Micro - Metabolism

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Last updated 4:08 AM on 10/17/26
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51 Terms

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Metabolism

all biochemical process to life

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Catabolism

breaking down big molecules (protein, carbs, lipids, fats) into smaller parts (ATP, reducing power, precursor metabolites)

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Anabolism

using small molecules (ATP, reducing power, precursors) and nutrients (CHNOPS) to make larger components (flagella, organelles)

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Energy

capacity to do work

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Photo

light energy

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Chemo

chemical energy

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Litho

inorganic electrons

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Organo

organic electrons

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Auto

CO2 as carbon source

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Hetero

organic carbon

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Energy sources

light (photosynthesis), dark (ATP, reducing power), chemical (respiration, fermentation)

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Chemical energy

respiration and fermentation

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Three types of work

chemical, transport, and mechanical

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Chemical work

polymerization of small precursor molecules for synthesis of complex molecules (amino acids -> proteins)

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Transport work

move molecules against gradient (ATP)

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Mechanical energy

rotate flagella for motility

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ATP is stood for

adenosine tri-phosphate

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ATP function

primary molecule used to conserve the energy supplied by an energy source

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ATP components

adenine, ribose, and 3 phosphate groups

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Oxidation

loss of electron

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Reduction

gain electron

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Reducing agent

molecule that donates electrons (reducing power)

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Oxidizing agent

molecule that accepts electrons

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Standard reduction potential

measure of the tendency of reducing agent to donate electron

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Good electron donators

NADH/NADPH cus they're more electronegative

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Reducing power molecules

NADH, FADH, NADPH

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NADH

donate electrons to ETC and to NADPH

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NADPH

donates electrons to other molecules

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Electron transport chain

electrons flow from electron carrier having the most negative reduction potential to the most positive carrier

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Electron carriers

direct electrons to electron acceptor, the are close together to prevent energy loss

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Enzyme

protein catalysts that have great specificity for substrates

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Catalyst

increase rate of reaction without being used up in process

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Enzyme structure

proteins and the apoenzyme and cofactor (holoenzyme)

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Apoenzyme

protein in enzyme

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Cofactor

non-protein in enzyme

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Holoenzyme

apoenzyme + cofactor

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Prosthetic group

cofactor firmly attached to apoenzyme

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Coenzyme

cofactor loosely attached to apoenzyme

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Enzyme kinetics

enzyme is specific for substrate, coenzyme picks chemical group from substrate 1 and attaches it to substrate 2, substrates are released from enzyme

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Enzyme environmental effects

amount of substrate present, temp, and pH

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Amount of substrate present

low conc or high conc of substrate

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What happens when there is a low concentration of substrate for enzymes

hard for enzyme to find substrates, slow velocity

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What happens when there is a high concentration of substrate for enzymes

easy for enzyme to find substrate, fast velocity

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What happens when temp is high for enzymes

denatures proteins

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What happens if pH is too high or too low

enzyme slows or speeds up

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Enzyme regulation

synthesis of enzyme, pre-existing enzymes/post translational, and feedback inhibition

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Synthesis of enzyme

rate of transcription or translation (gene expression) to control amount of enzymes

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pre-existing/post translational enzymes regulation

already made enzymes go through allosteric regulation and covalent modification

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Allosteric regulation

effector binds reversibly to regulatory site and causes conf. Change of enzyme, can increase or decrease enzyme activity through positive and negative effectors

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Covalent modification

addition/removal of particular chemical group

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Feedback inhibition

use pacemaker enzyme to catalyze the rate-limiting (slowest) reaction in pathway, ensures balance (supply/demand)