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metabolism
all of the chemical reactions and physical workings of the cell
anabolism
. biosynthesis: synthesis of cell molecules and structures
. requires energy input
catabolism
. breaks the bonds of larger molecules
. releases energy
metabolism functions
. assembles smaller molecules into larger molecules for the cell, using ATP to form bonds (anabolism)
. breaks down macromolecules into smaller molecules, a process that yields energy (catabolism)
. collects and spends energy in the form of ATP or heat
examples of catabolism
. glycolysis
. Kreb’s cycle
. Respiratory chain
. Fermentation
catalysts
speed up the rate of chemical reactions without becoming part of the products or being consumed in the reaction
enzymes
overcome activation energy, allowing reaction to proceed
characteristics of enzymes
. most are made of protein and may require cofactors
. act as organic catalysts to speed up the rate of cellular reactions
. lower the activation energy required for a chemical reaction to proceed
. have unique characteristics such as shape, specificity, and function
. enable metabolic reactions to proceed at a speed compatible with life
. have an active site for substrates
. much larger than substrates
. are not used up permanently or changed by the reaction
. greatly affected by temperature and pH
. can be regulated by feedback and genetic mechanisms
substrates
reactant molecules upon which enzymes act
simple enzymes
consist of protein alone
conjugated enzymes
contain protein and some other nonprotein molecule
holoenzymes
whole enzymes
apoenzyme
. the protein portion of the holoenzyme
. where the substrate bonds
. three-dimensional site where the crevice or groove formed by the way amino-acids are folded
cofactor
. the nonprotein portion of the holoenzyme
. can be organic or inorganic
coenzyme
. organic cofactor
. work with the apoenzyme to to alter the substrate
. remove a chemical group from one substrate and add it to another substrate
. carry and transfer hydrogen atoms, electrons, carbon dioxide, and amino groups
. vitamins are an important component
inorganic cofactor
metal ions
each enzyme has a different…
primary structure
variation in folding
unique active site
metallic cofactors
. iron, copper, magnesium, manganese, zinc, cobalt, selenium, etc.
. assist with precise functions between enzyme and substrate: activate enzymes, help bring the active site and substrate close together, participate directly in chemical reactions
6 classes of enzymes:
oxidoreductases
transferases
hydrolases
lyases
isomerases
ligases
oxidoreductases
transfer electrons from one substrate to another
dehydrogenases
transfer a hydrogen from one compound to another
transferases
transfer functional groups from one substrate to another
hydrolases
cleave bonds on molecules with the addition of water
lyases
add groups to or remove groups from double-bonded substrates
isomerases
change substrates to their isometric form
ligases
catalyze the formation of bonds with the input of ATP and the removal of water
Lactase
hydrolase, breaks down lactose into glucose and galactose
Penicillinase
hydrolase, Hydrolyzes beta-lactam ring
DNA polymerase
transferase; synthesizes a strand of DNA using the complimentary strand as a model
lactate dehydrogenase
oxidoreductase; catalyzes the conversion of pyruvic acid to lactic acid
oxidase
oxidoreductase; catalyzes the reduction of O2 (addition of electrons and hydrogen)
oxidation
loss of electrons (OIL-oxidation involves loss)
reduction
gain of electrons (RIG- reduction involves gain)
coenzyme carriers
NAH and FAD
exoenzymes
. transported extracellularly
. break down large food molecules or harmful chemicals
endoenzymes
. retained intracellularly and function there
. most enzymes of metabolic pathways
constitutive enzymes
always present in relatively constant amounts, regardless of cellular environment
regulated enzymes
. production is turned on (induced) or turned off (repressed) in response to changes in concentration of substrates
pathogens role with enzymes
secrete unique exoenzymes that help them avoid host defenses or promote multiplication in tissues
. some enzymes function as toxins
nonfunctional enzymes
block metabolic reactions and can lead to cell death
competitive inhibition
. a molecule that resembles the substrate (the mimic) occupies the active site. preventing the substrate from binding
. enzyme cannot act on the inhibitor as is shut down
noncompetitive inhibition
. a regulatory molecule binds to the regulatory site and changed the conformation of active site so that substrates cannot enter
enzyme repression
. stops further synthesis of an enzyme somewhere along its pathway
. If the end product of an enzymatic reaction reaches excess, the genetic apparatus for replacing enzymes is suppressed
enzyme induction
enzymes appear only when suitable substrates are present
exergonic reactions
. release energy as they go forward
. energy is available for doing cellular work
endergonic reactions
require the addition of energy to move forward
reduced compounds
have more energy than they did in their oxidized state
dehydrogenation
the removal of hydrogens from a compound during a redox reaction
NAD
. most common electron carrier
. carries hydrogens and a pair of electrons from dehydrogenation reactions
. reduced NAD is presented as NADH+
FAD
. electron carrier
. reduced FAD is presented as FADH+
NADP
NAD phosphate
aerobic respiration
converts: glucose to CO₂
final electron acceptor: oxygen
pathways: glycolysis, the Krebs cycle, and respiratory chain
maximum net yield: 36-38 ATP
anaerobic metabolism
converts: glucose to CO₂
final electron acceptor: NO₃⁻, SO₄²⁻, CO₃²⁻
pathways: glycolysis, the Krebs cycle, the respiratory chain
maximum net yield: 2-36 ATP
. found in Escherichia coli
adenosine triphosphate
. adenine-base pair
. ribose- 5-carbon sugar
. three phosphate groups bound to ribose
. removal of the phosphates releases free energy
substrate-level phosphorylation
generation of ATP through a transfer of a phosphate group from a phosphorylated compound directly to ADP
oxidative phosphorylation
. a series of redox reactions occurring during the final phase of the respiratory pathway
. the coupling of ATP synthesis to electron transport
. each NADH that enters the ETS gives rise to 3 ATP molecules
.
photophosphorylation
ATP formed through a series of sunlight-driven reactions in phototrophs
3 basic catabolic pathways
aerobic respiration
anaerobic respiration
fermentation
glycolysis
. most common pathway used to break down glucose
. glucose is enzymatically converted to pyruvic acid
. may be the first phase of aerobic respiration or the primary metabolic pathway
fermentation
. uses only glycolysis
. oxygen is not required and uses organic compounds as electron acceptors
. the incomplete oxidation of glucose or other carbohydrates in the absence of oxygen
. yields a small amount of ATP
carbohydrates are good fuels because they…
. are readily oxidized
. are good hydrogen and electron donors
The Krebs Cycle
Pyruvic acid is converted to acetyl coenzyme A (acetyl CoA) before it enters the Krebs Cycle
oxidation reaction releases the first CO₂ molecule
a cluster of enzymes and coenzyme A dehydrogenate pyruvic acid to a 2-carbon acetyl group
NAD is reduced to NADH
NADH formed is shuttled to the electron transport system to produce ATP
. all reactions occur twice for each glucose molecule because two pyruvates are formed during glycolysis
. serves to transfer the energy stored in acetyl CoA to NAD+ and FAD by reducing them
products: reduced NADH and 2 ATP produced through substrate level phosphorylation
The Respiratory Chain (Electron Transport System)
. chain of special redox carriers that receives electrons from NADH
. electrons are passed sequentially from one redox molecule to the next
. flow of electrons allows the active transport of hydrogens outside the cell membrane
. oxygen receives hydrogens and electrons and produces water
sequence of electron carriers in the respiratory chain of most aerobic organisms
NADH dehydrogenase
flavin mononucleotide (FMN)
coenzyme Q
cytochrome b
cytochrome
cytochrome c
cytochrome a
ATP synthase
. stationed along the membrane in close association with the ETS carriers
. captures released energy from the ETS carriers
chemiosmosis
. as the electron transport carriers shuttle electrons, hydrogen ions are actively pumped into the space between the cell wall and the cytoplasmic membrane (periplasmic space)
proton motive force
. a concentration gradient of hydrogen ions created by chemiosmosis
. Consists of a difference in charge between the outside of the membrane (+) and the inside (−)
. Separation of charges temporarily stores potential energy
. can only diffuse into the membrane through ATP
synthase, which sets the stage for ATP synthesis
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location of ATP synthesis in eukaryotes
mitochondrial membranes, between the
mitochondrial matrix and the outer intermembrane space
total possible production of ATP from aerobic respiration
. 2 from glycolysis
. 2 from Krebs cycle
. 34 from electron transfer
. energy is used transporting NADH across the mitochondrial membrane during glycolysis
alcoholic fermentation
. occurs in yeasts or bacterial species that have metabolic pathways for converting pyruvic acid to ethanol
. decarboxylation of pyruvic acid to acetaldehyde
. reduction of acetaldehyde to ethanol
. NADH formed during glycolysis is oxidized, regenerating NAD and allowing glycolysis to continue
homolactic fermentation
lactic acid bacteria reduce pyruvate to lactic acid mainly
heterolactic fermentation
glucose is fermented to a mixture of lactic acid, acetic acid, and carbon dioxide
lipases
break apart fatty acids joined to glycerol
beta oxidation
oxidation of fatty acids
proteases
. break down proteins into their amino acid components
. amino groups removed through deamination
. remaining carbon compound can be easily converted to one of several Krebs cycle intermediates