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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

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2
Q
  • CELLULAR CATALYSTS
A

ENZYMES

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2
Q
  • Biologic catalysts that cause reactions in the body to take place
A

ENZYMES

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2
Q

act as base or acid

A

Amphoteric

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3
Q

inactive state of enzyme

A

(ZYMOGEN/PROENZYME)

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3
Q
  • non-protein organic biochemical that takes part in the enzyme reaction
A

COENZYME

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3
Q
  • Essential to the catalytic activity as a COSUBSTRATE
A

COENZYME

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4
Q

what are the example of activator

A
  • E.g. Mg++, Na+, K+, Zn++
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4
Q
  • Inorganic ionic cofactor
A

ACTIVATOR

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4
Q
  • Metabolic regulator of enzyme reaction
A

ACTIVATOR

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4
Q
  • Splits molecules with water as part of the reaction process
A

HYDROLASES

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4
Q
  • Assayed in disorders of skeletal muscles
A

LYASES

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4
Q
  • the combined enzyme & coenzyme
A

HOLOENZYME

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4
Q
  • Multichained enzymes of similar activity
A

ISOENZYMES

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4
Q

what are the example of coenzyme

A
  • E.g. NAD, Pyridoxal phosphate
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4
Q

 Assayed for investigation of cardiac & liver disorders

A

OXIDOREDUCTASES

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4
Q
  • A coenzyme that cannot be removed from its attachment to an enzyme using dialysis
A

PROSTHETIC GROUP

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4
Q
  • Enzyme without a cofactor
A

APOENZYME

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4
Q
  • a.k.a Non- specific, Practical name, Working name
A

TRIVIAL NAME

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5
Q
  • Several distinct forms of enzymes
A

ENZYME VARIANTS

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5
Q
  • Responsible for splitting molecules or breaking of bonds
A

LYASES

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5
Q

Describes the nature of the reaction catalyzed

A

Systematic Name

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5
Q
  • Inorganic activators existing as a part of the enzyme molecule
A

METALLOENZYME

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5
Q
  • Appear in specific tissue, organ & cell organelle of similar organisms
A

ISOENZYMES

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5
Q
  • Substance acted upon by an enzyme & is converted into a new substance
A

SUBSTRATE

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5
Q

 Move an intact group of atoms (NH2 or PO4) from one molecule to another

A

TRANSFERASES

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5
Q

 Catalyze oxidation-reduction reactions

A

OXIDOREDUCTASES

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5
Q
  • Substance derived from a transformed substrate
A

PRODUCT

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5
Q

Numerical code designation prefixed w/ the letters E.C.

A

Systematic Name

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5
Q

not inhibited by 2% Formalin

A

ACP (Prostate)

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5
Q

speed and direction wherein the molecule will move

A

Electrophoretic mobility

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6
Q
  • Having the same catalytic activity but different structure
A

ISOENZYMES

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6
Q

modified by proteases present in serum to produce forms that differ slightly from each other

A

ISOFORMS

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6
Q

less sensitive to α-naphthyl PO4

A

ACP (RBC)

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6
Q

 Genetically-transmitted enzyme

A

ALLOENZYME

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6
Q

class of non plasma that is carry out their functions within the cells in which they are formed

A

Enzymes Associated w/ Cellular Metabolism

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6
Q

inhibited by 2% Formalin

A

ACP (RBC)

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6
Q

 Found only in one location, particularly the cell sap

A

UNILOCULAR ENZYME

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6
Q

 Important in defining the biochemical characteristics of an individual

A

ALLOENZYME

6
Q

Generally secreted by the liver

A

PLASMA-SPECIFIC ENZYMES

6
Q

 Enzymes of similar catalytic activity but are specie specific

A

HETEROENZYME

6
Q

class of non plasma that is secreted in plasma at a high rate but rapidly disposed off to excretory channels

A

Enzymes of Secretion

6
Q

important in the use of Forensic medicine & genetics

A

ALLOENZYME

6
Q

– Compatible in structural and chemical characteristics

A

Molecular Compatibility

6
Q
  • How enzyme works and its efficacy
A

ENZYME KINETICS

6
Q
  • Found in the mitochondria & cell sap
A

BILOCULAR ENZYME

6
Q

commonness between Enzyme & Substrate

A

Molecular Compatibility

7
Q

of enzymes or substrates that can be reacted

A

Space Availability

8
Q

refers to the enzyme acting on a specific substrate

A

Specificity

8
Q
  • when an enzyme can act and catalyze one unique reaction
A

ABSOLUTE SPECIFICITY

8
Q
  • an enzyme acts only on the specific isomer
A

STEREOISOMERIC

9
Q

refers to the active site being complementary in shape & size to the substrate

A

Lock & Key

9
Q
  • when some enzymes act on different substrates belonging to the group
A

GROUP SPECIFICITY

9
Q

ALP is active at what pH

A

10.5

9
Q

rate of enzyme action

A

TIME

9
Q

 Rate of reaction is almost directly proportional to substrate conc. at low values

A

First Order Kinetics

9
Q
  • When maximum velocity is reached, the rate of increase in velocity is “O”
A

Zero Order Kinetics

9
Q

the enzyme changes in shape during binding to accommodate the substrate

A

Induced Fit Model

9
Q

the point at w/c the reaction rate is greatest (pH)

A

pH 7.0 – 8.0

9
Q

shows the relationship of the reaction velocity to the substrate concentration

A

 MICHAELIS-MENTEN CURVE

9
Q

– Introduced by Emil Fischer (theory)

A

Lock & Key

9
Q
  • Binds w/ the E-S complex; no product formed
A

Uncompetitive Inhibition

10
Q

– Introduced by Koshland (theory)

A

Induced Fit Model

10
Q

Enzyme conc. is fixed; Substrate conc. is varied

A

First Order Kinetics

10
Q

enzyme undergoes inactivation and denaturation

A
  • 50 – 60°C
10
Q

°T considered favorable for enzyme activity

A

30-37°C or 37 – 40°C

10
Q
  • Reaction rate is unaffected by increased substrate concentration
A

Zero Order Kinetics

10
Q
  • Binds to the active site, blocks access of the S to the E (type of inhibition)
A

Competitive Inhibition

10
Q
  • Bind the substrate to the active site by forming ionic bridges
A

Activators

10
Q
  • Inhibitors are possible removed from the system
A

Reversible Inhibition

10
Q

enzyme is fully restored - Physical processes that remove inhibitors

A

Reversible Inhibition

10
Q

reaction rate is doubled for every 10°C increase

A
  • Q10 value
10
Q
  • Pepsin is active at what pH
A

1.5

10
Q
  • Binds elsewhere on the E causing change in shape that interferes w/ S binding
A

Non-Competitive Inhibition

10
Q

causes competition between substrate molecules for a single binding site

A

Excess substrate

10
Q
  • Orients the substrate so it is attached to the enzyme in the correct configuration
A

Activators

10
Q
  • Decrease the rate of enzyme reaction
A

inhibitors

10
Q
  • Multiple measurements (e.g. OD change) are made at specific time intervals or by a continuous recording spectrophotometer
A

CONTINUOUS-MONITORING or KINETIC ASSAYS

10
Q
  • Inhibitors covalently combine w/ the enzyme
A

Irreversible Inhibition

10
Q
  • Physical methods are ineffective in separating inhibitors from the enzymes
A

Irreversible Inhibition

10
Q
  • Required for the reaction to proceed
A

Coenzyme concentration

10
Q
  • Reaction proceeds for a designated time & is stopped
A

FIXED TIME ASSAYS

10
Q

Chemical substances E.g

A

Fluoride, Chelators,Tartrate

11
Q

 Disruption of the 3-dimensional structure of the enzyme molecule

A

ENZYME DENATURATION

12
Q

IU - Expressed in terms of

A

U/L or mU/L

12
Q

unit Proposed by the Commission on Enzymes (IUB)

A

IU

12
Q
  • conforms w/ the Systemè International (SI) scheme of units
A

katal unit

13
Q
  • unit of enzyme activity w/c converts 1 mol of substrate per second
A

katal unit

13
Q
  • Least preferred specimen
A

plasma

13
Q

increases product formation

A
  • Prolonged reaction
13
Q

denaturation and inhibition of enzyme reaction

A
  • Prolonged incubation
14
Q
  • Reduction in the supply of oxygenated blood perfusing any tissue
A

LEAKAGE of ENZYMES from CELLS

14
Q

error that - Release of intracellular enzyme

A

hemolysis

14
Q

an error that - Inhibits CK & Amylase

A

Turbid/Lactascent Serum (Lipemia)

15
Q
  • Genetic deficiency of enzyme production
A

ALTERED ENZYME PRODUCTION DECREASE

16
Q

NOT a major route for elimination

A
  • URINARY EXCRETION
16
Q
  • Inactivated enzymes are removed by the
A

RES

CC2 (5 decks)

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