Clinical enzymology Flashcards
Examples of Oxidoreductases
LDH, G6PD, GLDH, MDH
Examples of Transferases
AST, ALT, CK, PK, GGT
An enzyme also called SGOT
AST (aspartate aminotransferase)
SGOT stands for
serum glutamic-oxaloacetic transaminase
Also known as SGPT
ALT (alanine aminotransferase)
SGPT stands for
Serum glutamic pyruvic transaminase
Examples of hydrolases
ALP, ACP, Amylase, lipase, chymotrypsin, elastase, cholinesterases, 5’ nucleotidase
Ex of Lyases
aldolase
ex. of Isomerases
Triose phosphate isomerase
Ex. of Ligases
Glutathione synthetase
The reaction of Oxidoreductases/Dehydrogenases
Oxidation-reduction
The reaction catalyzed by Transferases
Transfer of functional groups
The reaction catalysed by Hydrolases
Hydrolysis
The reaction catalyzed by Lyases
Removal of groups to form double bonds
The reaction catalyzed by Isomerases
Interconversion of isomers
The reaction catalyzed by Ligases
Bond formation coupled with ATP hydrolysis
describes the rate of catalysis of the enzyme at some particular substrate concentration.
Michaelis-Menten equation
Double reciprocal of Michaelis-Menten equation
Lineweaver-Burk equations
What is a first-order kinetics?
- Where enzyme concentration exceeds substrate
- More substrate, faster the reaction
- There is continuous increase in velocity as more substrate is added or bound to an enzyme up too a certain point
What is zero-order kinetics?
- No further increase in velocity but the reaction continues; all active sites have been occupied
True or False: Measurement of enzyme is based on its activity and not in concentration.
TRUE
a method of measurement where reaction is usually stopped by inactivating the enzyme with weak acid
Fixed-time/endpoint
A method of measurement where multiple measurements of absorbance change as a function of time.
Continuous-monitoring/Kinetic
A unit of measure for the amount of enzyme that catalyzes the reaction of 1 umol of substrate per minute
IU (international unit)
a unit of measurement for the amount of enzyme that catalyzes the reaction of 1 mol of substrate per second.
Katal
how many Katal are there in 1 IU
17 nanokatal or 0.0167 microkatal
In which pH range do most reactions occur
pH 7-8, except ACP and ALP
The denaturation point of enzymatic reactions is…
40-50 degree Celsius
A factor that affect enzymatic reactions that must bind to particular enzymes before a reaction occurs
Cofactors
Are inorganic cofactors
Activators
Are organic cofactors
Coenzymes
What are the three types of enzyme inhibitors?
competitive, non-competitive, uncompetitive
Inhibitor that binds to the active site
Competitive inhibitor
An inhibitor that binds to site other than the active site (allosteric site)
Non-competitive inhibitor
An inhibitor that binds to the enzyme-substrate complex
Uncompetitive inhiitor
High-molecular mass forms of the serum enzymes that can be bound to Immunoglobulin and non-immunoglobulin
Macroenzymes
Which tissues is CK found?
brain, heart, skeletal muscles
Enumerate the CK Typical Isoenzymes
CK-BB (CK 1), CK-MB (CK 2), CK-MM (CK 3)
enumerate CK Atypical Isoenzymes
MI, Macro-CK
CK Isoenzyme that is elevated in CNS damage, tumors, presence of macro-CK
CK-BB
A CK isoenzyme present in significant amounts in cardiac tissue
CK-MB
A CK isoenzyme present in striated muscle and normal serum
CK-MM
The only CK isoenzyme that is a cathode
MI (Mitochondrial CK)
What are the methods for CK determination called?
Tanzer-Gilvarg and Oliver-rosalki
Which CK method is a forward reaction?
Tanzer-Gilvarg
Which CK method is a reverse reaction?
Oliver-Rosalki