Ch 8 Microbial Metabolism Flashcards

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1
Q

Metabolism of microbes

A

-All chemical reactions and physical workings of the cell
-Occurs through arise of enzyme-catalyzed reactions

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2
Q

Anabolism

A

-Synthesis - built up
-Biosynthesis: synthesis of cell molecules and structures
-Requires energy input
*Lipids, polysaccharides, proteins and nucleic acid

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3
Q

Catabolism

A

-Break the bonds of larger molecules
-Release energy

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4
Q

Catalysts (enzyme)

A

-Speed up the rate of a chemical reaction without becoming part of the products or being consumed in the reaction

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5
Q

Enzymes overcome the activation energy allowing the reaction to proceed by:

A

-Increasing thermal energy (heating) to increase the velocity of molecules
-Increasing the concentration of reactants to increase the rate of molecular collisions
-Adding a catalyst

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6
Q

Characteristics of Enzyme

A

-Most composed of protein; 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 an active site for target molecules (substrates)
-Associate closely with substrates but do not become integrated into the reaction products
-Are not used up or permanently changed by the reaction
-Can be recycled, thus function in extremely low concentrations
-Can be regulated by feedback and genetic mechanism

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7
Q

Substrates

A

-reactant molecules upon which enzymes act
-Bind to the active/catalytic site “ock and key” fit.

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8
Q

How do enzymes work?

A

-Bind to substrates and participate directly in changes to the substrate
-Does not become part of the products
-Is not used up by the reaction
-Can function over and over again

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9
Q

Simple enzymes

A

consist of protein alone

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10
Q

Conjugated enzyme/holoenzyme

A

-Contains protein and some other non-protein molecule
-A combination of the protein called apoenzyme and one or more cofactors

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11
Q

Apoenzyme

A

-Protein portion of the enzyme
-the actual site where the substrate binds
-three dimensional crevice or groove formed by the way amino acid chains are folded
*Each enzyme has a different primary structure, variations in folding and unique active site

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12
Q

Cofactor

A

-Non protein portion (metal ions/ in-oraganic)
-Binds to the enzyme
-increase the rate of the reactions with covalent interactions
-

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13
Q

Coenzyme

A

-Organic cofactors
-Organic non-protein molecules that carry chemical groups between enzymes
-“carriers”
-loosely bound
-made of vitamins, biotin, coenzyme A

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14
Q

Apoenzyme levels of structure

A

-Primary: polypeptide chain
-Secondary: chain begins to fold
-Tertiary: folds turn into 3D shape which creates active sites

-Quaternary: Complex enzymes consists of several polypeptide chains bound by weak forces.

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15
Q

Constitutive enzymes

A

-Present in constant amounts inside the cell

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16
Q

Regulated enzymes

A

-Concentration of regulated enzymes in cell increase or decrease in response to substrates
-Production is turned on (induced) or turned off (repressed)

17
Q

Enzyme repression

A

-Stops further synthesis of an enzyme somewhere along it’s pathway
-if product of enzymatic reaction reaches excess, the genetic apparatus for replacing enzymes is suppressed

18
Q

Enzyme induction

A

-Enzymes are induced when suitable substrates are present

19
Q

Competitive inhibition

A

-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

20
Q

Non-competive inhibition

A

-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
-Often, the regulatory molecule is the product of the enzymatic reaction
-Provides negative feedback that slows enzyme activity once a certain concentration of product is reached

21
Q
A