Lecture 10 Flashcards

(39 cards)

1
Q

What enzyme catalyzes the transfer of a C-, N-, or P- containing groups

A

Transferases

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2
Q

What enzyme catalyzes the cleavage of bonds by addition to water

A

Hydrolases

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3
Q

What enzyme catalyzes the cleavage of a C-C, C-S, and certain C-N (without water)

A

Lyases

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4
Q

What enzyme catalyzes racemization of optical/ geometric isomers?

A

Isomerases

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5
Q

What enzyme catalyzes the formation of bonds between carbon and an N,O,S,C coupled to hydrolysis of high-energy phosphates

A

Ligase

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6
Q

_______ is a small molecule required for the
catalytic activity of an enzyme.

A

Cofactor

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7
Q

________ (inorganic) include Cu2+, Fe3+ or Zn2+

A

Metal ions

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8
Q

When the cofactor is an organic molecule, then
it is a ________. E.g.: vitamins

A

Coenzyme

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9
Q

When the coenzyme is only transiently
associated, then it is a_________

A

cosubstrate

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10
Q

When the coenzyme is permanently associated with the protein, either through covalent or non-covalent interactions, then it is a __________

A

Prosthetic group

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11
Q

_________ is the catalytically active enzyme-cofactor complex.

A

Holoenzyme

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12
Q

________ is the inactive protein lacking the cofactor.

A

Apoenzyme

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13
Q

_________ is a small molecule that binds to a larger one

A

Ligand

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14
Q

_________ is the molecule undergoing the reaction. It is the specific molecule(s) that is bound by the enzyme at its active site.

A

Substrate

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15
Q

___________ is the region of the enzyme that binds the substrate(s) and where the ________ takes place.

A

Active site, catalytic reaction

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16
Q

In our cells, groups of enzymes work
together in specific metabolic pathways
consisting of several steps. They are called
___________

A

Multi-enzyme pathways.

17
Q

Multi-enzyme pathways can be _______ or
_____________, and they are all __________.
Since some metabolites are shared among
pathways, the fate of a certain metabolite
affects the other pathways.

A

Linear, branched, interconnected

18
Q

The slowest step in the pathway
is the _____________.

A

Rate-limiting step

19
Q

______________ catalyze the slowest, irreversible step

A

Rate-limiting enzymes

20
Q

Rate-limiting steps are targets of _________
and targets of ________ by drugs

A

Regulation, intervention

21
Q

Organelles preventing a _______ in enzyme pathways with common products, separating by space

22
Q

Seperation in time: Glucose breakdown (glycolysis)
and synthesis (gluconeogenesis) share
enzymes in the same compartment,
but have different ________

A

Rate-limiting steps

23
Q

The concentration of many regulatory enzymes
is controlled by ______ and _____

A

Inducers and inhibitors

24
Q

Enzyme synthesis is a

A

Very slow process

25
Compartmentalization is an important but ________ of regulation
Passive means
26
Product inhibition; Products display ______ to the substrate, and cannot be competed off by the substrate.
Structural similarity
27
Product inhibition- Products can bind _______ to the active site. The response of the enzyme is _______.
Reversibly, immediate
28
Facts about allosteric regulators
They have quaternary structure, effector binds at a regulatory site (not active site), they bind reversibly, no need for structural similarity, show sigmoidal curve
29
Allosteric regulation of enzymes: Classification is based on
Chemical nature of the effector
30
Allosteric regulation of enzymes; __________ = true substrate. __________ = different chemical nature from true substrate.
Homotropic, heterotropic
31
Allosteric activators (positive effectors) have what effect on enzyme activity, enzyme state, enzyme activity curve
Increase activity, stabilize R-state, shift left
32
Allosteric inhibitors (negative effectors) have what effect on enzyme activity, enzyme state, enzyme activity curve
Decrease activity, stabilize T-state, shift right
33
_______________: upstream substrate of a multi-enzyme pathway activates a downstream enzyme.
Feedforward activation
34
Disease of the day: Pulmonary emphysema may be produced by ______________. As A1A is defective, that leads to increased __________ activity.
alpha1-antitrypsin deficiency (A1AD), neutrophil elastase
35
What are major risk factors for a1-Antitrypsin deficiency, and where does it effect
Smoking, lungs and liver
36
Covalent regulation refers to the ________ of specific chemical groups via _______ bonding. They have an ________ effect, either reversible or irreversible. They may _________ enzymatic activity, depending on the enzyme considered.
Addition or removal, covalent, immediate, increase or decrease
37
Many enzymes are produced in an inactive precursor form called ________
Proenzyme or zymogen
38
Proteolytic cleavage results in an _________ conformational change that exposes the active site
Irreversible
39