enzymes Flashcards

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1
Q

enzyme

A

biological catalysts
biological- all living things + proteins
catalysts- speed up reactions without change

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2
Q

substrate

A

SUBSTANCE on which an enzyme ACTS

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3
Q

enzyme substrate complex

A

when a SUBSTRATE is BOUND to the enzymes ACTIVE SITE

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4
Q

product

A

the substance(s) MADE

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5
Q

globular protein

A

roughly SPHERICAL

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6
Q

primary structure

A

sequence of AMINO ACIDS in the chains

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7
Q

secondary structure

A

folded to form ALPHA HELIX and BETA PLEATED SHEETS, held by HYDROGEN bonds

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8
Q

tertiary structure

A

form 3D shape held by HYDROGEN, IONIC, DISULPHIDE and HYDROPHOBIC bonds

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9
Q

quaternary structure

A

how some proteins are made of MORE than ONE POLYPEPTIDE chain

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10
Q

active site

A

a 3 dimensional CLEFT, formed by a few AMINO ACIDS where a SUBSTRATE BINDS

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11
Q

specific

A

only ONE TYPE of SUBSTRATE can bind

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12
Q

denaturation

A

the BREAKING of BONDS changes 3D structure of ENZYME including ACTIVE SITE, so substrate CANT BIND to form its E-S complex

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13
Q

collision theory

A

for molecules to REACT they have to COLLIDE with enough ENERGY to BREAK and FORM bonds

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14
Q

activation energy

A

energy required to START a REACTION

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15
Q

lock and key model

A

lock- ENZYME
key- SUBSTRATE

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16
Q

induced fit theory

A

where CHANGES in the SHAPE of ACTIVE SITE and SUBSTRATE brings REACTIVE groups of enzyme and substrate closer together

17
Q

metabolism

A

combination of ANABOIC and CATABOLIC reactions, happens in CELLS

18
Q

anabolic

A

the CONSTRUCTION of molecules from SMALL-LARGE units

19
Q

catabolic

A

the BREAKING DOWN of molecules from LARGE-SMALL units

20
Q

intracellular

A

INSIDE the cells

21
Q

extracellular

A

OUTSIDE the cells

22
Q

what is NON COMPETITIVE inhibition?

A

the inhibitor has a DIFFERENT shape to substrate and so binds to the enzymes ELSEWHERE to the active site. This DISTORTS the active site and so the substrate can no longer bind to it

23
Q

what is an INHIBITIOR

A

a substance which SLOWS DOWN/STOPS a reaction by affecting the BINDING of substrate to enzymes

24
Q

what is COMPETITIVE inhibition?

A

the inhibitor is a SIMILAR shape to the substrate and so COMPETES with it to fit into the active site. It can fit into the active site as it has a COMPLETMENTARY shape. Once it binds it prevents the substrate from doing so.

25
Q

what happens to the LEVEL OF COMPETITIVE INHIBITION when the concentration of substrates INCREASE?

A

it DECREASES (MORE COMPETITION) and becomes OVERCOME when substrate is in EXCESS

26
Q

what happens to the LEVEL OF NON COMPETITIVE INHIBITION when the concentration of substrates INCREASE?

A

it is UNEFFECTED because an increase in substrates DOESNT AFFECT the ability to BIND with an enzyme

27
Q

immobilised enzymes

A

enzymes that have been TRAPPED into an INERT MATRIX or MATERIAL which PREVENTS them from MOVING

28
Q

metabolism

A

all LIVING THINGS in the BODY

29
Q

catalysts

A

the LOWERING of ACTIVATION ENERGY

30
Q

metabolic pathways

A

a SERIES of ENZYME CONTROLLED reactions