Case 2 BIOCHEM - enzymes, micronutrients Flashcards
1
Q
Define an enzyme
A
- proteins that catalyse biochemical reactions
2
Q
Enzymes’ role in digestion
A
- digest food by hydrolysing bonds that link the building blocks of dietary macromolecules
3
Q
Function of digestive enzymes
A
- hydrolyse peptide bonds in dietary proteins. Breakdown of proteins into peptides and then into amino acids for absorption
- hydrolyse glycosidic bonds in dietary carbohydrates. Breakdown of complex carbohydrates into monosaccharides and disaccharides for absorption
- hydrolyse ester bonds in dietary fats. Breakdown of fat into fatty acids, glycerol, and monoacyglycerol for absorption
4
Q
Enzyme specificity
A
- type of reaction (oxidation, hydrolysis or isomerisation)
- nature of substrates
- defined by the active site structure
5
Q
Active site
A
Small area of an enzyme where substrates bind and reaction takes place
6
Q
Roles of amino acid residues at the active site
A
- bind substrates in the correct orientation for the reaction to occur
- take part in catalysis of the reaction
7
Q
Carboxypeptidase
A
- hydrolyse peptide bond at the amino acid residue at the C terminus
8
Q
Pancreatic Serine Proteases
A
- chymotrypsin, elastase and trypsin use the same mechanism for catalysis but have different active sites that have different substrate specificities
- chymotrypsin: hydrolyses the peptide bond at the bulky hydrophobic amino acid residue
- elastse: hydrolyses peptide bond at a small amino acid residue
- trypsin: hydrolyses peptide bond at a Lys or Arg (basic) amino acid residue
9
Q
Thermodynamically favourable reactions
A
free energy change (delta G) is negative
10
Q
Thermodynamically speaking, how does an enzyme catalyse a reaction?
A
- by lowering the activation energy. This increases the rate and the fraction of molecules reaching the transition stage.
- the lowest the activation energy, the higher the fraction of substrate molecules which attain the transitions state thus the higher the reaction rate.
11
Q
Mechanisms of enzyme catalysis (molecular)
A
- straining substrate conformation so it starts to resemble the products
- covalently binding substrate in order to activate the substrate
- providing a suitable environment at the active site for the reaction to occur
- bringing substrates in close proximity and in correct orientation for reaction to occur at the active site
- acting as a base or acid
* different enzymes use different combinations of the mechanisms
12
Q
Shapes of enzyme-catalysed reactions
A
- Michaelis-Menten = hyperbolic.
2. Allosteric = sigmoid.
13
Q
Define Km
A
substrate concentration at which v=1/2vmax
14
Q
Significance of Km in the context of enzyme sensitivity
A
- [s] «_space;km: enzyme will be sensitive to changes in [s]
- [s] = km: enzyme will be half saturated with substrate
- [s]» km: enzyme will be insensitive to changes in [s] and will be operating at Vmax
15
Q
Significance of Km in the context of enzyme sensitivity
A
- [s] «_space;km: enzyme will be sensitive to changes in [s]
- [s] = km: enzyme will be half saturated with substrate
- [s]» km: enzyme will be insensitive to changes in [s] and will be operating at Vmax