BioMed Flashcards
Structure of a standard eukaryotic cell
> diverse in shape, structure and function
> Plasma membrane
> Nucleus
> Mitochondria
> Internal membrane bound organelles
Describe structure and function of cytoskeleton
> Helps cells maintain their shape and internal structures
> Provides mechanical support that lets cells carry out division and movement
Difference between prokaryotes and eukaryotes
> Prokaryotes: no nucleus, contains plasmids, usually unicellular, about 1-10 micrometers
> Eukaryotes: contains nucleus, usually multicellular, 10-100 micrometers
Primary structure of protein
Sequence of amino acids
Secondary structure of protein
Folding; alpha helix and beta pleated sheet
Tertiary structure of protein
3D shape; Defined by the hydrophilic and hydrophobic interactions between R groups of amino acid chains.
di-sulphide bridges
quaternary structure of a protein
A number of polypeptide chains linked together, and sometimes associated with non-protein groups to form a protein.
What is the action of oxidoreductases? Examples?
Reduction and oxidation reactions
Examples:
Dehydrogenase
Oxidase
What is the action of Transferases? Examples?
Transfer of amino, carboxyl, acyl, carbonyl, methyl, phosphate
Examples:
Transaminase
aldolase
What is the action of hydrolyses? Examples?
Change of bonds coupled with inserting water
Examples:
Esterase
Peptidase
What is the action of lyases? Examples?
Cleavage of C-C, C-S, C-N but not peptide bonds
Examples:
Decarboxylase
Aldolase
What is the action of isomerases? Examples?
Rearrangement of bonds
Examples:
Epimerase
Mutase
What is the action of ligases? Examples?
Formation of bonds between carbon and oxygen, sulphur, and nitrogen
Examples:
Synthetase
Carboxylase
What is Km? What does low km mean? high?
> the michealis constant
> Enzyme binds to the substrate tightly and works fast even at a low substrate concentration
> Enzyme binds to substrate weakly and requires a high concentration of substrate to work fast
What is Vmax?
Maximum possible rate of reaction
What are allosteric regulators
Bind to a regulatory site other than the active site and changes the enzyme activity by altering the proteins tertiary or quaternary structure
What are the 6 ways you can regulate enzyme activity
> feedback loops (short term)
> Feed forward activation (short term)
> allosteric regulation (short term)
> phosphorylation-dephosphorylation sequence (short term)..aka post-translational modification
> proteolysis (long term)
> Changes in gene expression (long term)
What enzyme does phosphorylation require? dephosphorylation?
> Kinase
> Phosphotases
What do irreversible inhibitors do?
Form covalent bonds
What happens to km and Vmax in competitive inhibitors
Km= increases
Vmax=unchanged
> More substrate required to saturate enzyme
What happens to km and Vmax in non-competitive inhibitors
km=unchanged
Vmax=decreases
What is an isoenzyme
Different enzymes the catalyze the same reaction but are subject to different regulatory controls (ex: DAHP synthase for aromatic amino acids)
mnemonic to remember classes of enzymes?
Over The Hills Live Intelligent Ladies
Oxidoreductases, Transferases, Hydrolyses, Lyases, Isomerases, Ligases
3 main uses of lipids
> storage of energy
> forming membranes
> signalling between and within cells