Enzymes Flashcards

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1
Q

enzymes are

A

biological catalysts

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2
Q

advantages of enzymes as inorganic catalysts

A

specific to 1 catalytic reaction, don’t produce a range of unwanted byproducts, a lot faster

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3
Q

extracellular enzymes

A

some enzymes are secreted from the cells where they’re made and act on their substrates extracellularly

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4
Q

why are enzymes specific in their action

A

each have a specifically shaped active site that is complementary only to the shape of the substrate molecule

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5
Q

why are enzymes described as biological catalysts

A

speed up reactions by up to 10^12 times at lower temperatures, neutral pH and normal pressures
able to function in conditions that sustain life
unchanged and reusable at end of reaction

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6
Q

turnover number of an enzyme

A

the number of moles of substrate converted to product per mole of enzyme per second under conditions at which the concentration of all substrates is saturating

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7
Q

why a non-functioning enzyme may cause serious disease

A

a metabolic disease due to genetic mutations which don’t allow the enzyme to catalyse chemical functions in the body to work normally

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8
Q

activation energy

A

chemicals need energy to activate reaction in order to increase kinetic energy of the molecules so they move more and are likely to collide then reaction more successfully- enzymes lower this to speed up metabolic reactions

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9
Q

Cofactor

A

Any substance that must be present to ensure enzyme-controlled reactions take place at the appropriate rate- non-protein

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10
Q

Coenzymes

A

Small, organic, non-protein molecules

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11
Q

Prosthetic groups

A

A cofactor permanently bound to an enzyme

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12
Q

Enzyme inhibitor

A

Any substance or molecule that slows down the rate of an enzyme controlled reaction by affecting the molecule in some way

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13
Q

Multi-enzyme complexes

A

Increase efficiency of metabolic reactions without increasing substrate concentration as they keep the enzyme and substrate molecules within the same vicinity and reduce diffusion time

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14
Q

Why are many metabolic reactions carried out in particular regions or organelles

A

Increases efficiency of metabolism and some of the enzymes within organelles are bound into the organelle membrane

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15
Q

Allosteric site

A

Region of an enzyme away from the active site where a non-competitive inhibitor may attach

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16
Q

Inactivators

A

When permanent inhibitors denature the enzyme they are called

17
Q

Medical drugs that act by enzyme inhibition

A

Aspirin, ATPase inhibitors, ACE inhibitors, protease inhibitors, nucleoside reverse transcript inhibitors

18
Q

Active site

A

Indebted area on the surface of an enzyme molecule with a shape that is complementary to the shape of the substrate molecule

19
Q

Catalyst

A

Chemical that speeds up the rate of a reaction and remains unchanged and reusable at the end of a reaction

20
Q

Metabolic/metabolism

A

The chemical reactions that take place inside living cells or organisms

21
Q

Product

A

Molecule produced from substrate molecules by an enzyme-catalysed reaction

22
Q

Substrate

A

Molecule that is altered by an enzyme-catalysed reaction

23
Q

Enzyme-substrate complex

A

Complex formed by temporary binding of enzyme and substrate molecules during an enzyme-catalysed reaction

24
Q

Enzyme-product complex

A

Enzyme molecule with product molecules in its active site joined temporarily by non-covalent forces

25
Q

Q10

A

Temperature coefficient calculated by dividing the rate of reaction at (T+10)’C by the rate at T’C

26
Q

Concentration

A

Number of molecules per unit volume

27
Q

Competitive inhibition

A

Inhibition of an enzyme where the inhibitor molecule has a similar shape to the substrate and competes with it for the enzymes active site preventing formation of ES complexes

28
Q

Inhibitor

A

A substance that reduces or stops a reaction

29
Q

Non-competitive inhibition

A

Inhibition of an enzyme where the competitor molecule attached to a part of the enzyme but not the active site, if changes the shape of the active site which prevents ES complexes forming as it’s no longer complementary in shape

30
Q

3 ways inorganic ion cofactors increased the rate of enzyme-catalysed reactions

A

certain ions, co-substrates, changing charge distribution