ENZYMES: Inhibition and Regulation Flashcards

1
Q

A type of inhibitor that binds directly only to free E (enzyme); reducing enzyme concentration available for substrate binding.

A

Competitive Inhibitor

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2
Q

A type of inhibitor that interacts with either an enzyme of an enzyme-substrate complex, that cannot be reversed by increasing substrate concentration.

A

Non-competitive Inhibitor

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3
Q

This type of inhibitor is similar to Non-competitive Inhibitor, which its binding affects the binding of the substrate.

A

Mixed Non-competitive Inhibitor

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4
Q

This type of inhibitor binds directly to the enzyme-substrate complex; distorts the active site, affecting catalytic function but not its substrate binding. It is significant only in multi-substrate enzymes.

A

Uncompetitive Inhibitors

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5
Q

This type of inhibitor binds directly to the enzyme-substrate complex; distorts the active site, affecting catalytic function but not its substrate binding. It is significant only in multi-substrate enzymes.

A

Uncompetitive Inhibitors

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6
Q

An end product inhibits key enzymes which forms the intermediates.

A

Feedback Inhibition

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7
Q

An enzyme which initiates the reaction for the synthesis of cytidine triphosphate (CTP).

A

Aspartate transcarbamoylase (ATCase)

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8
Q

What inhibits ATCase?

A

Cytidine triphosphate (CTP)

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9
Q

A process in which allosteric regulators bind to regulatory sites to regulate catalytic activity.

A

Allosteric Regulation

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10
Q

Conformational transitions that affect substrate binding.

A

Taut (T) Conformation and Relaxed (R) Conformation.

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11
Q

The relationship of T and R conformations to affinity

A

T confirmation means lower affinity; R conformation means higher affinity.

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12
Q

In the absence of a substrate, what exists?

A

An equilibrium between T and R conformation

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13
Q

Inhibitors that favor T conformation

A

Allosteric inhibitors

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14
Q

This favors to R conformation

A

Activators

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15
Q

Sequential activation of the sub-units upon binding of a substrate to one of the catalytic sites of a multi-domain enzyme.

A

Sequential Model

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16
Q

Introduction of a group to the enzyme either activate or deactivate the enzyme.

A

Covalent Modification

17
Q

Processes involved in Covalent Modification

A

Phosphorylation and Methylation

18
Q

The inactive precursor of enzymes

19
Q

Components of Zymogen

A

Pepsinogen, Trypsinogen, and Chymotrypsinogen

20
Q

Glucose transporters

21
Q

GLUT1

A

Erythrocyte

22
Q

GLUT2

23
Q

GLUT3

24
Q

GLUT4

25
The process where substrate binds to repressor allowing polymerase to transcribe mRNA
Genetic Induction
26
Similar structure but has a lower energy requirement when compared to a substrate.
Transition State Analog
27
DANA
2 - deoxy - 2,3 - dehydro-N-acetylneuraminic acid
28
It is essential for viral glycoprotein or gkycosaminoglycan synthesis and is a substrate for neuraminidase.
DANA