Bio 1 Flashcards
Mention Sources of ammonia and its bood level
1- Deamination of amino acid 2 Trandamination of most amino acids. 2 steps de→Trans
3- Released during purines catabolism
4- intestinal bacteria.
5- glutamine → NH3 + glutamate
6- From monoamines by MAO.
its blood level 10:60 Mg/dL.
Hepa Merz role in Treating Hyperammonia
LOLA adminstration increase Level of glutamate Level as They’re subtrates For glutamate transferase
ammonia as its utilized by making glutamine.
Mechanism of Sodium benzoate in ammonia
Sodium bezoate and glycine make hippurate which excreted by kidney and help in ammonia Loss.
How Lactulose decease nitogenous bad from gut
what also decrease it.
↓nitrogenous load through
1- Reduction of intestinal bacteria.
2- Acidification of The gut (Laculose lactic acid)
3-inhibit ammonia producing bacteria and increase non-ammonia producing bacteria
B/ Antibiotics
↓ Load by killing the bacteria.
mention amino acids Yellds Acetoacetate Acetyl CoA
Ketogenic amino acids
Lucine Lysine
Mention Mixed amino acids
Tyrosine
Tryptophan
Threonin
Iso lucine
phenylalanin
تف
Mention causes of ammonia Toxicity
1- interfere ATP production of brain
use a ketoglutarate →glutamate not ATP
2-synthesis of glutamine from glutamate (GABA)
deletrious effects
3- increased ammonia cause increase permeability of K, CL which interfere electrical activity of The brain.
How ammonia transported in The blood?
1- Free
2-Glutamine
3- Alanin
Alanin/Glucose cycle
Rate limiting Enzyme of urea Cycle
- Its regulation.
- Carbomyl phosphate synthetasel
↑ activated by
Nacetyl glutamate whic its synthetase enzyme activated by Arginine
area cycle and main points.
(1) carbo myl phosphate synthetase! 2 Atp
NH3 + CO2
N from ammonia
(2) make citrulline by
ornithine Transcarbamylase →
Cp+ ornithine.
B) Argininosuccinate by synthase
1 Atp
Citruline+ Aspartate (2nd N of urea)
(4) cleavage Argininosuccinate by
Arginosaccinase→
Arginine + Fumarate
(5) Arginin cleavage Arginase ornithine +urea.
Q: Mention 2 major Transaminases and Their reactions
•ALT (pyruvic)
glutamate + pyruvic ←→a keto. + Alanin
•Ast (oxabacetate)
Glutamate + oxaloacetate←→α keto +aspartate
Q: Mention amino acids can’t undergo transamination?
Q: What’s the Coenzyme for aminotransferases
A1:
1- Lysine
2-Threonine
3- proline, Hydroxy proline.
A2:
vit. B6 /plp
Mention non-oxidative deamination enzymes.
1- Glutaminase
2- Asparginase
Give example of axiditative deamination enzymes and their reactions.
(1) Glutamic Acid dehydrogenase
a keto. + NH3 ←→ glutamate
Reversible
NAD in oxidation
NADP in Reduction
inhibitors: ATP GTP NADPH activators: GDP ADP
(2) D-amino acid oxidase use FAD as coenzyme
Deaminate → Glycine
Enumerate Fates of ammonia
1- urea cycle
2- Excreted by kidney as urine
3-synthesis of glutamine by kidney!
- Smthesis of non-essential aminoa.
5- glutamate synthesis by GAD
Keto. + NH3 ←→Glutamate
Define one carbon unit?
What are The Carriers?
Transfere a single C from a donor to an acceptor
carriers of carbon unit:
1- SAM carry (CH3)
2- Biotin Carry Co₂
3-THF carry all carbons at N5,N10
What are types of one carbon unit?
CH3 Methyl
CH2 Methyelen
CH Methenyl
CHO Formyl group
CH=NH Formimino group
Mention Sources of Methelyen. CH2
1- Beta carbon of Serine
Serine →→ glycine
by ser hydroxy methyl transferase
2 Glycine
glycine cleavage enzyme.
Mention fate of Methylene.
CH2
1- Synthesis of thymidylate
- oxidized to Methenyl-CH
3- Reduced to Methyl CH3
Fate of Methenyl =CH
Hydrolysed to Formyl group THF
Mentionall
Sources of MethenyL
- Histidine
→Figlu→ 5- formimino THF ->
5.10 Methenyl THF
2- oxidation of Methynene.
CH2→ CH
NADP dehydrogenase.
Mention Sources of Furmyl group 0=CH
1- Free Fumarate ATP activate it.
2- Tryptophan catabolism
3- Hydrolysis of methenyl.
Q: Mention Fate of Formy L group 0=CH
synthesis of C2, C8 in purines
Mention
Sources of Methyl
CH3
- Reduction of Methylene_CH₂ by Reductase enzyme. (NAD linked)
