Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

CLINICAL CHEM. 2 > Lec 1: Enzymology > Flashcards

Lec 1: Enzymology Flashcards

You may prefer our related Brainscape-certified flashcards:
Periodic Table flashcards Chemistry 101 flashcards AP® Chemistry flashcards Organic Chemistry 101 flashcards
1
Q

The speed to which a reaction is completed

A

Reaction rate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

The 3 major factors that influence reaction rate

A
  • Concentration
  • Temperature
  • Pressure
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

A chemical reaction generally will occur when ___

A

When two particle reactants hit each other and start a reaction

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

[ TRUE or FALSE ]

  1. Higher concentration = faster rate reaction
  2. Higher pressure = faster reaction rate
  3. Higher temperature = lower kinetic energy = slower particle movement
A
  1. TRUE
  2. TRUE
  3. FALSE
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

It is the amount of kinetic energy particles have

A

Temperature

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

It is a substance that speeds up the rate of reaction without being consumed.

A

Catalyst

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

What is Activation Energy?

A

It is the minimum energy required to initiate the reaction

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

How does the catalyst work?

A

The catalyst will increase the reaction rate by lowering the Activation Energy.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

It facilitates the reaction by binding to the reactants allowing them to interact optimally and start the reaction.

A

Enzyme

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

[ TRUE or FALSE]

All of the reactions found in the human body are reversible

A

FALSE

• Most of the reactions found in the human body are reversible

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Differentiate Non-reversible reaction from Reversible Reaction.

A

Non-reversible reaction
• reactants »» products
• CANNOT convert back to the reactants

Reversible reaction
• reactants »» products
products »» reactants
• forward and backward reaction occur simultaneously

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

The state where the forward rate of reaction will equal the reverse rate of reaction.

A

Equilibrium

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

3 factors that will influence the movement of EQUILIBRIUM

A
  • Concentration
  • Temperature
  • Pressure
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

[ TRUE or FALSE ]

An enzyme is a protein

A

TRUE

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Define Active Site of an enzyme.

A

The Active Site is the central region that accommodates the substrate and facilitates the formation of the product.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

What is a Catalytic Site of an enzyme?

A

It is part of the Active Site where catalysis will occur.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q
  1. Apoenzyme
  2. Holoenzyme
A
  1. It is an incomplete & inactive enzyme that needs a non-protein component to be activated.
  2. • It is the activated Apoenzyme
    • apoenzyme + cofactor
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q
  1. The most common metal ions the enzyme systems need.
  2. The common coenzymes required by enzyme systems.
A
  1. • Calcium
    • Zinc
    • Magnesium
    • Manganese
  2. • NAD
    • NADP
    • Pyridoxal 5’-phosphate
    • Coenzyme A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

An inactive enzyme that will activate itself upon encounter with a certain environmental factor

A

Zymogen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

They are variants of the same enzyme that catalyze the same
reaction in a similar manner but different in location, susceptibility to inactivation, and electrophoretic mobility.

A

Isoenzymes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

LDH and their Primary Tissue location:

  1. LDH 1
  2. LDH 2
  3. LDH 3
  4. LDH 4
  5. LDH 5
A
  1. Heart
  2. RBC
  3. Brain, pancreas, kidney, spleen, lungs
  4. Placenta, kidney, pancreas
  5. Muscle, Liver
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

The 6 classifications of enzymes

A
  • oxidoreductases
  • transferases
  • hydrolases
  • lyases
  • isomerases
  • ligase
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

CLASSIFICATION OF ENZYMES

  1. It catalyzes oxidation/reduction (redox reaction)
  2. Like hydrolases, they can destroy bonds and remove functional groups, but they DO NOT incorporate water.
  3. It transfers a functional group from one substrate to another.
  4. It binds different materials together in order to create something else.
  5. It catalyzes hydrolysis or the breakdown of bonds by addition of water
  6. It will rearrange the structure of a substrate
A
  1. Oxidoreductases
  2. Lyases
  3. Transferase
  4. Ligase
  5. Hydrolase
  6. Isomerase
24
Q

[ TRUE or FALSE ]

An enzyme that can act on only one specific substrate and corresponding reaction is called absolute specificity

A

TRUE

25
Q

An enzyme that can act on all substrates that are of a certain structure of processing a particular functional group is called __.

A

Group specificity

26
Q

Example of an enzyme with absolute specificity

A

Urease

Urease will ONLY act on urea, converting it to ammonia. If urea is modified, urease can’t act on it.

27
Q

Example of an enzyme that is group specific

A

Hexokinase

It only acts on sugars that have 6 carbon atoms (mannose, fructose, glucose)

28
Q

When the substrate enters the active site, the site does not perfectly fit the substrate’s shape at first. So the active site changes its structure to accommodate the substrate, optimizing the fit.

A

Induced Fit Model of Enzyme Action

29
Q
  • the speed of the reaction is dependent on substrate concentration
  • the more substrates you have, the faster the reaction
A

First Order Kinetics

30
Q
  • the rate of the reaction is dependent on the enzyme concentration
  • there is excess substrate but further addition of it will no longer have any effect
A

Zero Order Kinetics

31
Q

Michaelis Menten Equation

A

Vo = Vmax [S]
Km + [S]

32
Q

[ TRUE or FALSE ]

The Lineweaver Burk Plot is the linear graph of your Michaelis Menten

A

TRUE

33
Q

How do pH & temperate influence enzymatic reactions?

A
  • Optimum pH level = good shape of Active Site
  • pH level changes = Active Site shape changes
  • if pH level returns to optimum level, Active Site also returns to its shape. Only if the change was not extreme.
  • the same with temperature
34
Q

Differentiate Coenzyme and Prosthetic group.

A

Coenzyme
• organic
• temporarily attaches to enzyme

Prosthetic group
• permanently attaches to enzyme

35
Q

Competitive Inhibition

A

The inhibitor binds to the active site first, so that the substrate cannot bind to the enzyme

36
Q

Non-competitive Inhibition

A

The inhibitor binds to an allosteric site, so that the active site will be deformed and will not work properly. So, catalysis happens at a slower rate.

37
Q

Uncompetitive Inhibition

A

The inhibitor needs a substrate that is already bound to the enzyme ,so that the inhibitor will work. Without a substrate, the uncompetitive inhibitor is useless.

38
Q
  • transformation of 1 umol of substrate to product per minute
  • expressed in IU/L
A

International Unit

39
Q
  • transformation of 1 umol of substrate to product per second
  • expressed in kat/L
A

Katal (kat)

40
Q

What are the clinical reasons to analyze enzymes?

A
  • to confirm a diagnosis
  • to prognosticate
  • to monitor treatment or progression of disease
41
Q

Creatine kinase is responsible for the transfer of ___.

A

Transfer of phosphate from ATP to creatine to form creatine phosphate

42
Q

This enzyme is responsible for the transfer of phosphate from ATP to creatine to form creatine phosphate

A

Creatine kinase

43
Q

LDH is responsible for the ___ reaction involving the conversion of ___ or vice versa.

A

• redox
• lactate to pyruvate

44
Q

This enzyme is responsible for the redox reaction involving the conversion of lactate to pyruvate or vice versa.

A

Lactate dehydrogenase (LDH)

45
Q

In what areas are the following found, with the highest activities?

  • CK-MM
  • CK-BB
  • CK-MB
A

CK-MM: skeletal muscles

CK-BB: brain

CK-MB: heart

46
Q

CK-MB

  1. Begins to rise within ___ hours after an infarction.
  2. Peaks at ___ hours.
  3. Returns to normal within ___ hours.
A
  1. 4 hours
  2. 12 to 24 hours
  3. 48 to 72 hours
47
Q
  1. Normally, which LDH isoenzyme is highest?
  2. What LDH isoenzyme significantly increases in myocardial infarction?
A
  1. LDH-2 is highest in normal people.
  2. LDH-1 significantly increases because it is mostly found in the heart.
48
Q

LDH

  1. Begins to rise in ___ hours.
  2. Peaks at ___ hours
  3. May remain elevated for ___.
A
  1. 12 to 24 hours
  2. 48 to 72 hours
  3. Almost 2 weeks or 10 days
49
Q

Preferred marker for myocardial infarction

A

Troponin

50
Q
  1. Why is troponin a preferred marker for myocardial infarction?
  2. Troponin increases in ___ hours, and remains elevated for up to ___.
A
  1. Very specific to the heart & very sensitive
  2. increases in less than 4 hours, remains for up to 2 weeks
51
Q

[ TRUE or FALSE ]

AST

A. It is found in highest concentrations in heart, liver, and skeletal muscle

B. It can elevate only in hepatic conditions

A

A. TRUE

B. FALSE
• It can elevate even in non-hepatic conditions

52
Q

[ TRUE or FALSE ]

ALT

A. There is only a significant increase when you have hepatic cause.

B. It is considered more specific to hepatocellular disease

A

A. TRUE

B. TRUE

53
Q
  1. What is the purpose of ALP?
  2. What is the purpose of GGT
A
  1. Hydrolysis of phosphate
  2. It transfers the gamma glutamine functional group to an amino acid to form glutathione
54
Q

an enzyme belonging to hydrolysis that catalyzes the breakdown of starch and glycogen

A

Amylase

55
Q

The primary sources of this enzyme are the parotid gland and the pancreas

A

Amylase

56
Q

It is an enzyme specific only to the pancreas

A

Lipase

57
Q
  • found in the liver
  • one of the most important enzyme systems in the body
  • metabolism of drugs, hormones, and various chemicals
A

(CYP) Cytochrome P-450

CLINICAL CHEM. 2 (3 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions