Chapter 3 - Biochemical Pathways Flashcards
Active Site
Particular region of an enzyme into which the substrate fits: pocket or groove formed by folding of the polypeptide chain (tertiary structure of the protein
Anabolic Reaction
A reaction that builds up complex molecules from more simple ones
Enzyme-substrate Complex
The step where a substrate binds to an active site of an enzyme forms the enzyme-substrate complex
Substrate
The substance binding to an enzyme to be catalysed
Function of enzymes and purpose.
Substrate binds to an enzyme at an active site, and the enzyme changes shape to fit around the molecule forming enzyme - substrate complex . The bonds of the substrate are stretched and weakened by molecular interactions between the substrate and enzyme. Thus a lower energy pathway is required for the reaction to occur. A lower activation energy is required for the reaction therefore reaction proceeds at required rate.
Co - factors and Co-enzymes
Co-factors are non protein compound that activate the action of an enzyme. Co-enzymes are a type of co-factor but are limited to organic co-factors only. Non Co-enzyme cofactors: Inorganic metal ions permanently bound to active site
CoEnzymes:
organic
non-protein
loosely bound to active site
Globular VS Fibrous Protein
Globular: Eg.) Egg, casein
folded ball like structures
soluble
have comparatively weak intermolecular forces
Fibrous: Eg.) Silk, skin, wool
Thin, thread like structure
insoluble
If energy is lost in a biochemical reaction it is….
Exergonic: releases energy
catabolic: breakdown of compounds complex–>simple
If energy is absorbed in a biochemical reaction it is….
Endergonic: requires energy
Anabolic: simple —>complex molecules
Protein denaturation, cause and concqeunce
Caused by..
High temperature: breaks bonds and disrupts tertiary structure
pH; Too much H+ or OH- interacts with bonds and changes 3D shape.
Protein can no longer function as required.
Metal ions: Charge disrupts bonds between amino acids.
detergents and solvents: For bonds with non-polar groups thus causing hydrogen bonding
Increase rate of reaction by:
Increase enzyme concentration,
increase temp
decrease product concentration
increase substrate concentration
Note: All changes have a saturation point where further increases either have no impact or a detrimental one.
two types of inhibition:
Non-competitive:
Substance binds to enzyme, not at the active site and changes the shape of the enzymes active site so it cannot bind with substrate.
Competitive enzyme:
binds to the active site of the enzyme, inhibiting the substrate from binding to the active site.
anaerobic glycolysis inputs and outputs
Glucose + NAD + H+ +2ADP +2pi—> 2*Pyruvate + NADH + 2ATP
What cells use cellular respiration?
All living organisms respire as it is required for growth, however some organism cannot respire aerobically (mostly bacteria).
Alcohol fermentation
- What organisms
- inputs and outputs
plants, fungi, bacteria
2* Pyruvate —–> Ethanol + 2*CO2