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Anatomy & Physiology > Chemical Reaction & Enzymes > Flashcards

Chemical Reaction & Enzymes Flashcards

1
Q

Metabolism

A

in any living thing thousands of chemical reactions take place at the same time to support life

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2
Q

Chemical reaction

A

the process of breaking existing bonds, rearrangement of atoms and formation of new bonds

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3
Q

What are the three parts of a chemical reaction?

A

breaking, rearrangement, and formation

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4
Q

What do all chemical reactions need to start?

A

Activation energy

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5
Q

Activation energy

A

the energy required to break existing chemical bonds

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6
Q

What are the three ways to speed up a chemical reaction?

A

heat, motion, and catalysts

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7
Q

Catalysts

A

substances that accelerate or promote chemical reactions

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8
Q

Enzymes

A

the biological active catalysts that facilitate chemical changes in the human body by lowering the activation energy

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9
Q

Uncatalyzed reaction

A

a chemical reaction without an enzyme

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10
Q

Catalyzed reaction

A

a chemical reaction with an enzyme

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11
Q

Enzymes are what kind of organic molecule?

A

proteins

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12
Q

Enzymes exist as what?

A

polymers

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13
Q

Why are enzymes polymers?

A

because they are proteins

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14
Q

Active site

A

region of an enzyme where the substrate binds

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15
Q

What is temporarily formed when a substrate binds to an active site?

A

an enzyme-substrate complex

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16
Q

What is the importance of the specificity of an active site?

A

only allows one type of substrate to bind to the enzyme; catalyzing only one specific reaction

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17
Q

How are enzymes formed?

A

through protein synthesis

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18
Q

Enzyme mechanisms steps

A

the substrate binds to the enzyme forming an enzyme-substrate complex, the enzyme changes shape resulting in an induced fit, the substrate is broken down, and finally the products are released

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19
Q

Cofactors

A

an inorganic chemical structure attached to an enzyme that aids in enzyme function

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20
Q

Inorganic cofactors

A

are attached to the enzyme and are required for their normal function

21
Q

Organic cofactors

A

are not attached to enzymes and have specific functions in assisting enzymes

22
Q

What are the six major classes of enzymes?

A

oxidoreductase, transferase, hydrolase, isomerase, ligase, and lyase

23
Q

Oxidoreductase

A

transfers electrons from one substance to another

24
Q

Transferase

A

transfers a functional group

25
Q

Hydrolase

A

splits a chemical bond using water

26
Q

Isomerase

A

Converts isomer to another

27
Q

Ligase

A

bonds two molecules together

28
Q

Lyase

A

splits a chemical bond in the absence of water

29
Q

Which class of enzymes participate in oxidation-reduction?

A

Oxidoreductase

30
Q

The rate of a chemical reaction may be accelerated by what?

A

an increase in enzyme concentration or substrate concentration

31
Q

Saturation

A

occurs when so much of a substarte is present that all enzyme molecules are actively engaged in the chemical reaction, resulting in no furthable (notable) increase in reaction rate

32
Q

Inhibitors

A

substances that bind to an enzyme and turn it off, preventing it from catalyzing the reaction

33
Q

Competitive inhibitor

A

interferes with active site of an enzyme so substrate cannot bind

34
Q

Allosteric inhibitor

A

changes shape of enzyme active site so substrate cannot bind to enzyme

35
Q

What determines the likelihood of competitive inhibitor occupying the active space?

A

the concentration of the substrate

36
Q

Inhibition

A

a molecule that binds o an enzyme and blocks its activity

37
Q

How are enzymes named?

A

root + -ase

38
Q

Enzymes are highly what?

A

highlt specific

39
Q

How do enzymes break down substrates?

A

they put stress in the substrate bonds

40
Q

Why are enzymes needed in small quantities?

A

becuase enzymes are reused

41
Q

What kind of conditions are required for enzymes to maintain their functional shape?

A

optimal conditions (temperature, pH)

42
Q

What are the two forms of enzyme regulation?

A

activation and inactivation

43
Q

Activation

A

binds a specific cofactor to an enzyme

44
Q

What kind of molecules are cofactors usually?

A

metals (Zn, Fe, Mg) and vitamins (B, C, K)

45
Q

Inactivation

A

binds inhibitors

46
Q

How do allosteric inhibitors differ from competitive inhibitors?

A

competitve inhibitors compete for the active site while allosteric inhibitors alter the overall shape of the enzyme

47
Q

The prefix allo- means what?

A

wrong

48
Q

The suffix”-steric” means what?

A

shape

Anatomy & Physiology (14 decks)

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