5 Written Questions
5 Matching Questions
- Enzyme Substrate Complex
A non-covalent complex composed of a substrate bound to the active site of the enzyme
Ammonia, a biproduct of the GDH reaction during deamination which is highly toxic and water soluble, thus able to move out of the mitochodrial matrix easily.
Small organelles which contain digestive enzymes with an internal pH of around 5. They are responsible for breaking down large molecules taken in to the cell by phagocytosis and also for the breaking down of old organelles.
- d A transmembrane protein responsible for the formation of caveola.
This shows as dark areas on the eukaryotic nucleas; it is densly packed chormatin (DNA and protein complex) which cannot be transcribed.
5 Multiple Choice Questions
This is the group which varies in proteins and can be any of twenty amino acids, the polarity of this Group dictates how a protein will behave in certain pH conditions. This explains why enzymes require a certain pH to function.
Small lipid-bounded spheres which transport proteins, glyco proteins and newly synthesized lipids (which are imbedded in the sphere itself) from the endoplasmic reticulum to the Golgi Apparatus or from the Golgi apparatus to another destination. They move short distances by the process of difussion, moving long distances requires the assistance of proteins associated with microtubules.
- This process involves the reversible addition of a small chemical group (e.g phosphate, acetyl) to the side chain of a particular amino acid residue. The most common example of this modification is protein phosphorolation. This process plays a major role in cell functioning.
Also known as A and Ade, this is a nucleobase (a purine derivative) with a variety of roles in biochemistry including cellular respiration, in the form of both the energy-rich adenosine triphosphate (ATP) and the cofactors nicotinamide adenine dinucleotide (NAD) and flavin adenine dinucleotide (FAD), and protein synthesis, as a chemical component of DNA and RNA. The shape of adenine is complementary to either thymine in DNA or uracil in RNA.
This bond occurs when the amino group from one protein joins with the carboxyl group of another, forming a dipeptide.
5 True/False Questions
This is an intermediate in the citric acid cycle, formed after reaction T6, used by cells to produce energy in the form of adenosine triphosphate (ATP) from food. It is formed by the oxidation of succinate by the enzyme succinate dehydrogenase. Fumarate is then converted by the enzyme fumarase to malate. Human skin naturally produces fumaric acid when exposed to sunlight.
Fumarate is also a product of the urea cycle.
The process by which substances are exported from a cell.
SDS-PAGE, sodium dodecyl sulfate polyacrylamide gel electrophoresis, is a technique widely used in biochemistry, forensics, genetics and molecular biology to separate proteins according to their electrophoretic mobility (a function of length of polypeptide chain or molecular weight). SDS gel electrophoresis of samples that have identical charge per unit mass due to binding of SDS results in fractionation by size. This method can be used to separate all types, even those that are not water soluble.
Non Competitive Inhibitor →
These inhibitors do not appear to have the same structure as substrate, it therefor binds at a different site on the enzyme and the ES complex can still form. It does however hinder the catylitic action of the enzyme and the end product is never produced.
A component of the citric acid cycle and is capable of donating electrons to the electron transport chain by the reaction:
succinate + FAD → fumarate + FADH2.
This is catalysed by the enzyme succinate dehydrogenase (or complex II of the mitochondrial ETC). The complex is a 4 subunit membrane-bound lipoprotein which couples the oxidation of succinate to the reduction of ubiquinone. Intermediate electron carriers are FAD and three Fe2S2 clusters part of subunit B.