MDCAT BIOLOGY-Enzymes (SMART INSTITUTE)

01-Specificity of an enzyme is determined by:
No. Of sequence of amino acids
Charge on substrate
PH of environment
Charge and shape of active site
02-An activating enzyme consisting of polypeptide chain and a co-factor is called:
Apoenzyme
Coenzyme
Holoenzyme
Proenzyme
03-Activators are usually derived from:
Vitamins
Proteins
Carbohydrates
Metals
04-At a certain point where conversion of substrate/s into product/s is maximum, the enzyme/s would be:
Free
Activated
Denatured
Occupied
05-A three dimensional cavity bearing a specific charge by which the enzyme reacts with its substrate is called:
Active site
Catalytic site
Binding site
Allosteric site
06-Which step causes activation of catalytic site of an enzyme?
Change in pH of enzyme
Change in the shape of substrate
Formation of ES complex
Change in temperature
07-In a naturally occurring chemical reaction, all active sites are occupied, the rate of reaction would be:
Minimum and constant
Maximum and accelerating
Zero and constant
Constant and maximum
08-Excessive increase in temperature of medium causes the enzyme molecule to be:
Activated
Denatured
Unaffected
None of these
09-Inhibitors are chemically
Metals
Inorganic
Organic
All of these
10-Optimum temperature of enzymes present in human body is:
27' C
47' C
37' C
30' C
11-Inhibitors which block the enzyme by forming weak bond are called:
Competitive inhibitors
Non-competitive inhibitors
Reversible inhibitors
Irreversible inhibitors
12-Malonic acid is an example of:
Irreversible inhibitor
Competitive inhibitors
Reversible inhibitor
Non-competitive inhibitor
13-Coenzymes are closely related to:
Hormones
Inhibitor
Antibodies
Vitamins
14-The effect of reversible competitive inhibitor can be neutralized by increasing the concentration of
Substrate
Enzyme
Activator
Inhibitor
15-Function of succinic dehydrogenase is aided by:
NAD
FAD
Metal ion
Vitamin
16-Prosthetic groups are
Metallic ions
Organic molecules
Inorganic molecules
Radicals
17-Optimum pH value of pancreatic lipase:
7.60
8.00
9.00
9.70
18-ES complex is converted into product by:
Cofactor
Catalytic site
Coenzyme
Binding site
19-It is an amino acid and also a part of phospholipid:
Serine
Choline
Ethanol amine
Aspartic acid
20-WOF properties of amino acids is affected by a change in pH?
Oxidation of amino acids
Reduction of amino acids
Atomization of amino acids
Ionization of amino acids
21-Change in temperature from 30' C to 40' C in human body will cause:
Increase in rate of reaction
Decrease in rate of reaction
First increase then decrease in rate of reaction
First increase then become constant
22-Optimum pH of enterokinase is:
Slightly acidic
Slightly basic
Highly acidic
Highly basic
23-The rate of reaction will always be directly proportional to the concentration of enzyme, if
Substrate concentration is limited
Substrate concentration is unlimited
Substrate concentration is constant
Substrate concentration is decreased
24-Enzymes belong to which class of proteins?
Fibrous
Globular
Glycoprotein
Lipoprotein
25-Apoenzyme is:
Protein part of enzyme
Non-protein part of enzyme
Activated enzyme
Co-enzyme
26-Optimum pH of salivary amylase is:
7.60
7.00-8.00
6.8
9.7
27-Allosteric enzymes have ................ Major sites.
1
2
3
4
28-Enzyme after catalysis detaches itself from the product:
Completely
Incompletely
Changed
Unchanged
29 .............. Forms weak linkages with enzymes and their effect can be neutralized completely or partly by an increase in the concentration of substrate.
Only competitive inhibition
Reversible inhibition
Irreversible inhibition
Both reversible and irreversible inhibition
30-The non protein part of enzyme which is covalently and permanently bonded is called:
Prosthetic group
Co-factor
Co-enzyme
Activator
31-Enzymes increase the rate of reaction by:
Increasing temperature
Decreasing pH
Decreasing activation energy
Increasing activation energy
32-An enzyme and substrate reacts through a special feature or site present in enzyme:
Building site
Active site
Catalytic site
Inhibition site
33-If the detachable co-factor is inorganic ion, then it is designated as:
Coenzyme
Prosthetic group
Holoenzyme
Activator
34-The type of inhibition in which inhibitor has no structural similarity to substrate and combine with enzyme at other than the active site is called:
Irreversible inhibition
Competitive inhibition
Non-competitive and reversible inhibition
Reversible inhibition
35-The inhibitors that bind tightly and permanently to enzymes and destroy their globular structure and catalytic activity are:
Reversible inhibitors
Irreversible inhibitors
Competitive inhibitors
Non-competitive inhibitors
36-Enzyme succinate dehydrogenase converts succinate into:
Malate
Malonic acid
Citrate
Fumarate
37-The view that active site of an enzyme is flexible and when a substrate combines with it, cause change in enzyme structure is known as:
Lock & key model
Induce fit model
Sliding filament model
Specificity model
38-The competitive inhibitors have structural similarity with:
Active site
Binding site
Substrate
Co-enzyme
39-Some enzymes require helper which is non-protein part for its efficient functioning that is called:
Accelerator
Co-factor
Prosthetic group
Apoenzyme
40-WOF is an example of competitive inhibitor?
Glucose
Fumarate
Succinic acid
Malonate
41-An enzyme required Mg++ to catalyze the substrate. The Mg++ is best identified as:
Prosthetic group
Activator
Co-enzyme
Inhibitor
42-According to .......... model, the active site of enzyme is modified as the substrate interact with enzyme.
Induced fit
Lock and key
Emil Fischer
Fluid mosaic
43-All enzymes are ...............
Fibrous proteins
Low molecular weight protein
Lipoproteins
Globular proteins
44-The reactants on which enzyme work are:
Products
Metabolites
Substrate
Catabolites
45-WOF comprises of inorganic ions?
Coenzymes
Activators
Prosthetic group
Apoenzyme
46-What is true about enzymes?
Fibrous proteins
Use in reaction
No effect on end product
Non-specific
47-Modified form of lock and key model was proposed by:
Koshland
Fischer
Watson
Rosalind Franklin
48-The temperature that promotes the maximum activity of enzyme is referred as:
Fixed temperature
Optimum temperature
Controlled temperature
Active temperature
49-A molecule can bind to another site of the enzyme rather than the true active site is referred as:
Non-competitive inhibitors
Allosteric inhibition
Competitive inhibitors
Irreversible inhibition
50-The type of energy reduced by the enzymes for biological reactions to occur is called the:
Light energy
Activation energy
Active energy
Heat energy
51-What is common in both competitive and non-competitive inhibition?
Irreversible inhibition
Feedback inhibition
Reversible inhibition
Non-reversible inhibition
52-A student of chemical engineering engulfed the toxic compound 'A' which was a potent inhibitor of certain enzyme. He was immediately brought to hospital where Dr. Injected intravenously substrate 'B' to minimize the toxic effect of compound 'A' . His life was saved from serious damages. The treatment method shows that compound 'A' was a
Temperature sensitive
Competitive reversible
Irreversible
Non-competitive reversible
53-Lock & Key model for enzyme action proposed by Emil Fischer suggests that:
Enzymes are unbiased for substrate
Enzymes can modify their active site
Enzymes are restricted to one reaction type
Enzyme can catalyze variety of reaction
54-A metabolic pathway is a
Route taken by chemicals through a solution
Sequence of enzymes controlled reactions
Route taken by a single particular enzyme
Routes taken by all enzymes in a specific medium
55-Energy must be added for a chemical reaction to start. This is energy of:
Activation
Energy
Enthalpy
Oxidation
56-sucrase (invertase) act on:
Sucrose
Sucrose and starch
Any disaccharide
Any organic monomer
57-Blocking of active site of an enzyme temporarily is a type of
Non-competitive inhibition
Irreversible inhibition
Competitive inhibition
Feedback inhibition
58-A group of enzymes called hydrolases acts upon:
Lipids
Proteins
Carbohydrates
All of these
59-A complete enzyme is
Holoenzyme
Apoenzyme
Coenzyme
Co-factor only
60-Active site of an enzyme is produced by
Globular structure
Charges
Fibrous structure
Both globular structure and charges
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