chapter 4- enzymes Flashcards

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1
Q

what are enzymes made up of

A

amino acids=proteins (globular proteins)

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2
Q

are enzymes made up of high molecular weight

A

yes

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3
Q

what do globular proteins have

A

a spherical shape, alpha helix molecules, 1y, 2y and 3y structure- hydrogen, ionic and disulphide bonds

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4
Q

what do intracellular enzymes do

A

the synthesis of polymers into monomers in cells?????

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5
Q

what does anabolic mean

A

building up molecules it is required for growth

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6
Q

what does catabolic mean

A

breaking down molecules into sub units

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7
Q

eg of work down by a catabolic enzyme

A

digestion- amalase breaks carbohydrates into starch then glucose

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8
Q

eg of work down by anabolic enzymes

A

nail growth

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9
Q

what are enzymes

A

biological catalysts that speed up the ror without getting used up in the reaction and changing the produced substances.

An enzyme is a protein that acts as a catalyst, increasing the rate of a biochemical reaction.
It does this by lowering the activation energy.

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10
Q

what is enzymes specificity

A

the ability of an enzyme to select a specific substrate from a range of chemically similar compounds

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11
Q

what is a cofactor

A

a non protein chemical compound or metallic ion that is required for the enzymes activity as a catalyst. they can be considered as helper molecules that assist in biochemical reactions

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11
Q

what is a holoenzyme

A

refers to the active enzyme with its nonprotein component.

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11
Q

what is an apoenzyme

A

is an inactive enzyme without its nonprotein part

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12
Q

what is an enzyme

A

a protein that acts as a catalyst increasing the rate of a biochemical reaction by lowering the activation energy

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13
Q

Why is the tertiary structure of enzymes important?

A

the active site has a specific tertiary structuee which is complementary to a specific substrate enabling an enzyme-substrate complex

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14
Q

what is an active site

A

the group of amino acids that make up the region where a substrate fits to catalyse a reaction

An active site is the region on an enzyme where a substrate fits to catalyse a reaction
The shape of the active site is determined by the enzyme’s tertiary structure

15
Q

what does the lock and key hyphothesis state

A

that the binding of the substrate with the enzyme occurs because the active site has a shape which is complementary to the shape of the substrate meaning the substrate fits the active site like a key fits a lock

The lock and key hypothesis says that the active site and substrate have fixed shapes that are complementary

16
Q

what does the induced fit hyphothesis state

A

that the interaction between the substrate and the tertiary structure of the enzyme causes the shape of the active site to change slightly allowing the substrate to “fit”

The induced-fit hypothesis says that when the substrate starts to bind to the active site, the shape of the active site changes. This puts stress on the bonds in the substrate and makes them easier to break. This lowers the activation energy.

17
Q

what is a substrate in the context of enzymes

A

a substance that is acted on or used by another substance or process

18
Q

define activation energy

A

the energy required to bring about a reaction

Activation energy is the minimum amount of energy required to bring about a reaction.

19
Q

what is a competitive inhibitor

A

an inhibitor that binds to the active site of an enzyme

20
Q

what is a non-competitive inhibitor

A

an inhibitor that binds to an enzyme but not at the active site at an allosteric site

21
Q

what are coenzymes

A

organic molecules such as vitamins loosely bound to enzymes allowing them to by catalytic

22
Q

what are cofactors

A

inorganic ions which combine with apoenzyme to activate it forming holoenzyme

23
Q

example of a cofactor

A

chloride ion for amylase

24
Q

what is a prosthetic group

A

inorganic ion or organic molecules that are tightly bound to the enzymes

25
Q

xample of a prosthetic group for an enzyme

A

zinc ion for carbonic anhydrase

26
Q

is amylase intra or extracellular

A

extra

27
Q

is catalase intra or extracellular

A

intra

28
Q

are vitamins a source of coenzymes

A

yes

29
Q

is Cl- a cofactor for carbonic anhydrase

A

no it is for amylase

30
Q

do Both inorganic ions and coenzymes bind temporarily to enzymes.

A

yes

31
Q
A