JSR - Bio 101 - Enzymes with Protein Review

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Last updated 1:58 AM on 7/8/26
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37 Terms

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Active site

Location where substrate binds to.

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Denaturing

The shape or structure of the enzyme is changed due to extremes in temperature, pH or salinity; enzyme is unable to execute its function.

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lock and key theory

One substrate fits one enzyme;

enzymes can only catalyze one biochemical reaction.

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Enzyme

globular protein;

Catalyzes chemical reactions

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Activation energy

the energy put into reactants to get a reaction started

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Induced fit model

model that describes how enzymes may act on one or more similarly-shaped substrates and catalyze similar reactions

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Substrate

reactant that binds to the enzyme's active site

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Primary Structure

sequence of amino acids connected by peptide bonds

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Secondary structure

one of two shapes formed as a result of hydrogen bonding between the carboxyl of one amino acid and the amine of another. .

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Alpha Helix

coiled shape held together by hydrogen bonding between every fourth amino acid

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Beta pleated sheet

accordion shape formed due to hydrogen bonds.

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Tertiary Structure

complex globular shape due to R group interactions.

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Quaternary structure

Two or more polypeptide chains held together by R group interactions

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Insulin

Hormone (sends signals) - Controls sugar level

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Antibodies (Immunoglobulins)

Defense - Part of immune response.

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Spider Silk

Strong structural protein

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Collagen

Strength and structure in skin

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Amino acid sequence of polypeptides is coded for by ______________.

DNA

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temperature

increases cause increasing activity up to the optimum; beyond optimun rapid denaturing occurs

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pH

denaturing occurs on either side of optimum as increases or decreases disrupt hydrogen bonds

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endergonic

reactions where products store more energy than the reactants

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exergonic

reactions that release energy

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metabolism

the sum of all chemical processes that occur in an organism

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competitive inhibitor

A substance that reduces enzyme activity by binding to the active site in place of the substrate.

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noncompetitive inhibitor

A substance that reduces enzyme activity by binding to a location away from the active site. Binding changes the shape of the active site so that the substrate can not bind.

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example of a competitive inhibitor

sarin gas bind to the active site on acetylcholinesterase; prevents muscle contraction.

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example of non-competitive inhibitor

cyanide binds to cytochrome c in cellular respiration; changes the shape of the active site such that the substrate cannot bind.

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How can competitive inhibition be overcome?

add more substrate

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end product inhibition

The regulation of metabolic pathways where the last product in a sequence of enzyme-controlled reactions becomes an inhibitor of one of the enzymes earlier in the sequence; prevents the production of two much product.

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Number of amino acids used by living things to make proteins

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condensation

process that combines amino acids into dipeptides or polypeptides by removing water

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hydrolysis

process that breaks polypeptides or dipeptides into amino acids by adding water

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denaturing

changing the shape of a protein through, pH, temperature, or salt concentration changes thus making it ineffective

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metabolic pathway

chains or cycles of enzyme-mediated reactions

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graph showing an endergonic reaction

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graph showing an exergonic reaction

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graph showing activation energy

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