Topic 10: Amino Acid Catabolism Flashcards

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1
Q

What are the branched chain amino acids (BCAAs)?

A

Leucine (L), Isoleucine (I), Valine (V)

They are also hydrophobic with alliphatic side chains

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2
Q

What are the hydrophobic alliphatic side chain AAs?

A

Ala, Pro, Leu, Ile, Val, Met, Cys

APVLIMC

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3
Q

What are the hydrophobic aromatic side chain AAs?

A

Phe, Tyr, Trp

FYW

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4
Q

What are the hydrophilic uncharged side chain AAs?

They have OXYGEN (O or OH) in their side chains.

A

Ser, Thr, Asn, Gln

STNQ

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5
Q

What are the hydrophilic charged, BASIC side chain AAs?

Basic have long side chains with NITROGEN, normally have an accepted extra H+

A

His, Arg, Lys

HRK

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6
Q

What are the hydrophilic charged, ACIDIC side chain AAs?

Acidic have short side chains with a CARBOXY (COO-), normally missing an H+

A

Glu, Asp

DE

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7
Q

What is the simplest, uncharged, neither hydrophobic nor hydrophilic AA?

A

Gly

G

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8
Q

What other molecule is alanine very similar to?

A

PYRUVATE - pyruvate is alanine with an amino group

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9
Q

What are the two SULFUR containing AAs?

A

Cysteine and Methionine

So if you SEE SULFUR it is Cys or Met!!!

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10
Q

How could you recognize the aromatic AAs?

A

Phe is alanine with a phenyl group (aromatic ring)

Tyr is Phe with an added OH

Trp is the other one… has DOUBLE RING STRUCTURE

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11
Q

What AAs are in over-represented in muscle?

A

BCAAs – when muscle begins to break down in the body you will see elevated levels of these AAs

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12
Q

Where does primary AA digestion take place?

A

Small intestine: duodenum and jejunum

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13
Q

What type of enzymes are trypsin and chymotrypsin? (endo or exo)

A

ENDONUCLEASES

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14
Q

How are AAs absorbed into the enterocytes?

A

Na+ symport. They rely heavily on the sodium gradient. Even in times of low [AA] the high Na+ gradient will drive absorption from the lumen.

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15
Q

How does the Na+/K+ pump work?

A

3 Na+ OUT

2 K+ IN

uses ATP

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16
Q

How are AAs stored?

A

THEY ARE NOT STORED. If AAs are not needed they are broken down. Protein and Peptides are not storage molecules for AAs.

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17
Q

How is glutamate converted into its ketoacid? This reaction is reversible, what happens in reverse?

A

Glu via Glutamate-DH has amino group removed and water added to become alpha-KG

NADH is generated, H2O used, amino group generated

Reverse:
NADPH is used and NADP+ is generated, H2O generated, amino group put back on

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18
Q

What’s another name for Alanine Transferase (ALT)?

A

Serum Glutamate Pyruvate Transferase (SGPT)

19
Q

How does Alanine become Pyruvate?

A

Ala amino group removed by ALT, replaced with O and amino is given to a-KG. Ala becomes pyruvate and a-KG becomes Glu.

20
Q

What is another name for Aspartate Aminotransferase (AST)?

A

Serum Glutamate Oxaloacetate Transaminase (SGOT)

21
Q

How does Asp become OAA?

A

Asp amino group removed by AST, replaced with O and amino is given to a-KG. Asp becomes OAA and a-KG becomes Glu.

22
Q

How does Asp become Asn?

A

ATP generates Pyrophosphate (PPi) to drive reaction. Amino group is taken from Gln and added to Asp, H2O is removed, yields Asparagine. Glu is generated.

23
Q

What vitamin do AA transferases require?

A

Vitamin B6/Pyridoxine – Pyridoxyl Phosphate

24
Q

How do AA Oxidases directly remove amino groups?

A

FMN reduces AA to make FMNH2. (Requires B2/Riboflavin)
This generates H2O2.
AA Oxidase rips off the remaining NH2 to generate free ammonia.

25
Q

How can you get ammonia to the liver from muscle?

A

One way is put it on Glutamate (Glu) to make Glutamine –> go to liver –> recover Glu and give NH3 to UREA CYCLE

26
Q

What are the KETOGENIC ONLY AAs?

A

Leucine (Leu/L) and Lysine (Lys/K)

27
Q

What are the ketogenic AND gluconeogenic AAs?

A

Isoleucine, Phenylalanine, Tryptophan, Tyrosine

Ile, Phe, Trp, Tyr

I,F,W,Y

28
Q

What vitamin(s) is(are) needed to turn proprionate into succinyl-CoA?

A

Biotin/B7 and B12/Cobalamin

29
Q

What AA can make Acetyl CoA?

A

Leucine, Isoleucine and Tryptophan

30
Q

What AA can make Acetoacetyl CoA?

A

Leucine, Lysine, Phenylalanine, Tryptophan, Tyrosine

31
Q

What causes the Maple Syrup Urine Disease?

A

a defect in catabolism of the BCAAs, the second enzyme: alpha-KetoAcidDeHydrogenases

problem comes from the buildup of all 3 BCAAs a-KA’s but smell comes from ISOLEUCINE’s a-KA

32
Q

What causes the smell from MSUD?

A

ISOLEUCINE’s alpha-ketoacid, alpha-keto-beta-mehtylglutarate

33
Q

What are signs/symptoms of ketoacidosis?

A

Neuro Signs:

poor appetite, lethargy, irritability, mental retardation, physical disabilities, seizures, vomiting, coma, death

34
Q

How does MSUD/ketoacidosis affect neonate cattle?

A

Show signs within 24 Hours!! Death within 5 days

35
Q

What AA breakdown product causes the SWEATY FOOT smell?

A

Leucine’s breakdown product: isovaleryl CoA

36
Q

What AA breakdown product causes the CAT URINE smell? (this can make any animals urine smell like tomcat stank!)

A

Leucine’s breakdown product: beta-methylcrotonyl CoA

37
Q

What enzyme causes the blackening of bananas and potatoes?

A

TYROSINASE

Tyrosine is converted to melanin by tyrosinase.

38
Q

What cofactor does TYROSINASE require to function properly? Why do we care?

A

COPPER

We care because some soils are deficient in copper and animals can become deficient in this essential cofactor.

39
Q

What would you expect to see in a copper deficient animal?

A

some Loss of Hair Pigment, especially around the eyes. (spectacles!!)

Also: iron deficiency anemia, CT problems, Immune system problems, muscle loss, weakness, low protein, mood disorders, liver damage, hypothyroid, low body temp, and low NTs Epi, NorE, and Dopamine

40
Q

Why is Tyrosine conditionally essential?

A

Tyrosine is derived from Phenylalanine! If you can’t get Phe then you can’t make Tyr!!

Some animals have a deficiency in the enzyme Phenylalanine Hydroxylase (PAH) (puts the OH on Phe to make Tyr) and require Tyr as essential in their diet.

41
Q

What happens to animals deficient in PAH?

A

PKU!

Phe is converted to Phenylpyruvic acid (a phenylKETOACID) ==> PHENYLKETONURIA

Phenylpyruvate is then converted to Phenylacetate which can give urine and sweat a MOUSY smell

42
Q

Why do PKU patients lack pigment?

A

PKU can’t make Tyrosine which is the foundation for Melanin.

43
Q

How does Gln become Glu? This is a reversible reaction, how does it occur in reverse?

A

Glutaminase removes an amino group from Gln and adds H2O to make Glu.

Glutamine synthetase adds an amino group to Glu to make Gln. Uses ATP and generates water