Week 6 Flashcards

1
Q

__________ are catalysts involved in biochemical reactions.

A

Enzymes.

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2
Q

Enzymes are usually __________ proteins.

A

Globular.

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3
Q

__________ is a molecule or molecules that acts as the reactant in an enzymatically catalyzed reaction.

A

Substrate.

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4
Q

_____________ is the location where the enzyme binds to the substrate and catalysis occurs.

A

Active site.

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5
Q

__________ model is when the active site is already in a configuration that can only fit 1 shape of substrate.

A

Lock and key.

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6
Q

_____________ catalyze reaction involving the gain or loss of electrons.

A

Oxidoreductases.

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7
Q

_____________ transfer on functional group to another.

A

Transferases.

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8
Q

____________ cleave a bond with water.

A

Hydrolases.

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9
Q

______________ break double bond using some other means than oxidation or hydrolysis.

A

Lyases.

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10
Q

___________ catalyze a rearrangement of the molecule.

A

Isomerases.

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11
Q

__________ join two molecules.

A

Ligases.

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12
Q

___________ is a type of transferase which specifically transfers a phosphate group from ATP to another molecule and thus also has hydrolase activity.

A

Kinase.

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13
Q

An induced fit binding model requires what to be reorganized to fit what?

A

The enzyme is reorganized to fit the substrate.

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14
Q

If there is enough substrate, the enzyme will reach full saturation this is called __________

A

Saturation Kinetic Curve.

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15
Q

The _____________ is a double reciprocal of Michaelis-Menten equation and an easier method to interpret graphical data.

A

Lineweaver-Burke Plot

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16
Q

The____________ is the number of reactions the enzyme can catalyze per unit of time. Also can be used to measure catalytic efficiency.

A

Turnover number.

17
Q

____________ is an occurrence when rate-limiting step becomes the diffusion of enzyme and substrate together.

A

Diffusion controlled limit.

18
Q

____________ prevent the generation of products.

A

Inhibitors

19
Q

_____________ Covalently modifies the active site of the enzyme, irreversibly blocking its function, directly poisons the enzyme.

A

Suicide inhibitors.

20
Q

_____________ competes directly with the substrate but can be overcome if the substrate concentration is high.

A

Competitive inhibition

21
Q

_____________ binds to the ES complex and decreases Vmax but increases KM.

A

Uncompetitive inhibition

22
Q

_______________ bind in the presence or absence of a substrate. Effective regardless of substrate concentration.

A

Mixed inhibition.

23
Q

On a Lineweaver-Burke plot, the intercepts can be used to obtain which information about the reaction?

A

Km and Vmax.

24
Q

In induced fit models, the enzymes bind substrates that favor the _______________.

A

Transition state.

25
Q

In _______________ catalysis amino acid side chains donate or accept protons.

A

General acid-base.

26
Q

In_____________ catalysis the active site metal can act as a redox active center.

A

Metal ion.

27
Q

In________________ catalysis nucleophilic or electrophilic attack on an atom results in a covalent intermediate.

A

Covalent

28
Q

______________ is an enzyme example of acid-base catalysis that is a natural antibiotic and the active site contains two negatively charged residues.

A

Lysozyme.

29
Q

___________ is an example of metal ion catalysis.

A

Anhydrase.

30
Q

____________ are enzymes that degrade proteins. Are important in protein maturation, blood clotting, and protein trafficking.

A

Proteases.

31
Q

_____________ is an example of covalent catalysis and cleaves dietary protein on the C-terminus of Try,Phe, and Trp.

A

Chymotrypsin.

32
Q

Cymotrypsin is a _____________ protease.

A

Serine.

33
Q

The inactive for of chymotrypsin is called_____________

A

Chymotrypsinogen

34
Q

What are the categories of proteases named after?

A

The catalyst responsible for generating the nucleophile