enzymes Flashcards
1
Q
- branch of medicine which deals with the study of enzymes and their importance in the diagnosis and treatment of diseases
A
CLINICAL ENZYMOLOGY
2
Q
- CELLULAR CATALYSTS
A
ENZYMES
2
Q
- Biologic catalysts that cause reactions in the body to take place
A
ENZYMES
2
Q
act as base or acid
A
Amphoteric
3
Q
inactive state of enzyme
A
(ZYMOGEN/PROENZYME)
3
Q
- non-protein organic biochemical that takes part in the enzyme reaction
A
COENZYME
3
Q
- Essential to the catalytic activity as a COSUBSTRATE
A
COENZYME
4
Q
what are the example of activator
A
- E.g. Mg++, Na+, K+, Zn++
4
Q
- Inorganic ionic cofactor
A
ACTIVATOR
4
Q
- Metabolic regulator of enzyme reaction
A
ACTIVATOR
4
Q
- Splits molecules with water as part of the reaction process
A
HYDROLASES
4
Q
- Assayed in disorders of skeletal muscles
A
LYASES
4
Q
- the combined enzyme & coenzyme
A
HOLOENZYME
4
Q
- Multichained enzymes of similar activity
A
ISOENZYMES
4
Q
what are the example of coenzyme
A
- E.g. NAD, Pyridoxal phosphate
4
Q
Assayed for investigation of cardiac & liver disorders
A
OXIDOREDUCTASES
4
Q
- A coenzyme that cannot be removed from its attachment to an enzyme using dialysis
A
PROSTHETIC GROUP
4
Q
- Enzyme without a cofactor
A
APOENZYME
4
Q
- a.k.a Non- specific, Practical name, Working name
A
TRIVIAL NAME
5
Q
- Several distinct forms of enzymes
A
ENZYME VARIANTS
5
Q
- Responsible for splitting molecules or breaking of bonds
A
LYASES
5
Q
Describes the nature of the reaction catalyzed
A
Systematic Name
5
Q
- Inorganic activators existing as a part of the enzyme molecule
A
METALLOENZYME
5
Q
- Appear in specific tissue, organ & cell organelle of similar organisms
A
ISOENZYMES
5
- Substance acted upon by an enzyme & is converted into a new substance
SUBSTRATE
5
Move an intact group of atoms (NH2 or PO4) from one molecule to another
TRANSFERASES
5
Catalyze oxidation-reduction reactions
OXIDOREDUCTASES
5
- Substance derived from a transformed substrate
PRODUCT
5
Numerical code designation prefixed w/ the letters E.C.
Systematic Name
5
not inhibited by 2% Formalin
ACP (Prostate)
5
speed and direction wherein the molecule will move
Electrophoretic mobility
6
- Having the same catalytic activity but different structure
ISOENZYMES
6
modified by proteases present in serum to produce forms that differ slightly from each other
ISOFORMS
6
less sensitive to α-naphthyl PO4
ACP (RBC)
6
Genetically-transmitted enzyme
ALLOENZYME
6
class of non plasma that is carry out their functions within the cells in which they are formed
Enzymes Associated w/ Cellular Metabolism
6
inhibited by 2% Formalin
ACP (RBC)
6
Found only in one location, particularly the cell sap
UNILOCULAR ENZYME
6
Important in defining the biochemical characteristics of an individual
ALLOENZYME
6
Generally secreted by the liver
PLASMA-SPECIFIC ENZYMES
6
Enzymes of similar catalytic activity but are specie specific
HETEROENZYME
6
class of non plasma that is secreted in plasma at a high rate but rapidly disposed off to excretory channels
Enzymes of Secretion
6
important in the use of Forensic medicine & genetics
ALLOENZYME
6
– Compatible in structural and chemical characteristics
Molecular Compatibility
6
- How enzyme works and its efficacy
ENZYME KINETICS
6
- Found in the mitochondria & cell sap
BILOCULAR ENZYME
6
commonness between Enzyme & Substrate
Molecular Compatibility
7
of enzymes or substrates that can be reacted
Space Availability
8
refers to the enzyme acting on a specific substrate
Specificity
8
- when an enzyme can act and catalyze one unique reaction
ABSOLUTE SPECIFICITY
8
- an enzyme acts only on the specific isomer
STEREOISOMERIC
9
refers to the active site being complementary in shape & size to the substrate
Lock & Key
9
- when some enzymes act on different substrates belonging to the group
GROUP SPECIFICITY
9
ALP is active at what pH
10.5
9
rate of enzyme action
TIME
9
Rate of reaction is almost directly proportional to substrate conc. at low values
First Order Kinetics
9
- When maximum velocity is reached, the rate of increase in velocity is “O”
Zero Order Kinetics
9
the enzyme changes in shape during binding to accommodate the substrate
Induced Fit Model
9
the point at w/c the reaction rate is greatest (pH)
pH 7.0 – 8.0
9
shows the relationship of the reaction velocity to the substrate concentration
MICHAELIS-MENTEN CURVE
9
– Introduced by Emil Fischer (theory)
Lock & Key
9
- Binds w/ the E-S complex; no product formed
Uncompetitive Inhibition
10
– Introduced by Koshland (theory)
Induced Fit Model
10
Enzyme conc. is fixed; Substrate conc. is varied
First Order Kinetics
10
enzyme undergoes inactivation and denaturation
- 50 – 60°C
10
°T considered favorable for enzyme activity
30-37°C or 37 – 40°C
10
- Reaction rate is unaffected by increased substrate concentration
Zero Order Kinetics
10
- Binds to the active site, blocks access of the S to the E (type of inhibition)
Competitive Inhibition
10
- Bind the substrate to the active site by forming ionic bridges
Activators
10
- Inhibitors are possible removed from the system
Reversible Inhibition
10
enzyme is fully restored - Physical processes that remove inhibitors
Reversible Inhibition
10
reaction rate is doubled for every 10°C increase
- Q10 value
10
- Pepsin is active at what pH
1.5
10
- Binds elsewhere on the E causing change in shape that interferes w/ S binding
Non-Competitive Inhibition
10
causes competition between substrate molecules for a single binding site
Excess substrate
10
- Orients the substrate so it is attached to the enzyme in the correct configuration
Activators
10
- Decrease the rate of enzyme reaction
inhibitors
10
- Multiple measurements (e.g. OD change) are made at specific time intervals or by a continuous recording spectrophotometer
CONTINUOUS-MONITORING or KINETIC ASSAYS
10
- Inhibitors covalently combine w/ the enzyme
Irreversible Inhibition
10
- Physical methods are ineffective in separating inhibitors from the enzymes
Irreversible Inhibition
10
- Required for the reaction to proceed
Coenzyme concentration
10
- Reaction proceeds for a designated time & is stopped
FIXED TIME ASSAYS
10
Chemical substances E.g
Fluoride, Chelators,Tartrate
11
Disruption of the 3-dimensional structure of the enzyme molecule
ENZYME DENATURATION
12
IU - Expressed in terms of
U/L or mU/L
12
unit Proposed by the Commission on Enzymes (IUB)
IU
12
- conforms w/ the Systemè International (SI) scheme of units
katal unit
13
- unit of enzyme activity w/c converts 1 mol of substrate per second
katal unit
13
- Least preferred specimen
plasma
13
increases product formation
- Prolonged reaction
13
denaturation and inhibition of enzyme reaction
- Prolonged incubation
14
- Reduction in the supply of oxygenated blood perfusing any tissue
LEAKAGE of ENZYMES from CELLS
14
error that - Release of intracellular enzyme
hemolysis
14
an error that - Inhibits CK & Amylase
Turbid/Lactascent Serum (Lipemia)
15
- Genetic deficiency of enzyme production
ALTERED ENZYME PRODUCTION DECREASE
16
NOT a major route for elimination
- URINARY EXCRETION
16
- Inactivated enzymes are removed by the
RES
