METABOLIC REACTIONS, BIOMOLECULES & ENERGY PRODUCTION Flashcards
(22 cards)
what are ions?
electrically charged particles
positive / negative charge
cations / anions
molecules / compounds
containing 2 or more elements / molecule made of different elements
acids
more H+ / liberates H+ when mixed with water
bases
less H+ / takes up H+ ion released from acid
synthesis / anabolism
chemical reactions where molecules are added together to form new molecules
catabolism
when one molecule is broken down into smaller molecules
metabolism
sum of biochemical process which produce/consume energy
energy
transferred to ATP which is storage form of energy
molecules of life
proteins, lipids/fats, carbs
biomolecule
any molecule made within an organism
carbs
general formula CHO (1:2:1)
provides glucose, raw energy needed for energy production
smaller in size the more soluble
approx 1-2% cell mass
types of carbs
monosaccharides -> smallest
e.g. glucose, fructose, galactose, deoxyribose & ribose
combine to form disaccharides
disaccharides -> 2 mono are joined & water molecule removed
e.g. maltose, sucrose, lactose
too large to pass through cell membrane
digested via hydrolosis (add water molecule to break bond & release mono)
polysaccharide -> chains of simple sugars linked by dehydration synthesis
e.g. starch, glycogen, cellulose
used as storage products e.g. glycogen stored in muscle/liver and released when needed
fats / lipids
insoluble organic molecules
e.g. triglycerides, phospholipids, cholesterol
types of fats/lipids
triglycerides (neutral fats) -> protect internal organs, stores energy fuel, insulates, building blocks are 3 fatty acid chains attached to glycerol molecule
phospholipids -> modified triglycerides whihc one fatty acid chain replaced by phosphate group
also known as phosphoglycerides - non polar fatty chain & phosphate polar portion
form cell membrane
cholesterol -> most important steroid molecule - ingested in animal products
structure consists of 4 interconnected carbon rings
plays role in stabilisation of cell membranes
synthesise steroid hormones e.g. sex hormones, vit D, bile
proteins
prime importance
10-30% cell mass
response for multiple physiological functions
e.g. enzymes, antibodies, blood proteins
formed from 20 different amino acid building blocks
structure of proteins
primary -> determined by the sequence of amino acids connected by peptide bonds to from a polypeptide chain
secondary -> depending on the sequence of the amino acids the protein may use hydrogen bonds to form a secondary structure consisting of coils or pleats
tertiary -> final dimensional shape determined by variety of bonding interactions between ‘side chains’ on amino acids
bonds can be stronger than the hydrogen bonds & this the protein will bend, fold & loop
the 4 types of bonding interactions between “side chains” include:
hydrogen bonding, disulphide bonds, salt bridges, & non-polar hydrophobic interactions
quaternary -> combination of 2 or more chains to form complete unit
interactions between the chains are not different from those in tertiary structure, but a distinguished only by being interchain rather than intrachain
e.g. haemoglobin
what are proteins vulnerable to?
high temps, change in pH, various chemicals, radiation
examples of polypeptides in body
body’s natural painkillers
e.g. encephalins & endorphins
polypeptides bind to receptors in brain to provide temporary relief
endorphins may produce sedative effect by prevention of release of substance P which transmits pain signals to brain
pituitary gland produces nonapeptides vasopressin & oxytocin
examples of enzymes
unique 3D shape that binds with a small group of reacting molecules (substrates)
much larger than substrates
affected by changes in pH, temp & some chemicals
vitamins & coenzymes
water/fat soluble
water soluble vit not stored in body
water soluble vits are required by many enzymes as co-factors to carry out catalytic reactions
catabolic reactions
stage 1 -> digestion where enzymes break down large molecules into smaller ones
polysaccharides -> glucose
fats -> fatty acids & glycerol
proteins -> amino acids
digested products then diffuse across bloodstream
stage 2 -> newly delivered nutrients are either:
built into lipids, protein & glycogen by anabolic pathways
or broken down by catabolic pathways to pyruvic acids & acetyl CoA into cell cytoplasm
digestion products are further broken down to yield 2 to 3 carbon compounds
e.g. pyruvate & acetyl CoA
stage 3 -> major production of energy happens in mitochondria
2 carbon acetyl group is oxidised in the citric acid cycle, which produces coenzymes NADH & FADH2
as long as the cells have an adequate supply of oxygen, electrons & hydrogen ions from the reduced coenzymes are transferred to the electron transport chain to phosphorylate ADP to ATP