FACTORS AFFECTING ENZYME ACTIVITY-MCQ

89問 • 1ヶ月前

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通報

問題一覧

Factors affecting enzyme activity

ENERGY, MOLECULAR COMPATIBILITY

Factor affecting enzyme acitvity which helps stabilize the enzyme substrate complex

ENERGY

The more optimal the energy interactions, the____the binding.

STRONGER

Factor affecting enzyme activity which substrate must have a chemical structure compatible with the enzyme active site

MOLECULAR COMPATIBILITY

Molecular compatibility involves

COMPLEMENTARY SHAPE, CHARGE, FUNCTIONAL GROUP

Models explaining enzyme substrate binding

LOCK AND KEY MODEL, INDUCED FIT MODEL

Enzymes active site has a specific fixed shape that exactly matches the substrates shape

LOCK AND KEY MODEL

Lock and key model explains

HIGH SPECIFICITY

Lock and key model is proposed by

EMIL FISCHER

More accepted theory which enzymes active site is flexible and changes shape upon substrate binding

INDUCED FIT MODEL

This model enhances binding stability and catalytic efficiency by improving complementary dynamically and explains hopw enzymes can sometimes accomodate structurally related substrates with slight variations

INDUCED FIT MODEL

Induced fit model is proposed by

DANIEL KOSHLAND

Factor affecting enzyme acttivity which susbtrate must fit physically into the enzymes active site as geometry and size of the active site limit substrates binding

SPACE AVAILABILITY

Factors affecting enzyme activity which enzymes exhibit substrate specificity, meaning they selectively bind certain substrates

SPECIFICITY

Specificity depends on

SHAPE OF ACTIVE SITE, PRESENCE OF AMINO ACID RESIDUE

Specificity which enzymes acts on only one specific substrate and catalyzes only one specific reaction

ABSOLUTE

Specificity which enzyme acts on substrates that have a specific functional group or a c'mon chemical group

GROUP

Specificity which the enzyme distinguishes between different stereoisomers of a substrate

STEREOSPECIFIC

Lactate dehydrogenase acts only in what lactate isomer

Refers to the rate or duration of the enzymatic activity

TIME

If the enzyme has high catalytic efficiency, the reaction time is___

SHORTER

A longer reaction time may suggest

LOW ENZYME ACTIVITY, SUBOPTIMAL TESTING CONDITION, LACK OF COFACTOR

Refers to the rate of enzymatic reaction which described by the michaelis menten kinetics usually visualized through the michaelis menten curve

SUBSTRATE CONCENTRATION

Enzyme reaction genrally ___with increasing substrate concentration up to a certain limit

INCREASE

A graphical representatioin of how reaction velocity changes with varying substrate concentration is held constant

MICHAELIS MENTEN CURVE

Occurs at low substrate concentration as enzyme concentration is fixed and substrate is varied

FIRST ORDER KINETIC

In first order kinetics, the rate of reaction is _____to substrate concentration

DIRECTLY PROPORTIONAL

Occurs when substrate concentration is very high and the enzyme becomes saturated when VMAX is reached

ZERO ORDER KINETIC

In zero order kinetic, adding moe substrate ____the reaction rate

NOT INCREASE

The reaction rate is constant and depends only on enzyme concentration

ZERO ORDER KINETIC

The plateau or the maximum velocity of michaeis menten curve is known as

VMAX

Factors affecting enzyme reaction which explains driect relationship as increase in enzyme concentration results to an increase in the catalytic activity

ENZYME CONCENTRATION

The range at which enzymes are most active

OPTIMUM TEMPERATURE

Optimum temperature for human enzymes

37-47

Optimum temperature for enzyme

30-37

Refers to the reaction rate which approximately doubles until the enzyme reaches its optimum temperature

Q10 VALUE

Q10 value doubles for every

10C

Temperature where enzymes lose functionality due to denaturation

50-60

pH is also known as

HYDROGEN ION CONCENTRATION

Enzyme where it is active in a acidic environment

PEPSIN

What ph is pepsin active at

1.5

What ph is alkaline phosphatase active

10.5

Enhances enzymatic activity by aiding the interaction between the enzyme and substrate

ACTIVATOR

Mechanism of activators

IONIC BRIDGE, SUBSTRATE ORIENTATION

Mechanism of Activator which acts like a magnet

IONIC BRIDGE

Mechanism of activator which guides enzyme approaching to the active site

SUBSTRATE ORIENTATION

Examples of activators

CALCIUM, MAGNESIUM, FLURIDE

Reduces or completely block enzyme activity by interfering with the enzyme substrate interaction

INHIBITOR

Examples of inhibitors

EXCESS SUBSTRATE, PRODUCT OF REACTION, ENZYME SUBSTRATE NOT BREAK, CHEMICAL SUBSTANCE

Form of inhibition which mimics the substrate and competes for the enzymes active site

COMPETITIVE

Form of inhibition which effect can be overcome by increasing substrate concentration

COMPETITIVE

Form of inhibition whihc inhibitor binds to the allosteric site altering the enzymes shape and reducing its activity

NON COMPETITIVE

Form of inhibition which effect cannot be overcome by increasing substraet concentration

NON COMPETITIVE

Form of inhibition which wait for the ES complex before bind and prevent formation of product

UNCOMPETITIVE

Form of inhibition which inhibitor binds only to the enzyme substrate complex peventing the reaction from proceeding

UNCOMPETITIVE

Form of inhibition which effect decreases both the maximum reaction rate VMAX and the apparent affinity of the enzyme for the the substrate KM

UNCOMPETITIVE

Type of inhibition whihc inhibitors can be removed form the enzyme allowing the enzyme to regain its full capacity

REVERSIBLE

Type of inhibition which has no permanent damage to the enzyme

REVERSIBLE

Type of inhibition which inhibitors permanently inactivate the enzyme by covalently bonding to it

IRREVERSIBLLE

Type of inhibition which structural modification prevents the enzyme from performing its catalytic function

IRREVERSIBLE

Example of inhibitor when substrate concentration is extremely high, it can lead to competition among substrate molecules for the same active site which temporarily reduce the reaction rate due to crowding effects

EXCESS SUBSTRATE

Example of inhibitor which act as a feedback inhibitor by binding to the enzyme and preventing further reactions

PRODUCT OF THE REACTION

Irreversible inhibitor of cytochrome c oxidase in the electron transport chain

CYANIDE

Inhibits bacterial transpeptidase disrupting cell wall synthesis

PENICILLIN

Refers to the disruption of the enzyme's three-dimensional structure, which is essential for its catalytic activity affecting enzyme's active site making it incapable of binding to substrates effectively.

ENZYME DENATURATION

Type of Enzyme of denaturation which restoration of the enzyme's structure and activity is possible

REVERSIBLE

Type of Enzyme denaturation which happen when prolong denaturation beyond 50-60C weaken bonds

IRREVERSIBLE

Denaturing condition which weakens hydrogen bonds and other stabilizing forces in the enzyme, causing unfolding.

ELEVATED TEMPERATURE

Denaturing condition which disrupts ionic and hydrogen bonds, altering the enzymes folding.

EXTREME PH

Denaturing condition which can break covalent bonds and disrupt the enzyme's structure.

RADIATION

Denaturing condition which introduces air causing protein denaturation through mechanical stress and exposure interfaces

FROTHING

Denaturing condition disrupting ionic bonds precipitating proteins leading to structural instability

STRONG SALT SOLUTION

Denaturing condition refering to physical forces like vigorous shaking or blending can distrupt weak bonds and cause denaturation

MECHANICAL TRAUMA

Methods of enzyme assay

FIXED TIME ASSAY, CONTINOUS MONITORING

Procedure which combine the enzyme with its substrate allowing the reaction to proceed for a fixed time and stop the reaction by inactivating the enzyme

FIXED TIME ASSAY

Method of enzyme assay which useful for straightforward reactions where the endpoint can be measured and typically involves quantifying the product form or substrate consume

FIXED TIME ASSAY

Method of enzyme has a which is ideal for studying detailed kinetic behavior and it provides a complete profile of the action over time including initial velocity and substrate depletion

CONTINUOUS MONITORING

Method of enzyme essay which the reaction progress is struck in real time and measurements are taken at specific time intervals or continuously using devices like spectrophotometer

CONTINUOUS MONITORING

Units of measurement proposed by the IUB

INTERNATIONAL UNIT

International unit catalyzes the conversion of_____under specified conditions

1 UMOL OF SUBSTRATE/MINUTE

Common expressions for international unit

U/L, mU/L

Fully conforms to the system international units as amount of enzyme converts 1 mol of substrate per second

KATAL

Conversion of katal to international unit

17 NKAT

This is the least preferred specimen in clinical chemistry as anticoagulants may inhibit enzyme activity leading to inaccurate result

PLASMA

Hemolysis could cause falsely____result

INCREASE

Source of error which refers to high lipid content may interfere with spectrophotometric readings

LACTESCENT SERUM

Lipemic example could inhibit enzymes such as

CREATIN KINASE, AMYLASE

Prolong reaction time can lead to excess product formation resulting in a false____enzyme activity

INCREASE

Prolong incubation could lead to enzyme denaturation or inhibition causing a false____result

DECREASE

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問題一覧

Factors affecting enzyme activity

ENERGY, MOLECULAR COMPATIBILITY

Factor affecting enzyme acitvity which helps stabilize the enzyme substrate complex

ENERGY

The more optimal the energy interactions, the____the binding.

STRONGER

Factor affecting enzyme activity which substrate must have a chemical structure compatible with the enzyme active site

MOLECULAR COMPATIBILITY

Molecular compatibility involves

COMPLEMENTARY SHAPE, CHARGE, FUNCTIONAL GROUP

Models explaining enzyme substrate binding

LOCK AND KEY MODEL, INDUCED FIT MODEL

Enzymes active site has a specific fixed shape that exactly matches the substrates shape

LOCK AND KEY MODEL

Lock and key model explains

HIGH SPECIFICITY

Lock and key model is proposed by

EMIL FISCHER

More accepted theory which enzymes active site is flexible and changes shape upon substrate binding

INDUCED FIT MODEL

Induced fit model is proposed by

DANIEL KOSHLAND

Factor affecting enzyme acttivity which susbtrate must fit physically into the enzymes active site as geometry and size of the active site limit substrates binding

SPACE AVAILABILITY

Factors affecting enzyme activity which enzymes exhibit substrate specificity, meaning they selectively bind certain substrates

SPECIFICITY

Specificity depends on

SHAPE OF ACTIVE SITE, PRESENCE OF AMINO ACID RESIDUE

Specificity which enzymes acts on only one specific substrate and catalyzes only one specific reaction

ABSOLUTE

Specificity which enzyme acts on substrates that have a specific functional group or a c'mon chemical group

GROUP

Specificity which the enzyme distinguishes between different stereoisomers of a substrate

STEREOSPECIFIC

Lactate dehydrogenase acts only in what lactate isomer

Refers to the rate or duration of the enzymatic activity

TIME

If the enzyme has high catalytic efficiency, the reaction time is___

SHORTER

A longer reaction time may suggest

LOW ENZYME ACTIVITY, SUBOPTIMAL TESTING CONDITION, LACK OF COFACTOR

Refers to the rate of enzymatic reaction which described by the michaelis menten kinetics usually visualized through the michaelis menten curve

SUBSTRATE CONCENTRATION

Enzyme reaction genrally ___with increasing substrate concentration up to a certain limit

INCREASE

A graphical representatioin of how reaction velocity changes with varying substrate concentration is held constant

MICHAELIS MENTEN CURVE

Occurs at low substrate concentration as enzyme concentration is fixed and substrate is varied

FIRST ORDER KINETIC

In first order kinetics, the rate of reaction is _____to substrate concentration

DIRECTLY PROPORTIONAL

Occurs when substrate concentration is very high and the enzyme becomes saturated when VMAX is reached

ZERO ORDER KINETIC

In zero order kinetic, adding moe substrate ____the reaction rate

NOT INCREASE

The reaction rate is constant and depends only on enzyme concentration

ZERO ORDER KINETIC

The plateau or the maximum velocity of michaeis menten curve is known as

VMAX

Factors affecting enzyme reaction which explains driect relationship as increase in enzyme concentration results to an increase in the catalytic activity

ENZYME CONCENTRATION

The range at which enzymes are most active

OPTIMUM TEMPERATURE

Optimum temperature for human enzymes

37-47

Optimum temperature for enzyme

30-37

Refers to the reaction rate which approximately doubles until the enzyme reaches its optimum temperature

Q10 VALUE

Q10 value doubles for every

10C

Temperature where enzymes lose functionality due to denaturation

50-60

pH is also known as

HYDROGEN ION CONCENTRATION

Enzyme where it is active in a acidic environment

PEPSIN

What ph is pepsin active at

1.5

What ph is alkaline phosphatase active

10.5

Enhances enzymatic activity by aiding the interaction between the enzyme and substrate

ACTIVATOR

Mechanism of activators

IONIC BRIDGE, SUBSTRATE ORIENTATION

Mechanism of Activator which acts like a magnet

IONIC BRIDGE

Mechanism of activator which guides enzyme approaching to the active site

SUBSTRATE ORIENTATION

Examples of activators

CALCIUM, MAGNESIUM, FLURIDE

Reduces or completely block enzyme activity by interfering with the enzyme substrate interaction

INHIBITOR

Examples of inhibitors

EXCESS SUBSTRATE, PRODUCT OF REACTION, ENZYME SUBSTRATE NOT BREAK, CHEMICAL SUBSTANCE

Form of inhibition which mimics the substrate and competes for the enzymes active site

COMPETITIVE

Form of inhibition which effect can be overcome by increasing substrate concentration

COMPETITIVE

Form of inhibition whihc inhibitor binds to the allosteric site altering the enzymes shape and reducing its activity

NON COMPETITIVE

Form of inhibition which effect cannot be overcome by increasing substraet concentration

NON COMPETITIVE

Form of inhibition which wait for the ES complex before bind and prevent formation of product

UNCOMPETITIVE

Form of inhibition which inhibitor binds only to the enzyme substrate complex peventing the reaction from proceeding

UNCOMPETITIVE

Form of inhibition which effect decreases both the maximum reaction rate VMAX and the apparent affinity of the enzyme for the the substrate KM

UNCOMPETITIVE

Type of inhibition whihc inhibitors can be removed form the enzyme allowing the enzyme to regain its full capacity

REVERSIBLE

Type of inhibition which has no permanent damage to the enzyme

REVERSIBLE

Type of inhibition which inhibitors permanently inactivate the enzyme by covalently bonding to it

IRREVERSIBLLE

Type of inhibition which structural modification prevents the enzyme from performing its catalytic function

IRREVERSIBLE

EXCESS SUBSTRATE

Example of inhibitor which act as a feedback inhibitor by binding to the enzyme and preventing further reactions

PRODUCT OF THE REACTION

Irreversible inhibitor of cytochrome c oxidase in the electron transport chain

CYANIDE

Inhibits bacterial transpeptidase disrupting cell wall synthesis

PENICILLIN

ENZYME DENATURATION

Type of Enzyme of denaturation which restoration of the enzyme's structure and activity is possible

REVERSIBLE

Type of Enzyme denaturation which happen when prolong denaturation beyond 50-60C weaken bonds

IRREVERSIBLE

Denaturing condition which weakens hydrogen bonds and other stabilizing forces in the enzyme, causing unfolding.

ELEVATED TEMPERATURE

Denaturing condition which disrupts ionic and hydrogen bonds, altering the enzymes folding.

EXTREME PH

Denaturing condition which can break covalent bonds and disrupt the enzyme's structure.

RADIATION

Denaturing condition which introduces air causing protein denaturation through mechanical stress and exposure interfaces

FROTHING

Denaturing condition disrupting ionic bonds precipitating proteins leading to structural instability

STRONG SALT SOLUTION

Denaturing condition refering to physical forces like vigorous shaking or blending can distrupt weak bonds and cause denaturation

MECHANICAL TRAUMA

Methods of enzyme assay

FIXED TIME ASSAY, CONTINOUS MONITORING

Procedure which combine the enzyme with its substrate allowing the reaction to proceed for a fixed time and stop the reaction by inactivating the enzyme

FIXED TIME ASSAY

Method of enzyme assay which useful for straightforward reactions where the endpoint can be measured and typically involves quantifying the product form or substrate consume

FIXED TIME ASSAY

Method of enzyme has a which is ideal for studying detailed kinetic behavior and it provides a complete profile of the action over time including initial velocity and substrate depletion

CONTINUOUS MONITORING

Method of enzyme essay which the reaction progress is struck in real time and measurements are taken at specific time intervals or continuously using devices like spectrophotometer

CONTINUOUS MONITORING

Units of measurement proposed by the IUB

INTERNATIONAL UNIT

International unit catalyzes the conversion of_____under specified conditions

1 UMOL OF SUBSTRATE/MINUTE

Common expressions for international unit

U/L, mU/L

Fully conforms to the system international units as amount of enzyme converts 1 mol of substrate per second

KATAL

Conversion of katal to international unit

17 NKAT

This is the least preferred specimen in clinical chemistry as anticoagulants may inhibit enzyme activity leading to inaccurate result

PLASMA

Hemolysis could cause falsely____result

INCREASE

Source of error which refers to high lipid content may interfere with spectrophotometric readings

LACTESCENT SERUM

Lipemic example could inhibit enzymes such as

CREATIN KINASE, AMYLASE

Prolong reaction time can lead to excess product formation resulting in a false____enzyme activity

INCREASE

Prolong incubation could lead to enzyme denaturation or inhibition causing a false____result

DECREASE