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Chemistry Module 1 '15 > Enzymes > Flashcards

Enzymes Flashcards

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1
Q

What are the 5 enzyme properties?

A
  1. ) Only small amounts of enzyme required
  2. ) Highly specific for a reaction
  3. ) Accelerate the speed of a reaction
  4. ) Lower the activation energy of a reaction
  5. ) Enzymes are not altered or consumed in the reaction
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2
Q

Define Denaturation, what is it caused by?

A

Proteins uncoil and can not refold. Caused by extreme temperature and pH on all spectrums.

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3
Q

Define Cofactor

A

Non-protein compounds required by some enzymes to make them active

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4
Q

Define Activator and examples

A

Inorganic, Zn, Fe, Cu, Mg, Mn

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5
Q

Define Coenzyme and examples

A

Organic, NAD+, NADH, NADP+, NADPH

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6
Q

Define Holoenzyme

A

Complete cofactor and enzyme complex

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7
Q

Define Prosthetic group

A

Bound Cofactor

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8
Q

Define Apoenzyme

A

Protein portion of the enzyme

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9
Q

Define Active Site

A

sequence of AA where enzyme attaches.

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10
Q

Define Allosteric Site

A

A region other than the active site where a separate compound reacts and alters the shape of the ACTIVE SITE. Used to regulate enzyme activity.

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11
Q

Define Isoenzyme

A

Different physical forms of an enzyme that all catalyze the SAME reaction. Vary by charge, response to inhibitors and response to heat inactivation which allows them to be identified and quantified. Come from different tissues

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12
Q

Define International Unit

A

What enzymes are reported out in. The quantities of enzyme that will catalyze the reaction of one micromole of substrate/min under defined conditions.

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13
Q

Define Katal

A

Amount of enzyme that catalyzes with a reaction rate of one mole/second.

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14
Q

What are the three phases of enzyme measurements? What are their orders and what happens at each?

A

Lag- No product made = no absorbance (no order)
Log (linear) phase- Where measurements are taken Linear with time and respect to Beets law. (ZERO Order)
Substrate Depletion Phase- Substrate gone= no products so no change in absorbance. Rate of reaction depend ate on substrate, not enzyme so…(FIRST order)

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15
Q

What is first Order?

A

The rate of the reaction is proportional to the reactant.

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16
Q

What is Zero order?

A

The rate of the reaction is independent of the reactant.

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17
Q

REVIEW 2 things

A

Abs vs Time

Reaction Rate vs [S]

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18
Q

What are six factors that influence enzymatic activity?

A
  1. ) Presence of Cofactors
  2. ) Presence of Inhibitors
  3. ) pH
  4. ) Enzyme [ ]
  5. ) Substrate [ ]
  6. ) Temperature
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19
Q

What is a plasma-specific enzyme and what concentration does it involve? Examples?

A

Expected to be higher concentrations in the blood because they FUNCTION here. Coagulations factors

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20
Q

What are non-plasma-specific enzymes, where do they function? Examples

A

Do not function in plasma…function in tissue. LD or CK

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21
Q

What are two general processes for increased rate of entry of enzymes?

A
  1. ) Increase in rate of enzyme release into the bloodstream. such as hypoxia from a heart attack
  2. ) Increased production of an enzyme.
22
Q

What are the 7 causes of cell damage or death?

A 
Physical agents (trauma)
Microbial Agents
Chemicals and drugs
Hypoxia
Immune mechanisms
Nutritional disorders
Genetic defects
23
Q

What are two causes for increased enzyme production?

A

Enzyme induction (via drugs, alcohol, etc.) and proliferation of cells that produce that enzyme (cancer)

24
Q

What are 5 physiological factors that affect enzyme reference ranges?

A 
Sampling time
Age
Race
Sex
Exercise
25
Q

Aspartate aminotransferase

Sources?
Elevated in what conditions?

A

AST

Heart, skeletal muscle and Liver
Viral hepatitis and Liver Carcinoma

26
Q

alanine aminotransferase

Sources?
Elevated means?

A

ALT

Liver
Liver problems

27
Q

Alkaline Phosphatease

Sources?
What if increased?
Diseases?

A

ALP

Liver and Bone (Only one from bone)
Increased= Bone and/or liver disease
Biliary Obstruction and Hepatocellular disease

28
Q

Gamma-glutamultransferase

Sources?
Diseases?

A

GGT

Liver (primarily) Kidney, pancreas and intestine
Biliary track disorders, chronic ALCOHOLIC relapse

29
Q

Cholinesterase and Acetylcholinesterase

What are sources for both?

DECREASED ChE levels?

A

ChE and AChE

AChE = Red blood cells
ChE = Liver, white brain and serum
Insecticide and nerve gas exposure

30
Q

Creatine Kinase

Types and Sources?

A

CK

CK-BB (CK1) = Brain tissue
CK-BM (CK 2) = Cardiac Muscle
CK-MM (CK 3) = Cardiac and skeletal muscle

31
Q

Lactate Dehydrogenase

Sources
Hemolysis
Diseases?

A

LD

Ubiquitous in all cells (nonspecific)
DONT USE (will elevate)
Hepatobiliary dieases and ANEMIA

32
Q

Aldolase

Sources?
Diseases?

A

ALS

Skeletal muscle, Liver and Brain
Skeletal M-related, ie. Dystrophy

33
Q

Amylase

Sources?
Diseases?

A

AMS

Salivary (mostly) and pancreas
Acute Pancreatitis, Perforated Peptic Ulcer

34
Q

Lipase

Sources?
Diseases?

A

LPS

Pancreas 
Acute pancreatitis (more specific than AMS)
35
Q

Acid Phosphatase

Diseases
Increased?

A

ACP

Bone
PROSTATE

36
Q

Glucose-6-phosphate dehydrogenase

Sources?
Decreased?

A

G-6-PD

RBCs, Adrenal, LN, Thymus
Hemolytic anemia

37
Q

AST

A

Aspartate aminotransferase

38
Q

ALT

A

alanine aminotransferase

39
Q

ALP

A

Alkaline Phosphatease

40
Q

GGT

A

Gamma-glutamultransferase

41
Q

ChE and AChE

A

Cholinesterase and Acetylcholinesterase

42
Q

CK

A

Creatine Kinase

43
Q

LD

A

Lactate Dehydrogenase

44
Q

ALS

A

Aldolase

45
Q

AMS

A

Amylase

46
Q

LPS

A

Lipase

47
Q

ACP

A

Acid Phosphatase

48
Q

G-6-PD

A

Glucose-6-phosphate dehydrogenase

49
Q

ALT or AST higher in normal conditions? What if ALT is higher for a period of time? What if AST is higher?

A

ALT
ALT for long= Hepatitis
AST higher than ALT = Cirrhosis

50
Q

What are causes for total CK elevations?

A

Myocardial Infarction (12x) CK-MB, Skeletal Muscle Disease (8x) CK-MM (DUCHENNES) and cerebral disease

Chemistry Module 1 '15 (5 decks)

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