This is just the part of my notes that I'm not sure about.
Main things of concern:
- Are these notes correct? Is there anything that's technically correct but could be misleading if I tried to read it later?
- Am I missing anything? These are notes for revising for SAC 1, so keep that in mind in regard to how much info I need for this. This is only part of my notes, but am I missing anything under each heading (the text that I haven't indented with >)?
- Do I need to include specific info on NAD and NADH? It's a common example, but is it a case study I need to memorise?
- What are the case studies and SPECIFIC (i.e. pertaining to one version of the concept and not the concept in general) examples I'll have to learn for SAC 1? Like the entire thing, not just enzymes. For example, I think lac operon is something I have to memorise (beyond the general concept of operons), though I'm not sure if it's for SAC 1.
Notes:
Regulation of enzymes
> Allosteric site
>> Some enzymes have receptor sites for the regulation / control of the enzymes, called an allosteric site
>> Substrate does not bind to these sites, it is not an active site. Molecules do bind to the allosteric site, we just don't call them substrates
>> Allosteric sites turn enzymes on or off by changing the shape of the enzymes
>> We call molecules that bind to the allosteric site non-competitive inhibitors because they don't compete with substrates to bind to the active site
Denaturation is the permanent change of the conformational shape of the active site caused by pH conditions outside of the optimal range or a temperature that is too high.
The reaction between an active site and substrate only starts if they collide with sufficient force. When the temperature is too cold, the enzyme doesn't denature, instead there is not enough kinetic energy for collisions of sufficient force to occur. This is deactivation. When the temperature is back at optimal levels, collisions of sufficient force can occur again and the enzyme reactivates.
Structure of Enzymes
> Enzymes are made of proteins
>> The basic building block of proteins is the amino acid
>> Many enzymes are tertiary proteins, folded so they have a specific active site
>> Many enzymes require the presence of other factors as well as the protein part before they act
>>> Non-protein parts are called cofactors and include metallic ions such as iron, calcium, copper, zinc, potassium and magnesium
>>>> Cofactors and coenzymes are not considered substrates
>>>> If the cofactor is an organic molecule, it is called a coenzyme
>>>> A good way to describe their purpose is that "cofactors provide crucial support in the enzyme mechanisms that are responsible for the enzyme working correctly"
>>>> All vitamins are coenzymes