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How many carbons do transketolases remove and what is required?
2, TPP
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How many carbons do transaldolases remove?
3
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The TPP on the Transketolase binds where?
On the E-NH2 group of a critical Lysine residue. Covalently bound via Schiff Base.
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What is the Rate Limiting step of HMP pathway?
What is the purpose of this pathway?
- Glucose-6-Phosphate Dehydrogenase.
- To create NADPH, Ribose-5-phosphate, and sugars of varying lengths.
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How many fates of Ribulose-5-phosphate and what are they?
- 2
- Changed to Xylulose-5-phosphate via epimerase
- Changed to Ribose5-phosphatevua isomerization
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What is Wernicke-Korsakoff Syndrome?
TPP (Vit B-1) deficiency in Transketolases. Seen in malnurashed alcoholics.
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What is the NAD+/NADPH ratio?
1/10
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Describe the reduction of ribonucleoside diphosphate to deoxyribonucleoside diphosphate.
What enzyme is required?
- Requires NADPH and Thioredoxin. NADPH reduces Thiorodoxin which in turn removes the Oxygen from Ribonucleoside to make H2O. The now oxidized Thioredoxin gets reduced.......
- Ribonucleotide reductase
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What is Glutathione made of?
Where is the SH group located?
What is its function? How?
- Glutamate, Glycine, and Cysteine
- SH group is on the Cysteine
- To keep proteins in essential reduced state. Does this by sacrificing its high energy SH bond for a S-S bond.
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Where do the CH3 (methyl) groups on glutathione origenate?
From Methionine
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What are Heinz Bodies? What causes them?
What happens to RBC when there is excessive oxidation. Loss of 3 structure. Leads to Hemolysis.
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What is Glutathione Peroxidase? What does it require to function?
What reestablishes the SH bonds?
Ratio of GSH/GSSH
- It detoxifies Peroxied (H2O2). GSH + H2O2--> GSSG + H2O
- Requires Se as a cofactor
- NADPH
- 500/1
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What is Glutathione-S-Transferase and what is its purpose?
Give an example of its use.
- Attaches Glutathione to toxic molecules to make them more soluble.
- Seen in detoxifying high levels of Acetaminophen.
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What does Cytochrome P450 do?
- Creates -OH groups of poorly soluble molecules, and breaks down acetominophen to a toxic intermediate that is detoxified by GSH-transferase.
- Very active in the liver.
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What makes NO? What enzyme and what is needed?
Whats is its function?
- Arginine + NADPH--> NO
- NO synthase (Needs Ca)
- NO is a vasodialator. easily crosses the cell membranes and activates NO dependent Guanylate cyclase that creates cGMP in muscle cells.
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G-6-P dehydrogenase Deficiency Mode of inheritance.
Similar to what?
- X-linked
- Pyruvate kinase deficiency
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Fat soluble reducers.
H2O suluble reducers.
Others
- Vit A,E
- Vit C, GSH,
- Bilirubin
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How is O2- made? Where does the e- escape?
Reactions
- electron binds to O2 creating O2-.
- at the Co Q.
- Can react with NO to create Peroxynitrate with will damage membrane bound proteins.
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What is Lou Gehrigs disease?
Deficiency of Superoxide dismutase. Cannot break down superoxide. Neuromuscular damage. Sensory it still intact.
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How are Hydroxyl radicals produced?
H2O2 (peroxide) + Fe++ --> OH (very reactive and harmful).
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Superoxide dismutase is made of what in the cytosole and mitochondria?
Catalase is found where? Its function?
- cytosol Zn, Cu
- Mitochondria Mn, Cu
- In peroxisomes.
- uses H2O2 in detoxification of particles.
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