Final: Co-factors, Mnemonics, etc. (Ben) Flashcards

1
Q

What prosthetic grp do aminotransferases use?

A

PLP

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2
Q

What is the co-factor for Glu Dehydrogenase?

A

NAD+ or NADPH

  • NAD+ in the Glu dehydrogenation direction
  • NADPH when re-aminating alpha-KG to Glu
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3
Q

What is the coenyzme for serine and threonine dehydratases?

A

PLP

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4
Q

What does glutamine synthetase require for formation of Gln from Glu?

A

ammonia and ATP

(giving ADP + Pi)

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5
Q

What is the co-factor for dihydrofolate reductase?

A

2 NADPH

2 reductions … folate to H2F to H4F

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6
Q

What is the cofactor for Methylene-H4F Reductase?

A

NADH

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7
Q

What is the prosthetic group for Homocysteine Methyltransferase?

A

Methyl-B12

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8
Q

What is the co-factor for Met adenosyl transferase?

How is it used differently here than in most reactions?

A

ATP

Here, all 3 Ps are broken off to get the adenosine for transfer to Met.

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9
Q

What is the co-factor for cystathionine synthase?

A

PLP

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10
Q

What are the cofactors for the enzymes which convert Met/Thr/Val/Ile from their alpha-ketoacid intermediates into succinyl-CoA?

(3 enzymes)

A
  1. BC-alpha-KA DH = TPP, lipoic acid, FAD, NAD, CoA
  2. propionyl-CoA carboxlase = biotin
  3. methylmalonyl-CoA mutase = 5-adenosyl cobalamine (B12)
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11
Q

What co-factor do both Serine and Threonine Dehydratases use?

A

PLP

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12
Q

What are the co-factors for serine hydroxymethyltransferase?

A

PLP

and

H4F ( becomes methylene-H4F )

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13
Q

Co-factor for Glu Decarboxylase?

A

PLP

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14
Q

What is the cofactor for Phe OHase?

And how is it formed?

A

H4F-Biopterin

  • H4F-Biopterin Reductase
    • uses NADPH to reduce H2F-Biopterin
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15
Q

What co enzyme is used by dihydro-orotate dehydrogenase?

A

NAD+

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16
Q

What co-factor do tyrosine hydroxylase and tryptophan hydroxylase use?

A

H4-Biopterin

17
Q

What co-factor does Dopamine B-Hydroxylase use?

A

ascorbic acid

(vitamin C)

18
Q

What is the cofactor for COMT?

(bonus… what does the enzyme make?)

A

SAM

  • methylates an NE metabolism intermediate to form MHPG the urinary indicator of CNS NE function
19
Q

In the extrinsic pathway of thrombin activation…

What is the “cofactor” for factor VII?

What is the “cofactor” for factor X?

And what complexes do these form with their cofactors?

A
  • VII plus TF is extrinsic tenase complex
  • X plus V is prothrombinase complex
20
Q

Which special domain do some clotting factors contain which enhances membrane binding?

Which factors have it?

What else has it?

A

Gla domain

  • II, VII, IX and X have it

(2, 7, 9, 10)

  • protein C and protein S also have it
21
Q

What co factor does vitamin k oxidoreductase use?

A

NADPH

(NOT vitamin K! that is used by gamma carboxylase… VKOR uses NADPH to reduce vit K from VKO to VKH2 form)

22
Q

What are the 3 most common bleeding disorders and their causes?

Why aren’t these fatal?

A
  1. Hemophilia A - factor VIII deficiency
  2. Hemophilia B - factor IX defic.
  3. Hemophilia C - factor XI defic.

(so 8, 9, 11 in that order)

Not fatal because they just play a part in positive feedback loops of the extrinsic pathway but aren’t essential to its function.

23
Q

What are the non-essential AAs?

Semi-essential?

A

A A A C G G G Pro S T

  • Alanine, Aspartate, Asparagine
  • Cysteine
  • Glutamine, Glutamate, Glycine
  • Proline
  • Serine
  • Tyrosine
  • Semi-essential: Arginine
24
Q

Which AAs can not be transaminated?

A

Lys, Thr, Pro and HydroxyPro

25
Q

Which AAs can form succinyl-CoA?

What must they first become to enter the succinyl-CoA forming pathway?

(And how do they get there?)

A

Met, Thr, Val, Ile

(Met Three Valiant Islanders)

  • all first become α-ketoacids
  • Met –(SAM cycle)–> HCys –(Cysta. Synthase)–> α-ketobutyrate
  • Thr –(Thr Dehydratase)–> α-ketobutyrate
  • Val, Ile –> α-ketoacids
26
Q

Which AAs form oxaloacetate?

How?

A

Asp and Asn

  • Asn + H2O –(asparaginase)–> Asp + NH4+
  • —(ASAT)—> Oxaloacetate
  • remember ASAT uses PLP
27
Q

Which AAs form pyruvate?

Two of them do so in one reaction… which?

A

Ala, Ser, Gly, Cys

Al + Sarah Glide (into the) Cysteine (chapel)

  • Alanine becomes pyruvate directly via ALAT
    • remember ALAT uses PLP
  • Serine Dehydratase
    • Serine —> Pyruvate + NH4+
    • also uses PLP, water is removed but then re-used
28
Q

Which AAs form alpha-ketoglutarate?

Generally, how?

A

Glu/Gln, Pro, Arg, His

(Gluttonous Professionals Are History)

  • all are first converted to glutamate which can be transaminated to alpha-KG
  • ( structure-wise … notice that it is Glu with a =O replacing the amine )