enzymes Flashcards
Activation energy definition
the energy required to raise the temp of 1 mole of a compound to a transitional state
transitional state is where…..
reaction can go backwards & forwards in equal amounts
E+S ES E+P (ES = transitional state)
Enzyme active site is where…
substrate interacts with molecule
Enzyme Allosteric site is …
part of the enzyme that does not interact with substrate
Isoenzymes are…
different forms of the same enzyme
Cofactors are:
A non-protein molecule required for the enzyme to function
activators are:
Inorganic cofactors
ex. Mg or Cl
Coenzymes are:
organic cofactors
ex. NAD+
Functioning enzyme =
Apoenzyme + coenzyme
Zymogen is:
inactive form of an enzyme
Apoenzyme is:
enzyme portion of the molecule after coenzyme disconnected
Why would a zymogen be released in the body?
To be activated elsewhere
6 classes of enzymes
oxireductases transferases hydrolases lyases isomerases ligases
Lyases work to…
remove substrate groups
Isomerases work to…
catalyze the interconversion of isomers
Ligases work to…
join 2 substances
*needs ATP
Oxidoreductase enzymes (2)
LDH
G6PDH
Transferases (4)
AST
ALT
CK
GGT
Hydrolases (5)
ALKP ACP SAMY LIPA Cholinesterase
First order kinetics Rxn used to measure ____
substrate
First order: Rxn rate proportional to ______ concentration
substrate
_____ in excess in 1st order kinetics
Enzyme
Zero-order kinetics used to measure ____
enzyme
____ in excess in zero order kinetics
substrate
zero order Rxn rate proportional to _____ conc.
enzyme
How is rate measured?
Michaelis-menton equation
curves are used to find ___ and ___ of M-M equation
Vmax
Km
6 things that influence enzymatic reactions
Enzyme concentration pH temp cofactors coenzymes inhibitors
Enzyme concentration;
If S>E, V is proportional to __
If E>S, V is ____
V
Faster
Cofactors allow for: (3 things)
Substrate binding
Substrate linkage
Redox Rxns
Prosthetic groups
(coenzymes)
Tightly bound second substrate
3 types of inhibitors
Competitive
Noncompetitive
Uncompetitive
competitive inhibitors
Substance that binds to active site of enzyme, competes with substrate
Noncompetitive inhibitor
binds to a site other than active site on enzymes and deactivates enzyme
Uncompetitive inhibitor
binds to enzyme-substrate complex
Indirect measurement of enzymes requires
auxiliary enzymes to visualize Rxn
Continuous readings
(usually done with zero-order kinetics)
International Units quantify…
enzymes based on activity (rather than direct measurement)
Measured in IU/L
IU =
amount of enzyme required to catalyze the reaction of 1 umol of substrate per minute under specified conditions
Ways to directly measure enzymes (2)
immunoassays- attaching Ab to actual enzyme, measuring protein and quantifying amount present
Electrophoresis
CK =
Creatine kinase
CK fx
Storage of creatine phosphate in muscle cells
Helps form CP from Creatine (catalyzes Rxn)
Creatine + ATP to Creatine Phosphate + ADP
(Transferase)
Source of CK
Widespread distribution, incl skeletal muscle, heart muscle and brain tissue
Diagnostic significance of CK
Isoenzyme activity
AMI or muscle breakdown
CKMM, MB, MM
____ is used to indirectly quantitate CK
NADH–NAD+
CK interference
hemolysis (false elevation due to color)
CK reference ranges
Male: 60-380 U/L
Female: 40-195 U/L
Normal CKMB
<6% of total CK
LD =
lactate dehydrogenase
LD function
supports the interconversion of lactate to pyruvate
oxidoreductase