Enzymes Flashcards

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
Aspartate aminotransferase Sources? Elevated in what conditions?
AST Heart, skeletal muscle and Liver Viral hepatitis and Liver Carcinoma
26
alanine aminotransferase Sources? Elevated means?
ALT Liver Liver problems
27
Alkaline Phosphatease Sources? What if increased? Diseases?
ALP Liver and Bone (Only one from bone) Increased= Bone and/or liver disease Biliary Obstruction and Hepatocellular disease
28
Gamma-glutamultransferase Sources? Diseases?
GGT Liver (primarily) Kidney, pancreas and intestine Biliary track disorders, chronic ALCOHOLIC relapse
29
Cholinesterase and Acetylcholinesterase What are sources for both? DECREASED ChE levels?
ChE and AChE AChE = Red blood cells ChE = Liver, white brain and serum Insecticide and nerve gas exposure
30
Creatine Kinase Types and Sources?
CK CK-BB (CK1) = Brain tissue CK-BM (CK 2) = Cardiac Muscle CK-MM (CK 3) = Cardiac and skeletal muscle
31
Lactate Dehydrogenase Sources Hemolysis Diseases?
LD Ubiquitous in all cells (nonspecific) DONT USE (will elevate) Hepatobiliary dieases and ANEMIA
32
Aldolase Sources? Diseases?
ALS Skeletal muscle, Liver and Brain Skeletal M-related, ie. Dystrophy
33
Amylase Sources? Diseases?
AMS Salivary (mostly) and pancreas Acute Pancreatitis, Perforated Peptic Ulcer
34
Lipase Sources? Diseases?
LPS ``` Pancreas Acute pancreatitis (more specific than AMS) ```
35
Acid Phosphatase Diseases Increased?
ACP Bone PROSTATE
36
Glucose-6-phosphate dehydrogenase Sources? Decreased?
G-6-PD RBCs, Adrenal, LN, Thymus Hemolytic anemia
37
AST
Aspartate aminotransferase
38
ALT
alanine aminotransferase
39
ALP
Alkaline Phosphatease
40
GGT
Gamma-glutamultransferase
41
ChE and AChE
Cholinesterase and Acetylcholinesterase
42
CK
Creatine Kinase
43
LD
Lactate Dehydrogenase
44
ALS
Aldolase
45
AMS
Amylase
46
LPS
Lipase
47
ACP
Acid Phosphatase
48
G-6-PD
Glucose-6-phosphate dehydrogenase
49
ALT or AST higher in normal conditions? What if ALT is higher for a period of time? What if AST is higher?
ALT ALT for long= Hepatitis AST higher than ALT = Cirrhosis
50
What are causes for total CK elevations?
Myocardial Infarction (12x) CK-MB, Skeletal Muscle Disease (8x) CK-MM (DUCHENNES) and cerebral disease