ENZYMES INTRO/CK/LDH Flashcards
(91 cards)
Enzymes
— _______; is a biological substance that catalyzed a reaction [make the chemical reaction faster]
When the enzymes are absent, the reaction would continue but _______.
— Location of enzymes: within the cells [______, ______,intestines and stomach]
Cellular injury/degradation → the enzymes would be ?
- Detection of _____ when certain enzymes are high.
biocatalyst
slower
saliva
pancreas
released into circulation
disorder
Essential to Physiologic Functioning:
✔ Hydration of _____—> ____ maintenance of the blood. as hydrogen can combine with it as acidic/ basic substances.
✔ _______ conduction
✔ ________ contraction
✔ ________ degradation found in _____ tract [______, _____]
✔ _______ use
CO2
pH maintenance
Nerve conduction
Muscle contraction
Nutrient degradation [GI: amylase, lipase]
Energy use
For a fast chemical reaction to occur, there must be the presence of ________[enzymes] + _________.
● _________ site [the substrate]— water-free cavity, where the substance on which the enzyme acts
- ideal environment, such as a slightly [basic/acidic] or [polar/non- polar] environment, for the reaction to occur.
o _________ complex— fast chemical reaction
● _________ site— area other than the active site: water- free
reactants
substrates
Active
basic
non-polar
ES
Allosteric
A chemical reaction may occur spontaneously if the [2] is higher for the reactant than the products.
_________— reactants have enough energy to break their bond and collide to form new bond [bond between the enzyme & substrate]
free energy [reactants]
available kinetic energy
Activation Energy
_________ Specificity– [strictest] enzyme + only 1 substrate and catalyzed a single reaction
_________ Specificity– + all substrates containing a particular chemical group
_________ Specificity– other enzymes are specific to chemical bonds [hydrogen bonds]
_________ Specificity + predominantly combine with only 1 optical isomer [mirror image] of a certain compound.
Absolute
Group
Bond
Stereoisomeric
_________: gen. temperature for preservation
_________: long term preservation
_________: for cold-labile enzymes
Examples [2]
_________ temperature– reversible inactivation enzyme
_________= NOT RECO → inactivates the enzymes
-20C
2-8C
RT
LD4,LD5
Cold temperature
Repeated Thawing
Enzymes that increase in terms of hemolysis:
KLAMP
potassium
LDH
AST
ACP
Aldolase
Magnesium
Phosphate/Phosphorus
A lactescence and milky specimen means that there is a [INC/DEC] in concentration, and there is the presence of______.
DEC
chylomicrons
Once the counterpart reactant is saturated, and an additional reactants are applied, what will happen to the reaction?
it will not result to faster reaction
In substrate and enzyme concentration, it follows the hypothesis of _______ “even in low substrate conc→ the substrate can ______with free enzyme”
Michaelis & Menten
readily bind
Enzymatic Reaction can be:
✔ _________– the rxn rate is directly proportional to substrate concentration.
✔ _________– rxn rate depends only on enzyme concentration.
First Order kinetic
Zero Order Kinetic
In First Order Kinetic, there is the addition of more _______ to easily find its counterpart.
In Zaro Order Kinetic, there is the addition of more _______ to easily find its counterpart.
substrate
enzyme
_________Enzymes are protein that carry a net molecular charge
— # physiologic enzymatic reactions occur in the pH range of _________ but some enzymes are active in wider pH ranges than others.
[2 Examples]
pH
7.0-8.0
ACP- acid
ALP- basic
TEMPERATURE
[INC] = [INC/DEC] chemical rate rxn
Temperature coefficient
– In every increase of [#] degree = [#]x increase rate rxn; until, of course, the
________ is denatured.
________– optimum temp.
________— [INC] denaturation rate increases as the temp
increases and is usually [significant/nonsignificant]
________— enzymes inactivation _______temperature— enzymes inactive
- ___________→ prevent activity loss until analysis.
10 degree
2x
protein
37C
40-50%
60-65%
Low
Frozen/Refrigerated
___________ non-protein entities that must bind with enzyme for a rxn to occur
- ___________—made up of inorganic cofactors
— function by alternating the enzyme ___________ [enzyme ___________ change that corresponds to the substrate] for proper substrate binding
—Linking substrate to the enzyme/coenzyme, or undergoing ___________.
✔ Metallic: [5]
✔ Non-metallic: [2]
COFACTORS
Activatiors
spatial configuration
shape
oxidation-reduction
Ca, Fe, Mg, Mn, Zn, K
Br, Cl
___________— made up of organic cofactors
— as 2nd substrates for enzymatic rxn.
▪ ___________ between the enzyme and substrate [↑ ___________ of the rxn]
___________– when bound tightly to the enzyme, coenzymes
o E.g. [3]
Coenzymes
Bridge
velocity
Prosthetic groups
Vit, NAD, NADP
Interfere with the reaction= Enzymatic reactions may not progress normally
Inhibitors
physically bind to the active site of an enzyme and compete with the substrate for the active site.
[same shape with the active site= NO ES complex formed]
Competitive Inhibition
Is competitive inhibition reversible or not? If yes, how?
Reversible
By increasing the substrate concentrate, so the possibility of its binding capacity is higher than the inhibitor.
binds an enzyme at a place other than the active site [allosteric site]= NO ES complex produced= NO RXN CATALYZED
Non-competitive Inhibition
Is Noncompetitive inhibition reversible, irreversible or both? explain.
Both
Reversible, by other substances that can bind other than the inhibitors.
Irreversible, when the inhibitors destroys the active site.
True or False
In NonCompetitive Inhibition, Increasing the substrate concentration would not reverse the reaction as it binds the enzyme independently from the substrate [binds to allosteric site]
True
inhibitor binds to the ES complex.
Uncompetitive Inhibition
2 METHODS IN MEASURING THE ENZYMATIC RXN
— Measure based on their _______ and not the absolute ______.
[2]
activity
value
Fixed-time/End point
Continuous Monitoring/Kinetic Assay
