Week 13 Flashcards

(46 cards)

1
Q

_______________ are an inactive form of enzymes also known as proenzymes and are how organisms protect themselves from their own digestive enzymes.

A

Zymogens

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

_____________ are proteases that cleave peptide (amide) linkages between amino acids.

A

Pancreatic enzymes.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

________________ are enzymes that cleave peptides into smaller individual amino acids or small peptides (di- or tripeptides).

A

Peptidases

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

The enzyme pepsin is an ______________ protease.

A

Aspartyl.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

The enzymes trypsin and chymotrypsin are _______________ proteases.

A

Serine.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Why would the active sites of trypsin and pepsin not function well in each other’s normal environment?

A

Trypsin is a serine protease- requires a neutral to basic environment to deprotonate serine.

Pepsin is an aspartyl protease- requires an acidic environment to readily protonate/deprotonate aspartate.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

________________ is the process in which ammonia can be removed from an amino acid.

A

Transamination.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

In transamination the _________________ is transferred to an α-keto acid (often pyruvate or α-ketoglutarate).

A

Amine.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

__________________ is the enzyme that transaminates pyruvate to the amino acid alanine.

A

Alanine Transaminase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Alanine then travels from the muscle to the liver, where it can be transaminated to ________________ from __________________.

A

Glutamate, α-ketoglutarate.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

__________________ is the process in which an amine is released as ammonia. Yields an α-keto acid and NADH/H+ is generated.

A

Oxidative Deamination

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

_________________ is commonly used and interconverted to α-ketoglutarate.

A

Glutamate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Free ______________ may be converted to waste products (in many organisms including mammals, urea).

A

Ammonia.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

_________________ is the enzyme used to oxidatively deaminate glutamate and regenerate α-ketoglutarate.

A

Glutamate Dehydrogenase.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

________________ is the metabolic process through which nitrogenous wastes generated in muscle are transferred to pyruvate, generating alanine; the alanine in turn is transported to the liver, where it is deaminated and the pyruvate presumably used in gluconeogenesis.

A

Glucose–Alanine Shuttle

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

________________ ATP-dependent enzyme responsible for the synthesis of glutamine from glutamate and ammonium ion in the liver.

A

Glutamine Synthetase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

_________________ is the main enzyme that deaminates glutamine and yields glutamate and free ammonia.

A

Glutaminase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Amines are added to pyruvate in the ______ and removed from the resulting alanine in the ______.
A. liver; kidney
B. muscle; kidney
C. kidney; liver
D. muscle; liver

A

D. muscle; liver

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

In the urea cycle, Ornithine and Carbomyl phosphate undergo a condensation to give rise to _________________ and the enzyme responsible for this is _________________.

A

Citrulline. Ornthine transcarbamoylase.

20
Q

In the urea cycle, cirtrulline is converted to ______________ by the enzyme _________________.

A

Argininosuccinate. Argininosuccinate synthase

21
Q

In the urea cycle, _______________________is split off from argininosuccinate to yield _________________. The enzyme responsible for this step is __________________.

A

Fumarate, Arginine. Argininosuccinate lyase.

22
Q

In the urea cycle, _______________ is cleaved off from arginine to generate _________________ by the enzyme________________.

A

Urea, Ornithine. Arginase.

23
Q

The function of the urea cycle is to detoxify and dispose of _______________.

24
Q

________________ is the compound created from ammonia in order to reduce ammonia levels in the blood and lower the risk for toxicity.

A

Carbamoyl Phosphate

25
________________ is the enzyme involved in the production of carbamoyl phosphate for the urea cycle.
Carbamoyl phosphate synthetase I (CPS-1).
26
_______________ is the enzyme responsible for the production of building blocks for pyrimidine biosynthesis.
Carbamoyl phosphate synthetase II (CPS-2).
27
_________________ are organisms that typically eliminate wastes as ammonia secreted through the skin.
Ammonotelic
28
______________ are organisms that synthesize uric acid and eliminate it in their waste, which is technically not urine.
Uricotelic
29
Which amino acid is directly generated in the urea cycle?
Arginine
30
Amino acids can be broken down into two categories:
glucogenic and ketogenic.
31
_____________ are the amino acids that are broken down into products that undergo gluconeogenesis.
Glucogenic
32
______________ are the amino acids that metabolizes products into ketone bodies. Made from over abundance of Acetyl-CoA.
Ketogenic.
33
3 carbon skeleton amino acids are broken down into _______________.
Pyruvate.
34
Which amino acids are used in ketogenesis but not glucogenesis?
Leucine and lysine
35
________________ are molecules the body recognizes as foreign. Not molecules found in human metabolism and need to be eliminated. May be cleaved into smaller fragments.
Xenobiotics.
36
__________________ is the process by which the body detoxifies and eliminates foreign molecules.
Xenobiotic metabolism.
37
In _____________ of xenobiotic metabolism, Oxidation or cleavage occurs, xenobiotics become more hydrophilic and products are metabolically active.
Phase I
38
In _____________ of xenobiotic metabolism, conjugation to larger molecules such as glutathione or glucuronic acid.
Phase II
39
___________________ are broad family of enzymes that employ NADPH and molecular oxygen (O2) to oxidatively modify substrate molecules. Membrane-associated enzymes commonly found in either the inner mitochondrial membrane or the endoplasmic reticulum.
Cytochrome P450
40
_______________ are enzymes that deactivate neurotransmitters. Covalently fix FAD+ to catalyze the conversion of a primary amine to an aldehyde.
Monoamine Oxidases.
41
_______________ oxidized form of glucose in which C-6 is oxidized to a carboxylic acid.
Glucuronic acid.
42
_________________ tripeptide of glycine, cysteine, and glutamate. Conjugated to xenobiotic via glutathione-S-transferase.
Glutathione (GSH).
43
___________________ is a network of highly porous capillaries that act as filters. Large objects are retained in the capillaries, and small molecules are filtered out.
Glomerulus
44
_________________ is a peptide hormone that acts via a seven-transmembrane helix spanning receptor to elevate cytosolic levels of cAMP.
Antidiuretic Hormone.
45
Pyrimidine is synthesized from amino acids ______________ and ________________.
Glutamate and Aspartate.
46
Presence of carbamoyl phosphate synthetase in the mitochondria means we go through __________________ and presence in the cytoplasm means we go through ____________________.
Urea cycle. Pyrimidine bio-synthesis.