LESSON 2 (part2)

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Total cards: 24•Content version: v4•Public deck•Updated: 8/1/2026

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Front (Question)

This talks about the hydrogen Ion concentration

Back (Answer)

Front (Question)

This talks about the point which the concentration rate is greatest.

Back (Answer)

Optimum pH

Front (Question)

At what pH does many enzymes shows maximum activity?

Back (Answer)

7.0 - 8.0

Front (Question)

At what pH is Pepsin active?

Back (Answer)

1.5

Front (Question)

At what pH is ALP active?

Back (Answer)

10.5

Front (Question)

This binds the substrate to the active site by forming ionic bridges and orients the substrate so it is attached to the enzyme in the correct configuration.

Back (Answer)

Activators

Front (Question)

What is the common activator?

Back (Answer)

Magnesium

Front (Question)

This decreases the rate of enzyme reaction and counterpart of activators.

Back (Answer)

Inhibitors

Front (Question)

Describe the ff: A. Competitive Inhibition B. Non-competitive Inhibition C. Uncompetitive Inhibition

Back (Answer)

A. Competes with the substrate B. Freely attached and will not compete to the substrate. C. The inhibitor will bind to the E-S complex

#10

Front (Question)

Enumerate the type of Inhibition

Back (Answer)

A. Reversible INhibition B. Irreversible Inhibition

#11

Front (Question)

Describe the following: A. Reversible INhibition B. Irreversible Inhibition

Back (Answer)

a. Inhibitors are possibly removed from the system. Therefore, the enzyme is fully restored. B. Inhibitors covalently combined with the enzyme

#12

Front (Question)

What are the examples f iNhibitors?

Back (Answer)

• Excess substrate • Product of Inhibition • E-S complex does not break to yield products • Chemical substances

#13

Front (Question)

This inhibitor causes COMPETITION between substrate and molecules for a single binding site.

Back (Answer)

Excess substrate

#14

Front (Question)

This maybe an inhibitor of the forward reaction.

Back (Answer)

Product of reaction

#15

Front (Question)

This is the loss of enzymatic activity.

Back (Answer)

Enzyme denaturation

#16

Front (Question)

Enumerate the reasons for Enzyme Denaturation.

Back (Answer)

• Disruption of the 3-dimensional structure of the enzyme molecule. • May be reversed if: denaturation is not extensive OR denaturing agent is removed • Elevated temperature - beyond 50 - 60’C • Extreme in pH • Radiation • Frothing • Strong salt solution • Mechanical trauma • Chemicals

#17

Front (Question)

MEASUREMENT OF ENZYME REACTION: The rate of an enzyme - catalyzed reaction is ___________________ to the amount of ________________ present in the system.

Back (Answer)

Directly proportional; active enzyme

#18

Front (Question)

What are the methods of Enzyme Assay?

Back (Answer)

• Fixed Time Assays • Continuous-MOnitoring or KINETIC ASSAYS

#19

Front (Question)

This Assay uses a serum+substrate where the reactants are combined and the reaction proceeds for a designated time and is stopped by inactivating the enzyme.

Back (Answer)

Fixed Time Assays

#20

Front (Question)

This Assay has multiple measurements made at specific time intervals or by a continuous recording spectrophotometer.

Back (Answer)

Continuous-Monitoring or Kinetic Assays

#21

Front (Question)

What are the Units of Measurement of enzymes?

Back (Answer)

IU and Katal

#22

Front (Question)

This unit of measurement is proposed by the Commission on Enzymes (IUB) and is expressed in terms of U/L or mU/L

Back (Answer)

#23

Front (Question)

This unit of measurement is the unit of enzyme activity w/c converts 1 mol of substrate per second. Conforms with the System International (SI) scheme of units.

Back (Answer)

Katal

#24

Front (Question)

Enumerate the sources of errors in enzyme Assay.

Back (Answer)

• Use of plasma • Hemolysis • Turbid/Lactascent Serum • Heat Labile enzyme • Contaminants