
(pH= 5.50)
Which of the following properties of amino acids is affected by a change in pH?
Ionization of amino acids
Change in tempertue from 30C to 40 C in human body will cause:
First increase then decreases the rate of reaction
Which of the following factor does not affect the rate of enzyme acton?
Light intensity
Which one of the following is the optimum pH of pancreatic lipase enzyme?
➡7.60=Catalase
➡9.00=Pancreatic Lipase
➡8.00=Chymotrypsin
➡9.70=Arginase
The temperature that promotes the maximum activity of enzyme is referred as:
Optimum Temperature
Which type of bond is mostly affected in an enzyme molecule when there is pH fluctuation?
Ionic Bonds
Most enzymes have an optimum temperature of around:
40C
Enzymes which require optimum temperature to be lower than 37C for their proper functioning are present in:
Testes
(Spermatogenesis takes place at 35C)
Which of the following statement is correct?
All enzymes in human body work at same temperature but different pH
Bond sensitive to change in temperatre and pH are respectively:
➡Hydrogen (Temperature)
➡Ionic (pH)
The tempeature where inactive enzyme becomes active is called:
Minimum Temperature
The rate of an enzyme-controlled reaction increases rapidly if the amount of enzyme is doubled in the presence of an unlimited substrate concentration. This is due to:
Number of active sites increase
THe optimum tempearture for enzymes to work at maximum rate in human is:
37C
Enzymes lower down the energy of:
Activation
Optimum pH for pepsin is:
2.00
4.50 is the optimum pH value for the enzyme:
Sucrase
Optimum pH for sucrase is:
4.50
Optimum pH for enterokinase enzyme is:
5.50
Salivary amylase acts best at pH:
6.8
The enzyme with optimum pH=7.60 is;
Catalase
The optimium pH of pancreatic lipase is:
9.0
The optimum pH for enzyme arginase is:
9.70
A little change in pH may lead to:
Ionization of active site of an enzyme
Extreme changes in pH cause the bonds in the enzyme to break, resulting in the enzyme:
Denaturation
Upon increasing the temperature the shape of enzyme’s active site?
Denatures
The optimum pH for enzyme arginase is which of the following?
9.7
The optimum pH for the function of the enzyme pepsin is?
2
If we add more substrate to an already occurring enzymatic reaction and it has no effect on the rate of reaction, the process is called?
Saturation
pH of salivary amylase is:
6.8
It works in acidic medium
Enterokinase
Extreme chagne in pH results in which of the following?
Denaturation of the enzyme
What is meant by optimum temperature of an enzyme?
The tempertature at which an enzyme makes the maximum amount of product
Rate of reaction is double for rise of every _____.
10C
Which of the following strategies of enzymatic inhibition is used by noncompetitive inhibitors?
Bind to an allosteric site to cause a conformational shift in the enzyme
If more substrate to an already occuring enzymatic reaction is added more enzyme activity is seen because:
There is probably more substrate present than there is an enzyme
The optimum pH for the functioning of pancreatic lipase is?
9
A researcher has designed a new type of inhibitor that binds at the active site of an enzyme. What type of inhibition does this molecule display?
Competitive inhibition
Which of the following changes could lead to loss of enzymatic function?
Increase in pH of the reaction
Which statement correctly describes why enzyme activity increases with increased enzyme concentration?
Collisions between enzyme and substrate molecules because more active sites are available
The rate of reaction enzyme directly depends upon which of the following?
Amount of enzyme present at a specific time at an unlimited substrate concentration
The enzyme-substrate complex is formed in which part of the enzyme molecule?
Binding site
Which step, causes activation of the catalytic site of an enzyme?
Formation of enzyme-substrate site
If the concentration of enzyme is kept constant and the amount of substrate is increased a point is reached where an increase in substrates concentration does not affect the reaction rate because of:
All the active sites on the enzyme molecule are occupied
What is the optimum temperature for working enzymes in the human body?
37C
In an acidic medium, amino acids carry a positive charge and act as:
Base
If we increase the pH then, enzyme reactivity is retarded due to:
The tertiary structure of the enzyme is destroyed
When we increase the concentration of substrate then an increase in the enzyme activity is due to which of the following?
It is a sufficient concentration of enzyme
At low enzyme concentration, optimum pH and temperature, the rate of reaction can be increased by:
Increasing enzyme concentration
The number of substrate molecules converted into the product by one molecule of enzyme active site per unit is called
Turn over number
The competitive inhibitors have structural similarities with:
Substrate
Which of the following type of inhibitor can be neutralized by adding more substrate into the reaction?
Reversible inhibitor
If a molecule can bind to another site of the enzyme rather than the true active site, it is referred to as:
Non-Competitive inhibitors
What is common in both competitive and non-competitive inhibition?
Reversible inhibition
A student of chemical engineering mistakenly engulfed the toxic compound “A” which was a potent inhibitor of certain enzymes. He was immediately brought to the hospital where the doctor injected intravenously substrate “B” to minimize the toxic effect of compound A. His life was saved from serious damage. The treatment method shows that compound A was a ____ inhibitor.
Competitive Reversible
Penicillin, an antibiotic inhibits bacterial growth. It is characterized as:
Irreversible inhibitors
Which of the following is not an inhibitor of enzymes?
Sucrose
Heavy metal ions that act as inhibitors (mercury, silver and copper) break ____ in enzymes.
Disulphide bridges
Poisons like cyanide, antibiotics and some drugs are examples of:
Inhibitors
The inhibitors that bind tightly and permanently to enzymes and destroy their globular structure stopping their catalytic activity are:
Irreversible inhibitors
The type of inhibition in which the inhibitor has no structural similarity to the substrate and combines with the enzyme at other than the active site is called:
➡Non-competitive
➡Reversible inhibition
Enzyme succinate dehydrogenase converts succinate into:
Fumarate
The effect of a competitive inhibitor on enzyme activity is such that it affects which of the following?
Decreases enzyme activity
What is the characteristic of a non-competitive inhibitor?
Adding more substrate does not reduce the effects of inhibition
Do reversible inhibitors form weak linkages with which of the following?
Enzyme
Inhibitors which block the enzyme by forming weak bonds are called:
Competitive inhibitors
Do reversible inhibitors form weak linkages with which of the following?
Enzyme
The end product of an enzymatic reaction inhibits the formation of the product in an earlier step. This type of enzymatic regulation is known as:
Feedback Inhibition
In incompetitive inhibition, the inhibitor binds with:
Enzyme
In mixed inhibition, the allosteric effects:
Shape of enzyme
The non-substrate molecules that bond to the allosteric sites are called?
Inhibitors
A chemical substance which can react (in place of the substrate) with the enzyme but is not transformed into a product/s and thus blocks the active site temporarily or permanently is called?
Inhibitor
Malonic acid is an example of which type of inhibitor.
Competitive Inhibitors
In non-competitive inhibition, the quantity which remains the same as the reaction proceeds are?
Km
A substrate which binds at the active site of the enzyme but does not result in the formation of the products is called:
Competitive inhibitor
An inhibitor is added, disrupting the function of a particular enzyme. The experimenter adds more substrate, and enzyme function increases again. These results indicate the involvement of what type of inhibitor?
Competitive
What is meant by enzyme denaturation?
➡Peptide bonds between amino acid residues are broken
➡The enzyme loses its secondary structure
➡The enzyme loses its tertiary structure
✅All of the above
The effect of a competitive inhibitor on enzyme activity is such that it affects which of the following?
Decreases enzyme activity
The non-substrate molecules that bind to the allosteric sites are called?
Inhibitors
Which of the following best describes competitive inhibitors?
Resemble structurally with the substrate
____ is a competitive inhibitor of succinic dehydrogenase.
Malonic acid
In competitive inhibition, a thing that binds to the enzyme active site is?
Inhibitors
Feedback inhibition in most metabolic pathways involves which type of enzymes?
Allosteric enzymes
These form weak linkages with enzymes:
Reversible inhibition
In uncompetitive inhibition, the inhibitor bonds with:
ES Complex
An allosteric enzyme will have:
Many binding sites
In mixed inhibition, the inhibitor binds to:
Allosteric site
Competitive inhibitors ____ enzyme activity.
Decrease
The structure of the enzyme is altered by:
Non-Competitive inhibitor
In competitive inhibition, two things attached to the enzyme’s active site are:
Substrate
The structure of an enzyme is altered by which of the following inhibition?
Irreversible inhibitor
Do phosphatases belong to which group of the following?
Hydrolases
Cytochrome oxidase is categorized in:
Oxidoreductases
Conversion of glucose 6-phosphate into fructose 6-phosphate is done by:
Isomerases
A statement that is not correct about enzymes;
➡They increase the rate of reaction❌
➡They contaminate end product✅
➡They lower the activation energy❌
➡They cannot start chemical reactions❌
When apoenzyme is separated from its metal compoenent, its activity is:
Lost
Synthesis of enzymes takes place by:
Translation
This is the core of induce fit model which distinguishes it from lock and key model
Change in enzyme
Which of the following is common between Lock and Key model and Induce Fit model?
Enzymes are specific in nature
Extreme changes in pH cause denaturation of enzyme by breakign:
Ionic bond
After a certain limiting concentraion of substrate, increasing the concentration of enzyme two times, rate of reaction will:
Remain constant
Their effect can be neutralized completely or partly by an increase in the concentration of substrate;
Reversible competitive
In an enzyme controlled chain reaction, if concentration of initial substrate is increased then it will cause:
Precursor activation
The enzyme needed in biological systems for joining two molecuels is called;
Ligases
Cofactors are;
➡Prosthetic groups
➡metallic ions
➡Co-enzymes
In eukaryotes, enzymes are mostly
Bound to organelles
Synthesis of enzymes takes place by;
Translation
The catalytic activity of an enzyme is restricted to a small portion of the structure known as:
Active site
An enzyme and its substrate react with each other through a definite charge bearing site called;
Active site of enzyme
If any factor alters the chemistry and configuration of an enzyme, it will probably be:
➡Temperature
➡pH
➡Inhibitor
The rate of reacton depends directly on the amount of enzyme present at a specific time at;
Unlimited substrate concentration
Their effect can be neutralized completely or partly by an increase the concentration of substrate;
Reversible competitive
In Krebs cycle, malonic acid blocks succinic dehydrogenase thorugh;
Reversible competitive inhibition
They occupy the active sites by forming covalent bonds;
Irreversible inhibitors
Any agent which reduces/slows down or stops the rate of reacton of enzymes is termed as
Inhibitor
In an enzyme controlled chain reaction, if concentraion of initial substrate is increase then it will cause;
Precurosr activation
In feedback inhibition, a metabolic pathway is switched off by:
Accumulation of end product
Amylase is an example of ;
Hydrolase
The enzymes catalyzing re-arrangement of atomic grouping without altering molceular weight or number of atom is;
Isomerases
The enzyme needed in biological systems or joining two molecules is called:
Ligases
Which of the following is more specific?
➡Lactase✅
➡Pepsin❌
➡Trypsin❌
➡Lipase❌
Which of the following is an example of a coenzyme?
FAD+ in Krebs cycle during succinate conversion to fumarate
The optimum pH for working of pancreatic lipase is:
9.00
Phosphorylation of glucose is done by:
Kinase
An enzyme which catalyzes different substrates into single product:
Hexokinase
ATP binds to ____ of phosphofructokinase:
Allosteric site
The temperature where an inactive enzyme becomes active again is called:
Minimum Temperature
Changing the pH from optimum results in:
Decrease in rate of reaction
Which of the followings is not an inhibitor of enzymes?
Maltose
Which enzyme can digest the following molecule?
➡Amylase❌
➡Pepsin❌
➡Lipase✅
➡Lactase❌
A protein that is not an enzyme:
➡Isomerase❌
➡Rennin❌
➡Prolactin✅
➡Maltase❌
The active site of an enzyme:
Determines by its structure the specificity fo the enzyme
Which of the following is the features of the enzymes:
➡Non-Crystalline❌
➡Spindle Shape❌
➡Soluble in aqueous medium✅
➡Fibrous Shape❌
The essential chemical components of many coenzymes are:
Vitamins
Select the option which is not correct with respect to enzyme action:
➡The addition of succinate does not reverse the effect produced by malonate✅
➡Malonate is a competitive inhibitor o succinate dehydrogenase❌
The specificity of enzyme was first proposed by:
E. Fischer
The temperature, where an inactive enzyme becomes active again, is called:
Minimum Temperature
All enzymes follow the induced fit model except:
➡Carbonic anhydrase❌
➡Allosteric Enzymes❌
➡Hexokinase❌
➡Urease✅
Cyanides are potent poisons for the living organisms because they can kill by inhibiting ____, essential for cellular respiration.
Cytochrome Oxidase
Penicillin control bacterial infection by:
Reversible Non-Competitive
Which one of the following is called biological catalysts?
Enzymes
The active site of enzymes consists of:
Only a few amino acids
_______ maintains the globular structure of the enzyme
The bulk of amino acids
Often it contributes directly to the chemical reactions which bring about catalysis:
Co-Factor
If the non-protein part of the enzyme is covalently bonded to the protein part, it is called
Co-Enzyme
An activated enzyme consisting of polypeptide chain and a cofactor is known as:
Holoenzyme
Enzymes are sensitive to even a minor change in:
➡pH
➡Temperature
➡Substrate COncentration
________ is a powerful protein digesting enzyme and is capable of destroying a cell’s internal structure and thus produced in inactive ________ form by the cell
Pepsin, Pepsinogen
After the formation of products, it is released unaltered and thus can be used again:
Enzyme
Enzymes involved in some metabolic pathways are normally present together:
In precise order
The charge and shape of the active site of the enzyme is formed by _______ in the polypeptide chain of the active site of the enzyme.
Some amino acids
The reaction between _______ activates the catalytic site of the enzyme
Substrate and Binding site of the enzyme
According to this model enzyme is a rigid structure:
Lock and Key Model
According to ________ the active site of enzyme is not a rigid structure
Induced Fit Model
The functional specificity of every enzyme is the consequence of its:
Specific chemistry and Cofiguration
The rate of reaction depends directly on the amount of enzyme provided the substrate concentration is
Unlimited
By increasing the enzyme molecules ________ will convert the substrate molecules into products, in the given period of time.
More active sites
If the enzyme conc. is kept constant, by increasing the substrate concentration the rate of enzyme action is
Increased or specific time
The rate of enzyme-controlled reactions may increase with the increase in:
Temperature up to optimum level
Chemical reactions are accelerated at high temperature because
Heat provides the activation energy
When reactants move more quickly and chances of their collision with each other are increased as a result the rate of enzyme-controlled reactions will?
Increase Initially
Inhibitors can be divided into:
Two basic types
They alter the structure of the enzyme in such a way that even if genuine substrate binds the active site, catalysis fails to take place temporarily:
Non-Competitive Inhibitors
Pick up the product:
➡Succinic Acid❌
➡Malonic Acid❌
➡Fumaric Acid✅
➡Dehydrogense❌
Succinic acid dehydrogenase + malonic acid ➡
No reaction possible, Enzyme is blocked
Which one of the following is reused?
Enzyme and Co-enzyme
Some enzymes are potentially damaging if they are manufactured in their active form e.g.
Pepsin
Which one of the following products will
control this pathway through feedback
activation?
A➡B➡C➡D➡E
E
Which one of the following products will control this pathway through feedback action
A➡B➡C➡D
E
A➡B➡C➡D➡E
Accumulation of “E” will control the above pathway through:
Feedback Inhibition
A➡B➡C➡D➡E
A deficiency of “E” will control the above
pathway through:
Feedback activation
Induce fit model was proposed by
Koshland
Salivary amylase works best at pH:
6.80
Optimum pH for the action of pancreatic lipase is:
9.00
Malonic acid is competitive inhibitor of:
Succinic Dehydrogenase
It causes denaturation of globular structure of enzyme:
Extreme pH change
Any molecule that increases the rate of a chemical reaction without being used up during that reaction is called:
Catalyst
Enzymes are not synthesized in:
Viruses
Enzymes enhance the rate of reaction by:
Lowering the activaton energy of the reaction
Which enzyme hydrolyses internal phosphodiester bonds in a polynucleotide chain?
Endonuclease
Which one of the following statements regarding enzyme inhibition is correct?
Competitive inhibition is seen when substrate and inhibitor compete
A competitive inhibitor of succinic dehydrogenase is:
Malonic acid
Enzymes often have additional parts in their structures that are made up of molecules other than proteins. When this additional chemical part is an organic molecule, it is called:
Co-Enzyme
The lipid synthesizing enzymes are present in:
Smooth ER
The term apoenzyme is applicable to:
Protein part of conjugate enzyme
Enzymes:
Enzymes generally have:
Different pH but same optimum temperature
Koshland’s model of enzyme action is known as:
Induced Fit model
Enzymes having slightly different molecular structure but performing identical activity are:
Isoenzymes
Which factor is responsible for the inhibition enzymatic process during feedback
End Product
One which is not an inhibitor:
Metabolites
Some of the enzymes, which are associated with converting fats into carbohydrates, are present in:
Glyoxysomes
Any molecule which acts directly on an enzyme to lower its catalytic rate is called:
Inhibitor
Which of the following statements is true regarding enzyme inhibition?
➡It may be reversible or irreversible
➡Reversible can be competitive or noncompetitive
The effect of a reversible competitive inhibitor can be nullified by:
Increasing the substrate concentration
The ____ acts as a “bridge” between the enzyme and its substrate.
Co-Factor
One which is inorganic in nature:
Activator
The following is a substrate-specific enzyme:
➡Pepsin❌
➡Protease❌
➡Lipase❌
➡Sucrase✅
Regarding the nature of enzymes, which one is correct?
They are specific both in their nature and action
Regarding enzyme molecules:
Greater in size than the substrate
The temperature at which enzymes can work at their maximum rate is called ____ temperature.
Optimum
The optimum pH for enterokinase is:
5.50
Which of the following does not work on an acidic medium:
Arginase
An enzyme and substrate react through a special feature or site present in an enzyme known as:
Active Site
Enzymes increase the rate of reaction by:
Decreasing activation energy
The non-protein part of enzyme which is covalently bonded is called:
Prosthetic Group
Most vitamins are
Co-Enzymes
Which of the following is a co-factor?
➡Calcium Ions
➡Copper Ions
➡Manganese ions
Co-Enzymes combine with:
Apoenzyme
The non-competitive inhibitor is one that:
Binds away from the active site of an enzyme
The shape of enzyme molecule is:
Globular
The protein cytochrome c functions only when it contains an atom of iron. Which term describes the atom of iron?
Part of a prosthetic group
