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How many carbons do transketolases remove and what is required?
How many carbons do transaldolases remove?
The TPP on the Transketolase binds where?
On the E-NH2 group of a critical Lysine residue. Covalently bound via Schiff Base.
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.
How many fates of Ribulose-5-phosphate and what are they?
- Changed to Xylulose-5-phosphate via epimerase
- Changed to Ribose5-phosphatevua isomerization
What is Wernicke-Korsakoff Syndrome?
TPP (Vit B-1) deficiency in Transketolases. Seen in malnurashed alcoholics.
What is the NAD+/NADPH ratio?
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
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.
Where do the CH3 (methyl) groups on glutathione origenate?
What are Heinz Bodies? What causes them?
What happens to RBC when there is excessive oxidation. Loss of 3 structure. Leads to Hemolysis.
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
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.
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.
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.
G-6-P dehydrogenase Deficiency Mode of inheritance.
Similar to what?
- Pyruvate kinase deficiency
Fat soluble reducers.
H2O suluble reducers.
- Vit A,E
- Vit C, GSH,
How is O2- made? Where does the e- escape?
- electron binds to O2 creating O2-.
- at the Co Q.
- Can react with NO to create Peroxynitrate with will damage membrane bound proteins.
What is Lou Gehrigs disease?
Deficiency of Superoxide dismutase. Cannot break down superoxide. Neuromuscular damage. Sensory it still intact.
How are Hydroxyl radicals produced?
H2O2 (peroxide) + Fe++ --> OH (very reactive and harmful).
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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