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All chemical reactions and physical workings of the cell
Metabolism
Anabolism: Biosynthesis:
synthesis of cell molecules and structures
· Requires energy input
Catabolism
Break the bonds of larger molecules
° Releases energy
Speed up the rate of a chemical reaction without becoming part of the products or being consumed in the reaction
Catalysts
Enzymes overcome the activation energy allowing the reaction to proceed by:
Increasing thermal energy to increase the velocity of molecules
o Increasing the concentration of reactants to increase the rate of molecular collisions
· Adding a catalyst
Enzyme Characteristics
Composed of protein; may require cofactors
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 target molecules (substrates)
Are not used up or permanently changed by the reaction
Can be recycled
Are greatly affected by temperature and pH
Can be regulated by feedback and genetic mechanisms
Substrates:
reactant molecules upon which enzymes act
Enzymes bind to substrates and participate directly in
changes to the substrate
note: Does not become part of the products, Is not used up by the reaction, Can function over and over again
METALLIC COFACTORS consist of
Iron, copper, magnesium, manganese, zinc, cobalt, selenium,etc.
ICMMZCS
METALLIC COFACTORS Assist with
precise functions between enzyme and substrate
· Activate enzymes
. Help bring the active site and substrate close together
. Participate directly in chemical reactions
COENZYMES
Organic compounds that work with the apoenzyme to alter the substrate
COENZYMES do what
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 of coenzymes
Simple enzymes: consist of
protein alone
Conjugated enzymes (holoenzyme): contain
protein and some other nonprotein molecule
Apoenzyme
protein portion of the enzyme
Cofactor
nonprotein portion; organic or inorganic (metal ions)
Coenzyme
organic cofactors
Oxidoreductases:
transfer electrons from one substrate to another, and dehydrogenases transfer a hydrogen from one compound to another
Transferases:
transfer functional groups from one substrate to another
cleave bonds on molecules with the addition of water
Hydrolases
Lyases:
add groups to or remove groups from double-bonded substrates
Isomerases:
change a substrate to its isomeric form
catalyze the formation of bonds with the input of ATP and the removal of water
ligases
Exoenzymes:
· Transported extracellularly
· Break down large food molecules or harmful chemicals
Retained intracellularly and function there
· Most enzymes of metabolic pathways
Endoenzymes
Always present in relatively constant amounts, regardless of the cellular environment
Constitutive enzymes
Regulated enzymes
Production is turned on (induced) or turned off (repressed) in response to changes in concentration of substrate
Role of Microbial Enzymes in Disease:
Pathogens secrete unique exoenzymes that help them avoid host defenses or promote multiplication in tissues
Considered virulence factors or toxins because they contribute to disease
EXAMPLES:
· Streptokinase- digests blood clots
· Elastase & collagenase- digest elastin and collagen
Weak bonds that maintain the shape of an apoenzyme are broken by heat, low or high pH, or certain chemicals
Denaturation
Disruption causes distortion of
the enzyme's shape.
Prevents the substrate from attaching to the active site
Nonfunctional enzymes block ______ and can lead to cell death
metabolic reactions
Competitive inhibition:
A molecule that resembles the substrate occupies the active site, preventing the substrate from binding
Enzyme cannot act on the inhibitor and is effectively shut down
Non competitive inhibition
Some enzymes have two binding sites-the active site and the regulatory site
Regulated by the binding of molecules other than the substrate to the regulatory site
Non competitive inhibition: Often, the ______ ______ is the product of the enzymatic reaction
regulatory molecule
Provides negative feedback that slows enzyme activity once a certain concentration of product is reached
Controls on Enzyme Synthesis: 2 terms
repression and inudction
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 repressed
Response time is longer than for feedback inhibition, effects more enduring
INDUCTION
Enzymes appear (are induced) only when suitable substrates are present
Synthesis of an enzyme is induced by its substrate
Inverse of enzyme repression
release energy as they go forward
· Energy is available for doing cellular work
Exergonic reactions
Endergonic reactions:
. Require the addition of energy to move forward
· Exergonic and endergonic reactions are often coupled
ATP aka Adenosine Triphosphate
3 part molecule
Adenine: nitrogen base
Ribose: 5 carbon sugar
In ATP, 3 phosphate groups bonded to the ribose
They’re bulky and have a NEGATIVE charge
Repelling electrostatic charges imposes a strain between the last 2 phosphate groups
Removal of phosphates releases free energy
Metabolic Role of ATP:
Primary energy currency of the cell
When it is used in a chemical reaction, it must be replaced
ATP utilization and replenishment is an ongoing cycle
generation of ATP through a transfer of a phosphate group from a phosphorylated compound directly to ADP
Substrate-level phosphorylation
-a series of redox reactions occurring during the final phase of the respiratory pathway
Oxidative phosphorylation
Photophosphorylation
ATP formed through a series of sunlight-driven reactions in phototrophs
3 basic catabolic pathways
aerobic respiration
anaerobic respiration
fermentation
_____ is the most common pathway used to break down glucose
glycolysis
AEROBIC RESPIRATION
Series of reactions that converts glucose to CO2 and allows the cell to
recover significant amounts of energy
Glycolysis
The Krebs cycle
Respiratory chain
Utilizes glycolysis
the Krebs cycle and the respiratory chain but does not use molecular oxygen as the final electron acceptor
Final electron acceptor: NO-3
ANAEROBIC RESPIRATION
Fermentation Pathway
Facultative and aerotolerant anaerobes
Uses only glycolysis
Oxygen is not required; use organic compounds as electron acceptor
Nitrite and Nitrate Reduction Systems
Nitrate reductase catalyzes the reaction of nitrate to nitrite and water
Testing for this is one major physiological tests of bacteria ID
The Four Stages of Cellular Respiration
Glycolysis
Preparatory Reaction
The Citric Acid Cycle
Electron Transport Chain
Glycolysis
· Breakdown of glucose into pyruvate, 2 ATP
Preparatory Reaction
. Pyruvate is oxidized- CO2 and NADH formed
The Citric Acid Cycle
· 2 ATP produced
Electron Transport Chain
. H20 created, 32 ATP generated
in eukaryotes, glycolysis occurs in the
cytoplasam
. Glucose (6 carbons) broken down into
two molecules of pyruvate (3 carbons)
. Divided into:
. Energy-investment steps
. Energy-harvesting steps
Energy-investment step
· 2 ATP transfer their phosphates to glucose
Energy-harvesting step
. Substrate-level ATP synthesis produces 4 ATP
. Net gain of 2 ATP
. 2 NADH made
Krebs cycle
also known as the citric acid cycle,
a series of chemical reactions that extract energy from molecules like acetyl-CoA. It's a crucial part of cellular respiration, occurring in the mitochondria of cells.
The cycle converts acetyl-CoA into carbon dioxide, releasing energy that's captured in molecules like NADH, FADH2, and ATP.
The incomplete oxidation of glucose or other carbohydrates in the absence of oxygen
Uses organic compounds as the terminal electron acceptors
Yields a small amount of ATP
What is this process called?
Fermentation
Occurs in yeast or bacterial species that have metabolic pathways for converting pyruvic acid to ethanol
alcohol fermentation
products of alcoholic fermentation
Decarboxylation of pyruvic acid to acetaldehyde
Reduction of acetaldehyde to ethanol
NADH formed during glycolysis is oxidized, regenerating NAD and allowing glycolysis to continue
In alcoholic fermentation, pathways are
extremely varied
Homolactic fermentation:
Lactic acid bacteria reduce pyruvate to lactic acid only
Heterolactic fermentation:
glucose is fermented to a mixture of lactic acid, acetic acid, and carbon dioxide
Lipases break apart and fatty acids are
joined to glycerol
Glycerol converted to dihydroxyacetone phosphate which can enter step 4 of glycolysis
Beta oxidation:
Oxidation of fatty acids
2-carbon units transferred to coenzyme A, creating acetyl CoA, which
enters the Krebs cycle
Oxidation of a 6-carbon fatty acid yields 50 ATP, compared to 38 for a 6-
carbon sugar
Protein catabolism: Proteases break down
Break down proteins to their amino acid components.
Amino groups removed through deamination
Remaining carbon compound can be easily converted to one of several
Krebs cycle intermediates
Amphibolism:
° Most catabolic pathways contain strategic molecular intermediates that can
be diverted into anabolic pathways
A given molecule can serve multiple purposes to derive
maximum benefit from all nutrients and metabolites.
_____ and ____pathways are integrated to improve cell efficiency
Catabolic and anabolic
cellular building blocks (2)
pyruvate, acetyl CoA
Pyruvate is a precursor, it provides
Provides intermediates for amino acids
Gluconeogenesis (gluco-neo-genesis)
pyruvate is starting point for glucose synthesis in the event of inadequate glucose supply
Acetyl CoA is a precursor:
. Can be converted into one of several amino acids
. Can be condensed into hydrocarbon chains for fatty acid and lipid synthesis
Precursors to DNA and RNA:
. Pathways that synthesize purines and pyrimidines originate in amino acids
· Can be dependent on intermediates from the Krebs cycle
During times of carbohydrate deprivation, organisms can convert amino acids to
intermediates of the Krebs cycle and derive energy from proteins
Carbohydrate Biosynthesis:
Crucial role of glucose in metabolism/energy utilization:
. ensured by several alternative pathways
. Major component of cellulose cell walls and storage granules
· Glucose-6-P used to form glycogen
Protein Synthesis
· Large proportion of a cell's constituents
° Essential components of enzymes, cytoplasmic membrane, cell wall, and cell appendages
o 20 amino acids are needed to make these proteins
Cell division: (process)
· Two cells need twice as many ribosomes, enzymes, etc.
o Cell wall and membranes nearly double
o Phospholipid bilayer components assemble spontaneously with no energy input
o Proteins and other components must be added to the membranes
o Cell wall growth requires energy input
______ ______photosynthesis
· Chlorophyll needed
. ATP is produced
Light Dependent photosynthesis
Light Independent photosynthesis
. "Calvin Cycle"
· Energy from ATP reduces CO2
The main events of the light reaction shown as an exploded view in one granum.
1.When light activates photosystem II, it sets up a chain reaction, in which electrons are released from chlorophyll.
2.These electrons are transported along a chain of carriers to photosystem I.
3.The empty position in photosystem II is replenished by photolysis of H2O. Other products of photolysis are O2 and H+.
4.Pumping of H+ into the interior of the granum produces conditions for ATP to be synthesized.
5.The final electron and H+ acceptor is NADP, which receives these from photosystem I.
6.Both NADPH and ATP are fed into the stroma for the Calvin cycle.
Oxygenic (oxygen-releasing) photosynthesis:
. Dominant type on earth
. Occurs in plants, algae, and cyanobacteria
Anoxygenic photosynthesis:
· Occurs in green and purple bacteria that utilize bacteriochlorophyll
· Have only cyclic photosystem I
. Generate a small amount of ATP
· Use H2, H2S, or elemental sulfur as an electron source
. Many are strict anaerobes