types of enzymes Flashcards

1
Q

what is catalase

A

-intracellular enzyme which catalyses the break down of hydrogen peroxide into water and oxygen

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

secondary structure of catalse

A

-primarily made up of alpha helices which are stabelised by hydrogen bonds

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

tertiary structure of catalse

A

-active site contains a heme group which is critical in breakdown of H2O2
-includes interactions like hydrogen bonds, ionic bonds, hydrophobic interaction, disulfide bridges

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

quaternary structure of catalse

A

-exists as a tetramer (composed of 4 polypeptide subunits) each one is identical and very similar

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

subunits of catalase

A

-each has its own active site so more efficient and each contain a heme group which faciliates redox reactions

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

where is catalase found

A

-in humans (liver cells)
-in plants(leaves, roots, other tissues)

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

steps involved in catalysis reaction of catalase

A
  1. binding of hydrogen peroxide to catalase (bind to iron atom in the heme group at its active site)
  2. breakdown of hydrogen peroxide molecule
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

the significance of catalse

A

-detoxifies peroxides in kidney and liver
-prevents oxidative damage to cells

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

what is amylase

A

-an extracellular and intercellular enzyme which cataylses the break down of carbohydtrates into simpler sugars, making them easier for the body to use
-specfically starch to maltose

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

secondary structure of amylase

A

-contains both alpha helices and beta pleated sheets

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

tertiary structure of amylase

A

-held by hydrogen bonds, ionic bonds, disulfide bridges, hydrophobic interactions

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

quaternary structure of amylase

A

-in humans there is no quaternary structure
-function is carried out efficiently by a single polypeptide
-the active site is fully formed by the tertiary strucutre and doesnt require multiple subunits

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

where is amylase found

A

-in humans in the salivary glands, small intenstine (secreted by pancreas into small intestine)
-in the epithelial cells lining the small intenstine
-in the seeds, roots, fruits of plants to break down stored starch into sugars during germination/ripening

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

example of how amylase is extracellular and intracellular

A

-extracellular pancreatic and salivary amylase
-intracellular is liver and muscle and chloroplasts

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

steps involved in the catalysis reaction of amylase

A
  1. substrate binding
  2. hydrolysis of glycosidic bonds
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

what binds to what in the catalysis reaction involving amylase

A

-the starch which consists of long chains of glucose molecules linked by glycosidic bonds binds to the active site

17
Q

significance of amylase

A

-important role in digestion, providing energy for the body
-allows maltose and glucose to be easily absorbed by the intestines

18
Q

what is trypsin

A

-an extracellular enzyme which breaks down proteins in the small intestine
-type of protease
-works by hydrolising peptide bonds

19
Q

secondary structure of trypsin

A

-contains both alpha helices and beta pleated sheets stabelised by hydrogen bonds
-secondary structure positions the active site and stabilises the enzymes function in breaking down proteins

20
Q

tertiary structure of trypsin

A

-stabelised by disulfide bonds and hydrophobic and hydrophillic interactions
-contains the ser-his-asp triad known as catalytic triad to enable break down of peptide bonds

21
Q

quaternary structure of trypsin

A

-single polypeptide chain, monomer
-functionstability governed by secondary and tertiary structure

22
Q

where is trypsin found

A

-primarily in the small intestine (activation and function) and pancreas (production and serotonin)

23
Q

steps in the catalysis reaction of enzymes

A
  1. substrate binding
  2. formation of catalytic complex (the catalytic triad working together to facilitate hydrolysis reaction)
24
Q

significance/importance of trypsin?

A

-key role in the breakdown of proteins which are essential for bodies nutrition and metabolic processes
1. digestion
2.activation of other digestive enzymes
3. critical for nutrient absorption