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SFM Final > Biochem Review > Flashcards

Biochem Review Flashcards

1
Q

Isoprenoids
Made from what?
Can be formed into what?
Components of what?

A
  • acetyl coA
  • steroids (cholesterol), vitamins, and coenzyme Q
  • Membranes and bile
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2
Q

What does bile contain and what can form if the levels are thrown off?

A

Cholesterol and salts

  • can cause gallstones, malabsorption (steatorrhea) and fat-sol vitamin def
  • helped w/ oral chenodeoxycholic acid
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3
Q

What are the essential AAs?

A

Pvt Tim Hall

Phenylalanine, Valine, Threonine, Tryptophan, isoleucine, methionine, Histidine, Leucine, Lysine

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4
Q

Hair has what that can be manipulated by curling and heating?

A

Keratin w/ high cysteine disulfide bonding

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5
Q

What type of reaction is delta G when neg or pos?

What is Gibbs FE equation

A

RTln(Keq)—prod/reactants
- exergonic, spontaneous, E producing
+ endergonice, non-spon, E consumed

The ability to do work

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6
Q

What is the bicarbonate buffer system equation (pH, etc)

A

bicarb+ H – H2CO3 – CO2 + Water

Acidosis= left shift = +acid (ketone bodiess, lactate) or -biocarb (diarrhea, weak kidneys)

Alkalosis= right shift= +strong base (antacid) or -acid (vomit) or Hyperventilate

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7
Q

Oxidation vs Reduction

A

Ox- lose Electrons (gain H)

Red- gain E (lose H)

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8
Q

Cofactor vs Coenzyme

A

-metal ions

(type of cofactor)- vitamin derivative

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9
Q

Cosubstrate vs prosthetic

A

temporary (NAD+)

-permanent association (FAD or heme)

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10
Q

The alpha keto-DH complex involves what vitamine derivatives?

A

Lipoic acid, B3 (niacin), B5 (panth), B1 (thy)

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11
Q

What affects enzyme activity? factors

A

Temp: doubles every 10 deg C (untill denatured)

pH: between 4-8 (pepsin in gastric)

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12
Q

Hydrogen/ K+ ATPase
Where found?
What direction does it pump
What are inhibitors prescribed for?

A

Parietal cells lining gastric lumen

  • H+ into the lumen…lowers pH (acidic) combines with Cl to form HCl- can cause hypochlorhydia– reduces reabsorption of nutrients
  • Omeprazole, etc to increase pH in Heartburn, indigestion, etc
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13
Q

Competitive Inhibition
Noncompeitive
Uncompetitve

A

C: compete with sub site… need more sub to overcome (increased Km)

N: binds to E and ES complex…. decreased Vmax

U: Binds to ES complex only… Decreased Vmax and Km by same factor

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14
Q

What does lead poisoning cause (symp) and what is used to treat?

A

Chelating agents

abdom pain, sideroblastic anemia, irribility, headaches, impaired NS

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15
Q

What is sideroblastic anemia?

A

Inability of bone marrow to produce normal rbcs

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16
Q

What are isozymes?

A

Enzymes with the same catalytic function, but different primary sequence (different biological properties)

(Troponin cTn, CK-MB, LDH1) all MI markers

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17
Q 
What enzymes are found in blood for these diseases?
Bone
Obstructive liver
Prostatic cancer
Acute pancreatitis
Muscular dystrophy
Liver disorder
A

Alkaline phosphatase
-Sorbitol DH or Lactate DH LDH1

  • Acid phosphatase
  • Amylase
  • Aldolase and ASH
  • CK-MM
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18
Q

Amphipathic means?

A

Both hydrophobic and hydrophilic

phospholipid bilayer

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19
Q

Whats the difference btw these phospholipids?
Glyceropholspholipids
Sphingolipids SL

A

G: glycerol backbone + phos and 2 fattys esterfied to bb

SL: sphingosine backbone + phosphorylcholine and long chain fatty
sphingolipids, has a long alkyl group connected at C1 and a free amine at C2, as a backbone.

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20
Q

What is a glycolipid?

A

found on membrane (outer leaf)

Sphingosine backbone w/ oligosacc residues and fatty acid attached

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21
Q

Membrane proteins:
Integral
Peripheral
Lipid Anchored

A

embedded and stabilized with hydrophobic intereactions

loosely bound w/ electrostatic interaction

tethered via covalent bonds to lipids

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22
Q

Carb shell of membrane that provides protection, cell adhesion, and cell identification?

A

Glycocalyx

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23
Q

What is the melting temp Tm of a membrane?

A

Temp where it switchese from fluid to rigid

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24
Q

What kinds of molecules utilize facilitated diffusion? (passive)

A

large and uncharged

  • need a facilitator (proteins)
  • ion channels or transporters (voltage gated Na… or GLUT1)
  • greatly increase transport rate
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25
Q

What are common ligands for ligand gated- ion channels?

Whats an example? and What are two inhibitors used to treat?

A

-neurotransmitters or hormones

-Glutamate receptor
The antagonists of GR (Mimantine/Namenda) used to treat Alzheimers

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26
Q

What does Tetradotoxin do and where can it be found in wild?

A

-binds to Na+ channel and inhibits neurotransmission

Puffer fish

Same function as topical anesthetics

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27
Q

P type ATPase
vs
ABC transporter

A

both active transport

ATPase: Primary: use ATP hydrolysis to drive

  • covalent bond with phosphate
  • occurs on conserved Asp residue
  • conformational changes occur (Na/K ATPase, Ca-ATPase

ABC: smaller molecules, use ATP hydro, but protein is not phosphorylated
-pathogens can upregulate, leading to drugs being pumped out too quickly to have effect

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28
Q

Examples of secondary transporters:

coupled to primary

A

Na/Ca exchanger: NCX: antiporter.. A in– B out

Lactose permease: Symporter: A and B in

Mito Ca transporter: Uniporter: A in – A out

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29
Q

What does the Sodium-Glucose transporter SGLT1 do? where does it happen?

What drugs relate to it?

A

Happens in the small intestine and renal tubules

  • unidirectional movement of Na+ and Glu
  • Na occurs down its gradient and provides E to move Glu up its gradient (secondary transporter)
  • Na+ gradient reset by the Na/K-ATPase

Invokana and Farxiga
-Inhibitors= keep glucose in intrestines–> more released in urinations–> helps lower blood pressure and weight loss

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30
Q

Flowing in the NCX? which is an antiporter of course

A

facilitated by integral membrane proteins

3 Na down gradient in….. and 1 Ca against gradient out

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31
Q

Transporters involved with monosaccharide transport
Which side of enterocyte and what category of transporter?
SGLT1
GLUT2
GLUT5
Na/K ATPase

A

S: on apical side (lumen of small intestine)

  • Glu, Gal, Na+ all come in
  • secondary active

G2: on basolateral side (bloodstream)

  • Glu, Gal, Fru leave to blood
  • fd

G5: on apical side

  • Fru in
  • facilitated diff

Na/K: basolateral side (blood)

  • 3Na in to blood….2K out of blood–> enterocyte
  • primary active
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32
Q

BMI calculation

A

Weight/height^2

Kg/m2

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33
Q

Percentage of cals from protein, fats, and carbs?

A

10-15% protein
20-35% fats
rest carbs

and more omega 6 than 3 (5-10% and 1%)

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34
Q

Type O blood contains which Ag and what Abs?

A

H antigen

AntiA and B antibodies (found in the plasma)

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35
Q

Where are Ags and Abs found in blood?

A

on rbcs

in the blood plasma

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36
Q

What are the drugs Ouabain and Digoxin? What are they used for and what do they do?

A

Cardiac Glycosides (contraction inducing)

  • Inhibits the Na/K ATPase in cardiac myocytes–> increase in Na+
  • ->impairs NCX that’s coupled to ATPase—> increase in Ca2+ in the sarco reticulum
  • Inc contractile force
  • Used to treat congestive heart failure, atrial dibrillation, dysrhythmias…. they are very potent! Have been used to coat arrords and rat poisons

Digitoxigenin: slowly reduces the resting potential of neurons to 0

  • can lead to confusion, vision issues, delirium
  • jumpstarts the heart but affects the brain
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37
Q

During a sprint, what path is utilized for ATP to outpace O2 delivery?

A

Lactate path via glycolysis (which doesn’t need O2)

The resulting Pyr can be oxidized under Aerobic conditions to produce much more ATP

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38
Q

What is the only fuel of red blood cells and brain (non-starving?

A

Glucose

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39
Q

Where does Gluconeogenesis occur?

A

Liver

and some in kidney cortex

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40
Q 
Glucose Transporters
GLUT:
1
2
3
4
5
A

1: Ubiquitous (in many cells ie. brain, cornea, placenta, cancer cells) but high in rbcs especially
- High affinity

2: Main transporter in liver (and pancreas)
- low affinity

3: Main transporter in neurons
- high affinity

4: Present in skeletal muscle, heart, adipose tissue
- medium affinity
- Insulin dependent
- -sequestered in cell vesicles–> insulin signals fusion to membrane–>then increases glucose uptake (promoted by exercise)

5: On apical side of enterocyte (intestinal)
- Lets fructose in into enterocyte

Km is inverse to affinity

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41
Q

Where is Glucokinase present? and what promotes its translocation to and from the nucleus from the cytoplasm?

A

Liver and Pancreatic Beta cells

F6P to nuc….Glu increase from nuc–>cyto

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42
Q

Rate limiting enzyme of glycolysis?
Activated by what? Inhibited by what?
Coupled with what (bifunctional enzyme) in Gneogenesis?

A

PFK1
+ AMP, F2,6BP
- ATP, Citrate

F1,6-BPase (phosphatase)

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43
Q

What activates and inhibits Pyr Kinase?

A

+insulin, F1,6BP
stim dephosphorylation of PK (activated)

-Glucagon, Alanine, ATP
stim cAMP phosphorylation of PK (inhibited)

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44
Q

What other paths is G6P used in?

A 
PPP (Ribose and NADPH)
Galactose metabolism
Glycogen Synthesis
Glycolysis (Pyr)
Gluconeogenesis (Glu)
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45
Q

What are some precursors of Pyruvate?

What are some things made from pyruvate?

A 
Pre:
Glucose
Trp
Thr
Ala

Makes:
Acetyl CoA (Pyr DH complex)– Aerobic fed
Alanine (Ala Aminotransferase)–Anaerobic/Aerobic fed
Oxaloacetate (Pyr Carboxylase)–Aerobic fasting
Lactate (lac DH)– Anaerobic

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46
Q

What do defects in glycolytic enzymes generally cause?
What do they most impact?
What are some of the enzymes?

A
  • Hemolytic anemia
  • RBCs (lack mitochondria)
  • PG Isomerase, Triose P Isomerase, Aldolase A
  • —PKinase (95% of defects)
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47
Q

Where does Gluconeogenesis occur?

What are the major precursors?

A

Liver, kidney, small intestine

Lactate, amino acids, and glycerol

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48
Q

Where is Pyruvate Carboxylase PC found?
What does it form? and what step follows?
What is its cofactor?
What activates it?

A

The mitochondria

Oxaloacetate–> PEP Carboxykinase - PEP
Ox reduced to Malate (M DH) and transported through Malate Shuttle in between

Biotin B7

Acetyl CoA and Cortisol

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49
Q

What is the rate-limiting step of Gluconeogenesis?

A

F1,6 Bisphosphatase

Act by Cortisol and Citrate
- by AMP and F2,6-BP

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50
Q

Where is glucose -phosphatase located?

What are its components?

A

Endoplasmic Reticulum on liver, kidneys, SI, pancreas

GLUT7 + catalytic unit, and Pi antiporder

51
Q

What does the Cori cycle do?

A

Links the lactate in anaerobic glycolysis in rbc and muscle to Gneo in liver

Prevents lactate accumulation, regenerate glucose

Lac–>blood–>liver——>glu–>blood–>muscle–Pyr–> back to lac

52
Q

What are precursors of gluconeogenesis?

A 
Fructose--DHAP and G3P
Galactose
Glycogen
Glycerol
Propionate
Lactate--Pyr
Alanine--Pyr
AAs
53
Q

The Polyol Pathway turns Glucose to Fructose. What are the two enzymes used and what is the intermediate between G and F? Where does this occur in the body?

A

Aldose reductase–>Sorbitol–>Sorbitol DH–>Fruc

In Hepatocytes (liver), Ovaries, seminal vesicles (sperm

Accumulation can occur in kidneys, lens, retina, schwann cells

54
Q

When Fructose is metabolized, what two paths can it take? and What critical Glycolysis step can it bypass (making it a faster process)?

A
  1. can turn to F6P by Hexokinase
  2. can turn to DHAP or G3P by FKinase->F1P–>Aldolase B–product

Bypasses PFK1 RL*

55
Q

Why can excess Fructose consumption be bad?

A

Bc it bypasses PFK1, too much pyruvate can accumulate–> turning to TAGs and fatty liver/adipose… process happens in an unregulated fashion
High Fruc Corn Syrup

56
Q

What is the rate limiting enzyme in Galactose Metabolism and where does the end product insert into Glycolysis?

A

Glucose 1P Uridyltransferase GALT

G6P

Makes UDP-Galactose used to synthesize Lactose in mammary glands and Glycolipids/proteins

57
Q

What causes Galactosemia?

A

deficiency in GALT–accumulation of galactitol

def. in Galactokinase

58
Q

What does the Pentose Phos Path produce?
What are its byproducts?
What is the RL Step?

A

Ribulose 5-P…or continues onto non-ox step to make R5P and various glycolytic intermediates like G3P, F6P

Makes 2 NADPHs in the Ox irreversible step

G6P DH (the first step)

59
Q

What does a deficiency in G6P DH cause? in what population? and what does NADPH regenerate as an antioxidant?

A

hemolytic anemia (lack of NADPH)

African Americans

NADPH–>glutathione GSH…detoxifies H2O2

60
Q

What would cause high NADPH demand?

How about Ribose 5P?

A
  • increased biosynthesis, Lactating mammary, phagocytosis, lung and liver tissue (non-ox phase favored for products)
  • Cells rapidly dividing (ox phase favored in PPP)
61
Q

Where is glycogen stored?

A

Liver (blood glu regulation) and muscle (physical activity reservoir) as granules

62
Q

What is the RL enzyme of Glycogenesis and Glycogenolysis?

what cofactor is used in the breakdown?

A

Gly Sythase! (dephos form +) Glucosyl 4,6 Transferase for the branching part

Gly Phosphorylase! (phos form +) w/ vit B6 (pyridoxal phosphate) Debranching enzyme w/in 4 residues

63
Q

When is glycogen breakdown favored?

A

Low BG, high Glucagon (fasting- doesn’t act on muscle), high Ca+ levels during exercise (high AMP)

64
Q

An antigen that evokes a specific immune response-

A

Immunogen

65
Q

An Ag inducing an immunologic tolerance-

A

Tolerogen

66
Q

In the Pyruvate DH complex (pyr-ACoA), what coenzyme is used for the E1 complex? and is the complex active in the phos or dephos form?

A

Thiamine pyrophosphate
-Cleavage of thioester linkages

Dephosphorylated form is active

67
Q

In a pyruvate phosphatase def., (where pdc is always inactive-phosphorylated), glucose generally becomes what instead of ACoA?
What should be restricted in a patient’s diet?
Which diet is recommended?

A

Lactate

Alanine

Ketogenic diet

68
Q

What are precursors to Alpha-Ketoglutarate?

A

Glutamate—-

Gln, Arg, Pro, His GAPH

69
Q

What are precursors to Fumerate?

A

Phe, Tyr, Asp

DRP derppp

70
Q

Where does the TCA cycle, Fatty Acid Oxidation, and OxPhos take place?

A

Mitochondrial Matrix (mostly)
MM
Inner Mito membrane space

71
Q

What does PEP carboxykinase do in relation to diseases?

A

Promotes cancer cell proliferation… colorectal and breast cancers

72
Q

What does accumulation of Citrate cause (metabolic)?

A

Shifts toward glycolysis, pyruvate accum, so lactate (and NAD+) increase, which promotes cancer.
Lipid and sterol synthesis also activated (good for cancer)

73
Q

Mutations in what lead to 2-hydroxyglutarate 2HG issues and cancer? What part of TCA cycle does this come from?

A

IDH1 and 2

Conversion of Alpha Ketoglutarate

74
Q

What is in the urine due to a Fumerase deficiency?

A

Fumerate associated with succinate and lactate…eventual 2-oxoglutaric aciduria
Death w/in 2 years or life of speech delay

75
Q

What genes are associated with Succinyl-Coa synthetase def

A

SUCLA2 and SUCLG1’

-associated with mild methlymalonic aciduria
TCA intermediated increased in urine

76
Q

What are the 3 main functions of OxPhos?

A
  1. Transfer e- from nadh and fadh2 to 0xygen
  2. est a proton gradient across the inner mito membrane
  3. make ATP
77
Q

What two factors constitute the proton motive force drive ATP synth in OxPhos?

A

ph gradient

Membrane potential

78
Q 
What are the inhibitors of OxPhos proteins? and their names?
Complex 1
2
3
4
5
A

1: NADH: ubiquinone Oxidoreductase
- –RAMP- Rotenone, Amytal, Myxothiazol, PiericidinA

2: Succinate DH (TCA)
- –Malonate

3: Cytochrome C reductase
- –Antimycin–> H2O2 buildup from superoxide

4: Cytochrome C Oxidase
- –Cyanide, CO, H2S

5: ATP Synthase
- –Oligomycin

79
Q

What does Dinitrolphenol DNP do?

A

lowers ATP synthesis
increases fuel consumption, oxygen consump, and heat production

It is an uncoupler–affect Complex 5 but not the rest….

80
Q

Oxphos effiecency is measured by what ratio?

A

Phosphate:O

81
Q

What happens in the Malate-Aspartate Shuttle in relation to the ETC?
Where is the body does it happen?

A

GAPDH in glycolysis generates NADH… which transfers a proton to Oxo–>Malate…which travels acros the mito membrane through the shuttle and re-distributes it back to a NAD+–> then enters complex 1 of OxPhos

Heart, liver, and kidney

82
Q

What does the Glycerophosphate shuttle generate and where does that insert into the ETC?

Where is the body is this occuring?

A

Generates FADH2 from G3P-DHAP of glycolysis
Inserts into Coenzyme Q

Skeletal muscle and brain

83
Q

What is the RL enzyme of FA synthesis?

Where do most of the NADPH molecules come from that are used?

A

Acetyl CoA Carboxylase (w/ biotin)… forming Malonyl CoA–which inhibits the FA degrade RL step

The PPP

84
Q

What makes up the Fatty Acid Synthase enzyme (turns Mal CoA—> palmitate?
What are the steps that it catalyzes?

A

2 id dimers, 7 enzymes, and an acyl carrier protein ACP that has a flexible arm

Condensation, Reduction, Dehydration, Reduction

85
Q

Where does elongation of Palmitate (Long chain fa) occur?
How many Fa’s at a time?
what is the reducing power?

A 
Smooth ER (Malonyl CoA) and Mitochondria (Acetyl CoA)
(as the C donors)

2 C at a time

NADPH

86
Q

To desaturate a FA, what enzyme is used? and what does it use to do it?

A

Acyl CoA Desaturase in the SER

using NADPH or NADH

87
Q

What can Lenolenic Acid (omega 3) be used to make?

A

EPA eicosapentanoic acid

DHA docosahexanoic acid

88
Q

What are omega 3s and 6s good for in the body?

A

Immune health, Cardiovascular, NS, Vision, Cell membranes

89
Q

Dietary TAGS are broken down where?
Using what key enzyme?
What do they form in the lymphatic system–then blood to get to adipose?

A

Intestinal cells—first broken down to MAG and FFA in the intest lumen, then remade to TAG in the Icells

FAcyl CoA Synthetase

Chylomicrons

90
Q

What paths work to make Glycerol 3P, which gets input into the FA synth path in the Liver cells?

What do liver TAGs form to join the chylomicrons in the blood?

A

Glycolysis: to DHAP–>G3P using glycerol 3P DH
Glycerol–>G3P using glycerol kinase

VLDL (Very Low Density Lipoprotein)

91
Q

What enzyme converts the FFAs from chylomicron breakdown and the VLDLs?

A

Capillary lipoprotein lipase

Then built up to form TAG in adipocytes

92
Q

What are the 3 main enzymes used in the breakdown of TAGS?

What hormones stimulate this?

A

Hormone Sensitive Lipase HSL
Lipoprotein Lipase LPL
Monoacylglycerol Lipase MAG Lipase

Glucagon, Epi, Norepi

93
Q

Hunger and exercise initiate TAG mobilization, what are key players in the breakdown?
Which is a target for obesity treatment?

A

cAMP
Protein Kinase A
ATGL
HSL

Perilipin—- Coats lipid droplets, controls the access to HSLipase—-this is the target (want to inhibit it)

94
Q

Where is phase 1 (activation) of FA oxidation occuring?

A

The cytosol—then enters the Inter mem space—-then Mito matrix

95
Q

What are the key players in the movement of FA across the Mito membrane?
What are the key enzymes?
What is one main inhibitor of this process? (from FA synthesis)

A

FA–Facyl CoA via Facyl CoA synthetase
enters intermem space

FACoA–Facyl Carnitine via CPT1 (——by Malonyl CoA)
–uses carnitine

FAC crosses inner membrane via CACT carn-acylcarn translocase

FAC–FAcylCoA via CPalmTransferase II
—carn then moves back to intermem via CACT

96
Q

Which enzyme of FA degradation is the RL step?

Where is it located?

A

Carnitine Palmitoyltransferase I

on the outer membrane–intermem space side

97
Q

What are the 4 basic steps of beta-oxidation (happening inside the mito matrix)?
What enzymes?

A

OHOT
Oxidation- acyl CoA DH–generates FADH2 for CoQ of ETC

Hydration- Enoyl CoA Hydratase

Oxidation- 3-hydroxyacyl CoA DH–generates NADH for complex I of ETC

Thiolysis- Acetyl CoA acetyltransferase— generates ACoA for TCA

whole processing of Palmitate gives 129 ATP

98
Q

What enzyme catalyzes the first Beta Ox step? What type is related to a specific deficiency?

A

ACAD
MCAD- 8C FA builds in liver, interferes with urea cycle, inc ammonia levels
Patients depend on glucose for fuel
Leads to secondary carnitine def.

99
Q

In odd number FA chains, What enzymes uniquely are used to degrade?

What product is formed (TCA)

Where do VLCFAs get metabolized?

A

Propionyl CoA Carboxylase (uses ATP and biotin)

Methylmalonyl CoA Mutase (uses vit B12)

Produces Succinyl CoA—-TCA

Peroxisomes

100
Q

Unsaturated FAs require what novel enzymes to be broken down?

A

Reductase- reduce double bond

Isomerase- move disruptive bond

101
Q

What Amino acids can be precursors to Oxaloacetate?

A

Aspartate Family
Asp, Asn

Thr, Lys, Met, Ile

102
Q

What Amino acids can be precursors to Alpha ketoglutarate?

A

Glutamate family
Glu, Pro, Gln, His, Arg
GAPH

103
Q

What amino acids can be precursors to Pyruvate?

A

Ala, Leu, Val

104
Q

What AAs can be precursors to PEP?

A

Aromatic family

Tyr, Trp, Phe

105
Q

Which end of a peptide does each type of Proteolytic enzyme work?
Exopeptidase
Endopeptidase

A

Exo: at the C or N terminus
Endo: within the protein at specific sites (internal bonds)

106
Q

Enterokinase is embedded in the intestinal membrane and activates what zymogen?

A

Trypsin from Trypsinogen–> activates Chymotrypsinogen and others

107
Q

What are the two purely ketogenic AAs?
What are the 5 keto/gluco AAs?
What are the Essential AAs?

A

Leu, Lys

PITTT- Phe, Ile, Trp, Tyr, Thr

PVT TIM HLL

108
Q

What do Transaminase reactions always need as a coenzyme?

A

Pyridoxyl 5’ Phosphate
-Vit B6 derivative

Alanine trans ALT—-for MI diagnosis
Aspartate Trans AST

109
Q

What disease can Methoinine metabolism relate to?

A

Homocystinuria
def. in vitamin B6, B12, Folic acid
Cystathionine beta-synthase (with a PLP Pyridoxal Phos cofactor)

110
Q

What is special about Phenyalanine?

What can it be converted into?

A

It’s glucogenic and ketogenic

Tyrosine and Fumerate (TCA)

111
Q

Why is tyrosine crucial to have? What can it help produce?

A

Thyroid hormones T3, T4 and endocrine regulation (GABA-neurotransmitter)

Seratonin—-Melatonin
Niacin—NAD+ w/ B6 help

112
Q

What is nitrogen removed as in the brain?

How about in other tissues?

A

Glu and Gln

Gln and Ala

113
Q

Where is urea formed?

Where is urea excreted?

A

Liver and kidneys

Kidneys–urine

114
Q

What is the process of Ammonia removal from the brain?

A

Alpha keto—>Glu adding NH4 (glutamate DH)
Glu–>Gln adding NH4
Gln shunted to blood and Liver to the urea cycle

115
Q

What is the process of removing excess ammonia from muscle?

A

Ala–>leaves muscle w/ NH4 from AAs–>Glu

Drops it off in the liver for urea cycle and then can return as glucose–>glycolysis to pyruvate

116
Q

What two enzymes are used to take NH4 from Ala all the way to the urea cycle in the liver?

A

ALT aminoacyl transferase
GLDH Glutamate dehydrogenase
Uses glutamate and alpha keto

117
Q

What is the start and end product in purine synthesis?
What is the RL step products?
What is special about the formation of the end products (GTP, ATP)?
What drug is used to inhibit cancer division in the path?

A

R5P from PPP and either GTP/ATP, dATP, dGTP

PRPP–>PRA using G. PRP Amidotransferase

They cross stimulate each other—form of one stim the other to be formed

Methotrexate– targets folate enzyme (DHFR)
-prevents oxidation of NADPH, disrupts DNA replication in cancer cells

118
Q

What is the important first intermediate in Pyrimidine synthesis?
Formation of what in the path happens elsewhere before returning to the cytosol?
What Purine Synth intermediate is incorporated toward the end of the path?
What is the RL step?

A

Carbamoyl Phosphate by CPSII—urea cycle can affect levels leading to hyperammonia w/ orotic aciduria

Orotate in the mitochondria briefly

PRPP (first step in Pur Synth)

Aspartate Transcaramoylase (second step)
-CP--> Carbamoyl Aspartate
119
Q

What do “Sulfa” drugs do? Where is the key found in Purine synthesis?

A

Competitively inhibit a bact. enzyme incorporating PABA into Folate—-in Pur, incorporated into PRA in lengthy step

Humans get folate vitamin in diet
BACTERIA

120
Q

In Purine Catabolism, what is one of the second steps in the path, what is the enzyme? and What can be caused by an excess of it? but mainly a defeciency?

What is the main enzyme used in the end? What can it cause? and What drug is used to inhibit it?

A

Adenosine–>Inosine using Adenosine Deaminase

  • -excess= Hemolytic Anemia
  • -Def= SCID—–bubble boys

Xanthine Oxidase: HX–>X–>Uric acid
GOUT—-inhibited by Allopurinol (Zyloprim)

121
Q

What are important end products of Pyrimidine Catabolism?

A

Malonyl CoA
Succinyl Coa
Methylmalonyl CoA

122
Q

What is the important enzyme in the Nuc Salvage Pathways? Leading to what complications?

A

HGPRT-hypoxanthine guanine phosphoribosyl transferase

Lesch Nyhan syndrome
Kelley-Seegmiller syndrome

123
Q

What is the purpose of the drug Acyclovir?

A

Antiviral
Base that resembles Guanine…inserts into viral sequence
-lacks a 3’ OH group–so DNA replication is terminated

Helps to heal sores related to chicken pox, shingles , and HPV

SFM Final (4 decks)

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