outcome 2 Flashcards
(40 cards)
catabolic vs anabolic
catabolic: the enzymatic breakdown of larger molecules into smaller molecules
–DECOMPOSITION+ EXERGONIC (energy releasing )
anabolic: the enzymatic synthesis of more complex molecules from simpler ones
–SYNTHESIS+ ENDERGONIC (energy requiring)
autotrophic vs heterotrophic
autographic: create own organic compounds from small inorganic molecules (plants make own food via photosynthesis)
heterotrophic: ingest/ absorb organic compounds from living or dead organisms and their by- products (animals)
what are photosynthesis and cellular res. in terms of types of reaction
PHOTOSYN:
-synthesis
-anabolic and endergonic reaction
-energy requiring
CELLLULAR RESP.:
- decomposition
- catabolic and exergonic
- release energy
what are enzymes?
they are biological catalysts so substances that speed up the rate of reaction w/o being used up
- they are proteins (most are soluble globular proteins)
- enzyme consist of one or more polypeptide chains
- tertiary structure, exception= monomeric enzyme (single polypeptide shape)
components of enzymes and what they do
- every enzyme has an active site ( substrate binding site)
- SUBSTRATE= the molecule that the enzyme acts on = INPUT to an enzyme- catalysed reaction
- PRODUCT= the OUTPUT of an enzyme catalysed reaction
group and bond specifity
bond spec. means enzyme only acts on a specific type of chemical bond and group spec. acts on molecules w/ spec. functional group near target bond
lock and key model
- simplest model to represent how an enzyme works. the substrate simply fits into the active site to form a reaction
STEPS:
1. substrate binds to enzyme active site
2. bonds in the subsrate are weakened Ae is lowered = substrate enzyme complex
2. substrate is broken products are formed
induced fit
- the combining of the enzyme and substrate results in a slight change in the shape of both
- this strained fit acts to break old chem bonds and form new ones
—> results in the formation of the product from the substrate
—-> once this occurs the product is released from enzyme and enzyme is free to combine w/ any other substrate molecule
activation energy and how enzymes lower it
the energy of the reactants required to initiate a reaction (acts as a barrier to the chem reaction occurring or speed at which it occurs)
HOW THEY LOWER AE:
enzymes carry out their function of lowering activation energy by temporally combining w/ the chemicals involved in the reaction. these chemicals are called the substrate:
…
Enzymes involved in PHOTOSYNTHESIS
- WATER OXIDIZING ENZYME: splits water molecules releasing hydrogen ions and electrons that will be built in energy- rich molecules oxygen is released as waste
- THE ATP SYNTHASE generates atp for use in photosyn
- THE RUBISCO ENZYME captures CO2 molecules from air and catalyses their conversion to organic 3 carbon molecules
cofactors + co-enzymes
cofactors:
are additional (non-protein) chemical components that are essential for ENZYME FUNCTION adding to stability and activity
CAN BE INORGANIC ex. iron in catalase, zinc in DNA polymerase
CAN BE ORGANIC which are either co enzymes and prosthetic groups
how coenzymes work
- BINDING: a co enzyme temp binds to the enzyme active site or near it
- TRANFER: during a reaction it transfer something ( like electrons hydrogen atoms, or chemical groups)
- RELEASE: after the reaction the co-enzyme is released- sometimes unchanged sometimes need to be recharged ( NAD+ –> NADH)
common co enzymes and function
ATP →ADP +pi
- energy transfer
NADH→NAD+
- transfer of electrons + proteins in cellular resp.
NADPH→NADP
- transfer of electrons + proteins in photosynthesis
FADH2→FAD
- transfer of electrons + proteins in cellular resp.
ATP
- a coenzyme
- ATP is an energy rich compound, formed in mitochondria (site for resp.)
- ATP provides the energy to drive all metabolic process in the cell
- energy is released when ATP is hydrolysed ( release energy and loses one of its phosphates as its unstable bond between last phos) into ADP +pi
loaded vs unloaded
FACTORS EFFECTING ENZYME ACTIVITY: temperature
- enzymes are proteins and as such can be denatured
- each enzyme has optimal temp depending on the ‘usual’ conditions in which the enzyme function.
Most enzymes denature above 40°
→ At low temps, not enough energy for enzyme to work
→ At high temps, the enzyme denatures (H-bonds break) due to too much energy, changing its structure - Some enzymes can reform old shapes when cooled down again
FACTORS EFFECTING ENZYME ACTIVITY: PH
Each enzyme Has an optimal pH depending on the “usual” conditions in which the enzyme function
→ This is due to increased levels of H+(acidic) or OH- (alkaline) particles, which interfere wl H-bonding of 2° and 3° structures.
- changes in pH can make and break intra- and intermolecular bonds, changing the shape of (denaturing) the enzyme and, therefore, its effectiveness
FACTORS EFFECTING ENZYME ACTIVITY: concentration
enzyme concentration: the more enzyme molecules (high conc.)the faster the reaction will proceed
substrate concentration:
high concentration will increase speed of reaction until all of the active site of the enzymes present are occupied
enzyme irreversible inhibitors:
- bind covalently (strong bond) to the enzyme active site
- causes a permant loss/ denaturation of catalytic activity – secondary/ tertiary structure is altered
- such molecules are toxic and poison to the cell
enzyme Reversible inhibitors
- bind to the enzyme via weak H-bonds and other intermoleculer bonds and can dissociate from the enzyme
- turn off a reaction but not permanently
- sometimes an end-product molecule used to slow/prevent production of a molecule that is no longer needed
—> can be competitive or non-competitive
competitive and non-competitive
competitive: compete directly w/ the substrate foe the active site
–it binds to active site blocking sub.
– HAVE SIMILAR SHAPE TO USAL SUBSTRATE THATS WHY IT CAN BIND TO ACTIVE SITE
non-competitive:
binds to enzyme not active site. changes conformational shape of enzyme, decreasing likelihood of sub. binding. HOWEVER IF IT DOES BIND NO REACTION WILL OCCUR
- the site it binds to is the allosteric site (side of enzyme)
why we regulate biochemical pathways:
precisely coordinated and regulated so that a balance is established between energy production and energy needs of the cell. Controlling enzyme activity is a major means by which regulation of biochem pathway is maintained
- prevents waste, build up in cells of products to potentially harmful lvls and depletion of substrate
what is photosynthesises and briefly describe components + stages + chlorophyll info. + equation
→ photosynthesis captures the energy in sunlight storing it as glucose. LOCATION: takes place in the chloroplast of plants and algae
→HAS TWO STAGES:
LIGHT DEPENTANT→ grana on thylakoid membranes
LIGHT INDEPENDANT (Calvin cycle)→ in the stroma
CHLOROPHYLL (green because it cannot pick up that colour)
- enables plants to capture the radient energy of sunlight, bringing it into cells as the starting point of photosyn.
- accessory pigments such as catenoids are also present they can capture sunlight energy and transfer the radiant energy they absorb to chlorophyll
6CO₂ + 12H₂O + (light energy, chlorophyll) → C₆H₁₂O₆ + 6H₂O
light dependant stage role + outputs+ inputs
takes place on the thylakoid membranes of the thylakoids and requires chlorophyll and light energy
BY THE END:
- a supply of high energy loaded ATP molecules
- a supply of high energy loaded NADPH co-enzyme
→ oxygen produced plays no further part will be released via leaves
role + outputs+ inputs:
SUNLIGHT→…
- initial input of energy to chlorophyll
NADP+→ NADPH
- NADP+ = unloaded coenzyme and acceptor of H+ and electrons
- NADPH = loaded coenzyme and doner of H+ and electrons
NADP+ +H +2e- → NADPH
ADP+pi → ATP
- ADP+pi = unloaded coenzyme ( waiting to act as a energy supplier
- ATP = loaded coenzyme and energy supplier
ADP+pi→ ATP
- atp synthase
Water→O2
- water = supplier of H+ (for NADP and atp) and electrons and O2
- O2 = (by product) by- product splitting water
coenzymes assist rubisco