Ch. 10 Microbial Metabolism

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75 Terms

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metabolism

all of the chemical reactions and physical workings of the cell

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anabolism

. biosynthesis: synthesis of cell molecules and structures

. requires energy input

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catabolism

. breaks the bonds of larger molecules

. releases energy

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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

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examples of catabolism

. glycolysis

. Kreb’s cycle

. Respiratory chain

. Fermentation

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catalysts

speed up the rate of chemical reactions without becoming part of the products or being consumed in the reaction

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enzymes

overcome activation energy, allowing reaction to proceed

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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

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substrates

reactant molecules upon which enzymes act

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simple enzymes

consist of protein alone

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conjugated enzymes

contain protein and some other nonprotein molecule

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holoenzymes

whole enzymes

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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

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cofactor

. the nonprotein portion of the holoenzyme

. can be organic or inorganic

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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

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inorganic cofactor

metal ions

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each enzyme has a different…

  1. primary structure

  2. variation in folding

  3. unique active site

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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

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6 classes of enzymes:

  1. oxidoreductases

  2. transferases

  3. hydrolases

  4. lyases

  5. isomerases

  6. ligases

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oxidoreductases

transfer electrons from one substrate to another

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dehydrogenases

transfer a hydrogen from one compound to another

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transferases

transfer functional groups from one substrate to another

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hydrolases

cleave bonds on molecules with the addition of water

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lyases

add groups to or remove groups from double-bonded substrates

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isomerases

change substrates to their isometric form

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ligases

catalyze the formation of bonds with the input of ATP and the removal of water

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Lactase

hydrolase, breaks down lactose into glucose and galactose

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Penicillinase

hydrolase, Hydrolyzes beta-lactam ring

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DNA polymerase

transferase; synthesizes a strand of DNA using the complimentary strand as a model

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lactate dehydrogenase

oxidoreductase; catalyzes the conversion of pyruvic acid to lactic acid

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oxidase

oxidoreductase; catalyzes the reduction of O2 (addition of electrons and hydrogen)

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oxidation

loss of electrons (OIL-oxidation involves loss)

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reduction

gain of electrons (RIG- reduction involves gain)

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coenzyme carriers

NAH and FAD

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exoenzymes

. transported extracellularly

. break down large food molecules or harmful chemicals

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endoenzymes

. retained intracellularly and function there

. most enzymes of metabolic pathways

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constitutive enzymes

always present in relatively constant amounts, regardless of cellular environment

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regulated enzymes

. production is turned on (induced) or turned off (repressed) in response to changes in concentration of substrates

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pathogens role with enzymes

secrete unique exoenzymes that help them avoid host defenses or promote multiplication in tissues

. some enzymes function as toxins

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nonfunctional enzymes

block metabolic reactions and can lead to cell death

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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

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noncompetitive inhibition

. a regulatory molecule binds to the regulatory site and changed the conformation of active site so that substrates cannot enter

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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

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enzyme induction

enzymes appear only when suitable substrates are present

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exergonic reactions

. release energy as they go forward

. energy is available for doing cellular work

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endergonic reactions

require the addition of energy to move forward

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reduced compounds

have more energy than they did in their oxidized state

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dehydrogenation

the removal of hydrogens from a compound during a redox reaction

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NAD

. most common electron carrier

. carries hydrogens and a pair of electrons from dehydrogenation reactions

. reduced NAD is presented as NADH+

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FAD

. electron carrier

. reduced FAD is presented as FADH+

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NADP

NAD phosphate

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aerobic respiration

converts: glucose to CO₂

final electron acceptor: oxygen

pathways: glycolysis, the Krebs cycle, and respiratory chain

maximum net yield: 36-38 ATP

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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

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adenosine triphosphate

. adenine-base pair

. ribose- 5-carbon sugar

. three phosphate groups bound to ribose

. removal of the phosphates releases free energy

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substrate-level phosphorylation

generation of ATP through a transfer of a phosphate group from a phosphorylated compound directly to ADP

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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

.

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photophosphorylation

ATP formed through a series of sunlight-driven reactions in phototrophs

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3 basic catabolic pathways

  1. aerobic respiration

  2. anaerobic respiration

  3. fermentation

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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

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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

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carbohydrates are good fuels because they…

. are readily oxidized

. are good hydrogen and electron donors

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The Krebs Cycle

  1. Pyruvic acid is converted to acetyl coenzyme A (acetyl CoA) before it enters the Krebs Cycle

  2. oxidation reaction releases the first CO₂ molecule

  3. a cluster of enzymes and coenzyme A dehydrogenate pyruvic acid to a 2-carbon acetyl group

  4. NAD is reduced to NADH

  5. 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

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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

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sequence of electron carriers in the respiratory chain of most aerobic organisms

  1. NADH dehydrogenase

  2. flavin mononucleotide (FMN)

  3. coenzyme Q

  4. cytochrome b

  5. cytochrome

  6. cytochrome c

  7. cytochrome a

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ATP synthase

. stationed along the membrane in close association with the ETS carriers

. captures released energy from the ETS carriers

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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)

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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

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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

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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

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homolactic fermentation

lactic acid bacteria reduce pyruvate to lactic acid mainly

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heterolactic fermentation

glucose is fermented to a mixture of lactic acid, acetic acid, and carbon dioxide

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lipases

break apart fatty acids joined to glycerol

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beta oxidation

oxidation of fatty acids

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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