P1: INTRODUCTION TO ENZYMOLOGY Flashcards

1
Q

It is the study of enzymes that deals with the:
a. Activity of enzymes
b. Chemical reactions it catalyzes
c. Clinical use

A

Enzymology

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2
Q

Enzymes are ______ that increases the speed of reaction.

A

Protein catalysts

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3
Q

Enzymes are biologic proteins that catalyzes biochemical reactions WITHOUT, give the 3 reasons.

A
  1. Without altering the equilibrium
  2. Without being consumed
  3. Without changed in composition
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4
Q

The molecule upon which an enzyme acts.

A

Substrate

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5
Q

Also known as, “Excess energy”, where its minimum energy required to:

  1. Start a chemical reaction
  2. Raise all molecules in 1 mol of a compound at a certain temperature to the transition state at the peak of the energy barrier
A

Activation Energy

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6
Q

This is the region of the enzyme where substrate molecules BIND and undergo chemical reaction and produces an enzyme-substrate complex.

A

Active site

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7
Q

Active site are often _____?

A

water-free cavity

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8
Q

Not a substrate may bind, changing the shape of the enzyme or confirmation, and changing its ability to either become active or inactive

A

Allosteric site

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9
Q

Give 2 kinds of Allosteric Site. and its function.

A
  1. Allosteric inhibitor: IMPAIRS activity of the enzyme
  2. Allosteric activator: ENHANCES activity of the enzyme
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10
Q

Results when an enzyme is subject to POSTTRANSLATIONAL MODIFICATION

A

Isoform

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11
Q

This are enzymes existing in DIFFERENT FORMS within the same individual but the SAME ACTION, differentiated from each other based on certain physical characteristics such as:
- Electrophoretic mobility
- Solubility
- Resistance to inactivation

A

Isoenzyme

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12
Q

This are NONPROTEIN MOLECULE that may be necessary for enzyme activity.

A

Cofactor

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13
Q

This are INORGANIC COFACTOR that includes Chloride ion and Magnesium ion.

A

Activator

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14
Q

This are ORGANIC COFACTOR such as Nicotinamide adenine dinucleotide (NAD).

A

Coenzyme

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15
Q

A coenzyme that is BOUND TIGHTLY to the enzyme.

A

Prosthetic group

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16
Q

Apoenzyme + Coenzyme = ?

A

Holoenzyme

17
Q

Also known as, “Zymogen”, which is the INACTIVE FORM OR PRECURSOR OF ENZYME.

[ADD. INFO] It is then converted to active form when it has reached the site of activity (E.g., Trypsinogen –> Trypsin, Chymotrypsinogen –> Chymotrypsin)

A

Proenzyme

18
Q

Term used to describe the ability of an enzyme to CHOOSE EXACT SUBSTRATE from a group of similar chemical molecules. Also, the capacity of protein catalysts to recognize and BIND ONLY 1 OR FEW MOLECULES.

A

Enzyme Specificity

19
Q

Enzymes may recognize and catalyze? Name the 3.

A
  1. Single substrate (Absolute)
    Ex. Urease catalyzes hydrolysis of urea
  2. Group of similar substrates (Group)
    Ex. Hexokinase adds a phosphate group to hexoses
  3. Particular type of bond (Linkage)
    Ex. Chymotrypsin catalyzes the hydrolysis of peptide bonds
20
Q
A