Untitled Flashcards

1
Q

How is de novo purine biosynthesis distinguished from de novo pyrimidine biosynthesis?

A

By inhibition by azaserine (a glutamine analog).

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2
Q

Roles of the reductase and nitrogenase in regard to nitrogen fixation.

A

Reductase: provides electrons with high reducing power
Nitrogenase: Vanadium cofactor
High reducing power needed to break triple bond.

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3
Q

What are the three ways to make glutamate?

A

Branch chain amino acid transaminase
Glutamate synthase
Glutamate dehydrogenase (not common)

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4
Q

What is meant when we say that an amino acid is conditionally essential?

A

They are usually only essential during illness, stress, or other physiological condition that could perturb normal biosynthetic processes.

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5
Q

From an evolutionary perspective, what is the major reason why we do not synthesize our essential amino acids?

A

Evolution has allowed for enzyme consideration. Since 8-10 enzymes are usually involved in amino acid synthesis, the balance of obtaining essential amino acids from diet conserves energy that would otherwise be used to make them.

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6
Q

Identify the major difference between aminotransferases and amidotransferases in regard to nonessential amino acid synthesis.

A

Amino: The enzyme that catalyzes the transfer of an amino group to a molecule.

Amido: The enzyme catalyzes transfer of amino group that replaces a carbonyl group on a molecule.

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7
Q

What is the major precursor for proline synthesis in the liver?

A

Liver can synthesize all nonessential amino acids, but proline must be synthesized a different route via arginine because the lack of a certain enzyme.

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8
Q

Identify the role of the intestine and kidneys in arginine synthesis.

A

Arginine contains guanadino group, NH4+ needed. If glutamine and glutamate are ultimate precursors for amino acid synthesis, the nitrogen must be obtained via pathways of glutamine and glutamate synthesis.

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9
Q

What role does S-adenosyl methionine play in polyamine synthesis?

A

S-AM: The sulfur serves as a good facilitator of ammonia transfer while also carrying the methyl group from products.

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10
Q

List three of the amino acid families identifies in class other than the “other amino acids” family.

A

TCA cycle: Oxaloacetate, a-ketoglutarate
Glycolysis: Pyruvate, PEP, 3-phosphoglycerate
PPP: Ribose-5P

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11
Q

What makes an essential amino acid essential?

A

Our metabolic ability to produce it’s a-ketoacid.

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12
Q

List three functions of nucleotides aside from genetics.

A

Glycogen, energy, coenzymes, regulation, group transfers (S-AM)

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13
Q

What two amino acids play a role in making purines and pyrimidines?

A

Aspartate & glutamine

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14
Q

Describe the mechanism involved in replacing a carbonyl group with an amino group.

A

Tautomerization then nitrogen attacks intermediate followed by removal of Pi.

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15
Q

Describe 3 methods of regulating purine synthesis in mammals.

A

Feedback inhibition
PRPP synthesis
Ribose-5P synthesis
IMP–> AMP or GMP

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16
Q

What nucleotide that we discussed could not be made if we were deficient in tetrahydrofolate?

A

Thymine. THF is the preferred methyl carrier and is made from folic acid. Used in both purine and pyrimidine synthesis.

17
Q

Describe substrate channeling with regard to PRPP and purine/pyrimidine synthesis.

A

PRPP synthesis allows for subsequent synthesis of other things such as histidine and pyrimidines and also resulting in a cumulative effect on regulation.

18
Q

What amino acids can undergo direct deamination and why can these types of amino acids do this?

A

Serine & threonine because of OH groups

19
Q

What are the two sources of nitrogen in the urea compound?

A

Aspartate and ammonium ion from glutamate or glutamine.

20
Q

What effect does dietary nitrogen have on the enzymes in the urea cycle?

A

The more dietary nitrogen present, the higher the production of urea.

21
Q

Diagram (explain) the glucose-alanine cycle.

A

Muscle: Glucose —–> Pyruvate—>alanine–…
Liver: …—>alanine —-> Pyruvate (also urea out) —> glucose —> (back to muscle)

22
Q

What role does pyridoxal phosphate play in amino acid metabolism?

A

Aminotransferases & helping to generate other amino acids.

PLP is a prosthetic group of aminotransferases and is an intermediate carrier of amino groups at the active site of aminotransferases.