1. At physiological pH ammonia exists as? 2. Storehouse for ammonia? Storage & transport? 3. To transport ammonia from muscle to liver 4. Synthesis of glutamine occurs in? 5. Glutamine is formed by? Which enzyme? 6. Glutamine is degraded by? 7. Normal plasma concentration of ammonia?

1. Ammonium ion NH4+ 2. Glutamine 3. Alanine 4. Liver Brain Muscle 5. From glutamate & ammonia By Glutamate synthase 6. Glutaminase 7. 15-45 ug/dl

1. When ammonia accumulate it causes? 2. What happens when ammonia combine to a-ketoglutarate? 3. Explain why ammonia is toxic to brain? 4. Which frugs are used when elevated plasma level of ammonia? 5. What happens in hepatic coma? 6. End product of protein metabolism? 7. What accounts for 80-90% of nitrogen excreted in urine? 8. Management of hepatic coma includes?

1 Slurring of speech Blurring of vision Tremors 2. Forms glutamate (Reversed by glutamate dehydrogenase) 3. In the rxn catalysed by glutamate dehydrogenase If ammonia increases------more glutamate-----less a ketoglutarate so more of it is taken from TCA cycle ---- impaired---- less ATP----impairs brain 4. Intravenous administration of; Sodium benozoate Phenyllactate (Form water soluble product with glutamate) 5. Hepatic encephalopathy Liver disease----affects brain 6. Urea 7. Urea 8. Restrict protein diet antibioticsfor bowel infections acid-bace balance Avoid hepatotoxic drugs

1. Clinical manifestation of albinism? 2. Localized hypermigmentation leads to? 3. What is piebaldism? 4. Main difference between leucoderma and vitiligo? Both are example of _____ hypopigmentation? 5. An example of diffused hypopigmentation! 6. Liver can fail in which disorder? 7. Which disorder is called black urine disease?

1. Sensitive to light Susceptible to skin cancer Photophobia (intolerance to light bcz lack of eyepigment) But normal eyesight 2. moles bcz of hyperactivity of melanocytes 3. Grey forelock of hair, scattered normal pigmented and hypopigmented areas on forehead - related to melanocytes - leucoderma - - - hypopigmentation starts from hands - vitiligo - - - around mouth, nose, eyes, nipple - localized hypomigmentation 5. Oculocutaneous albinism 6. Tyrosinosis/ Tyrosinemia I 7. Alkaptonuria (homogentisate - - - - oxidized to quinone - - - black color)

1. Patients with alkatonuria give which positive tests and wh? 2. Cabbage like odour is associated with which disorder? 3. Ochronosis and arthritis arr associated with which disorder? 4. In which disorder, tge patient responds to ascorbic acid? 5. Dermatitis, eye lesion are characteristics of which disorder? This disease is also known as? 6. Why is it called catechol? 7. Difference between epinephrine and Norepinephrine is only? 8. Norepinephrine is methylated by what to give epinephrine?

1. Positive ; Ferric chloride Silver nitrate Benedicts test (because of strong reducing activity of Homogentisate 2. Tyrosinosis or Tyrosinemia I 3. Alkaptonuria (Homogentisate - - - - - Benzoquinone acetate - - - - Alkaptone (deposit in tissues bones and organs) 4. Neonatal Tyrosinemia (substrate inhibition is overcome) - bcz ascorbic acid is used as coenzyme by P-HydroxyPhenyl Pyruvate dioxygenase 5. Tyrosinemia type II Richnert Hanhart syndrome 6. Because of dihydroxylated Phenyl ring 7. A methyl group (nor epinephrine has No methyl) 8. S-adenosyl methonine

1. Name Dopa analogs given yo parkinsons patients? And why? 2. Which 2 enzymes convert tyrosine to DOPA? 3. Precursor of melanin in synthesis from tyrosine is? 4. Black melanin is formed by? And red pigment? 5. Tyrosinase is a ___ containing oxygenase? 6. What type of protein is Homogentisate oxidase? 7. Ascorbic acid is needed by which enzyme in tyrosine metabolism?

1. Carbidopa a-Methyldopa Bcz Dopamine can't cross blood brain barrier so it's administration is useless So L-DOPA is used 2. tyrosinase (melanin synthesis) Tyrosine hydroxylase (catecholamines synthesis) 3. dopaquinone 4. - black - - -. melanochromes formed from indole quinone - - - polymerization----black melanin red Cysteine condenses with dopaquinone - - - red pigment 5. Copper 6. iron metalloprotein 7. P-HydroxyPhenyl Pyruvate dioxygenase (hydroxylase)

1. Kinureninase is a ______ dependant enzyme? Sensitive to? 2. In vitamin B6 deficiency what will form from 3-hydroxykynurenine? 3. Kinurenine hydroxylase is inhibited by? So what happens 4. Immediate precursor for NAD+ Acetyl coA 5. Cats have high activity of? So they are dependent on niacin? 6. How tryptophan is gluconeogenic and ketogenic? 7. Quinolinate is converted to nicotinamide mononucleotide by which enyzme?

1. Pyridoxal phosphate (PLP) - vitamin B6 deficiency 2. xanthurenate (elevates levels in urine--- indication of B6 deficiency) 3. Estrogen So No NAD (Niacin) formed So women are more Susceptible to pallegra 4. NAD+ - - - - quinolinate Acetyl coA - - - - glutaryl coA (from 2 aminomuconate) 5. picolinate carboxylase (competes with formation of quinolinate (so No NAD+ can be formed from tryptophan, so they have to rely on Niacin vitamin for NAD+) 6. Products formed: Alanine - - - - glucose Acetyl coA - - - - fat 7. Quinolinate phosphoribosyl transferase (QPRT)

1. Serotonin is degraded by? And product? 2. Largest amount of serotonin is synthesized in? 3. Name the drugs that elevate / depress serotonin levels? 4. Name a phsychic stimulant? How it works 5. Serotinin producing cells of GIT? And their uncontrolled growth leads to? 6. Melatonin is synthesized from serotinin by? 7. Rate limiting enzyme in melatonin synthesis? 8. Which amino acid is a sleep inducing amino acid?

1. MonoAmine oxidase (MAO) - product 5HIA (5-HydroxyIndole Acetate) 2. Intestinal cells 3. Elevate: iproniazid (inhibits MAO) -antidepressant Depress: Reserpine -( inc. Degradation of serotinin) - depressant drug 4. psychic stimulant Lysergic acid diethylamide (LSD) (Activates serotinin receptors) 5. argentaffin cells - argentaffinomas (malignant carcinoid syndrome) 6. Methylation (SAM) s-adenosyl methionine 7. serotinin N-acetylase (serotinin - - - - N-acetyl serotinin) 8. Tryptohan

1. Structure of tryptophan? Chemical name? 2. Tryptophan is precursor for? 3. Name 2 pathways in which tryptophan is metabolized? Which enzyme first acts? And what dependent enzymes) 5. Which enzyme in Kynurenine-anthranilate pathway is NADPH dependent? Which is PLP dependent 6. Alanine is produced bt action of which enzyme? 7. Serotinin is also called? 8. Platelet contain high conc of ____ but donot synthesise it?

1. Indole ring (5-membered) -a-amino B-indole propionic acid 2. NAD+ & NADP+ (niacin coenzymes) Serotinin Melatonin Gluconeogenic Ketogenic 3. Kynurenine-anthranilate pathway - Tryptophan pyrrolase (iron containing) Serotinin pathway - tryptophan hydoxylase (BH4) 5. Kynurenine Hydroxylase (NADPH) Kynureninase (PLP) 6. Kynureninase on 3-hydroxykynurenine 7. 5- hydoxytryptamine (5HT) 8. 5HT (Serotinin)

1. Name sulphur containing amino acids? 2. Precursor for cysteine and cystine? 3. Which amino acid can spare the requirrment of methionine? 4. Active form of methionine? 5. Define transmethylation? 6. What type of compound is SAM? 7. How many ATPS are consumed in formation of SAM?

1. Methionine Cysteine Cystine 2. Methionine 3. Cysteine 4. S-adenosylmethionine (SAM) 5. Transfer of methyl group from active methionine to an accepter 6. Sulfonium compound (S+) (So highly reactive due to positive charge) 7. 3 ATPs

1. Homocysteine can be rementhylated to methionine by which enzyme? And deficiency of this leads to? 2. Which enzyme require vitaminB12 and THF? 3. Prrcursor for methionine? 4. Carbon fragment of SAM is involved in synthesis of? 5. Precursor for a plant hormone, ethylene is? 6. Precursor for cysteine? 7. Enzyme involved in synthesis of cyateine from homocysteine? And uses what? It's deficiency leada to?

1. N5 - Methyl Tetrahydrofolate Homocysteine Methyl Transferase --- deficiency leads to homocystinuria III 2. Homocysteine methyltransferase 3. Homocysteine (which is derived from methionie itself so methionine is broken down... Its a cycle) that's why methionine is essential amino acid 4. (polyamines) Spermidine Spermine 5. SAM (S-adenosylmethionine) - this hormone causes growth of plants and ripening of fruits 6. Homocysteine (intermediate formed from methionie) 7. Cystathione B-synthase (CBS) (PLP dependent) - vitamin B6 - serine Deficiency: homocystinuria I

1. 2 products from Cystathione (from homocysteine)? 2. What type of rxn is formation of cysteine from homocysteine? 3. What part of cysteine come from Homocysteine Serine 4. Which amino acid is elevated in heart attacks or coronary artery disease? -how it causes? 5. How homocysteine affects pregnancy? 6. How plasma homocysteine level is lowered? 7. Taurocholate (taurine) which conjugates with bike acids is produced by? 8. Mucopolysaccharide is produced ny whivh amino acid?

1. Cysteine Succinyl coA 2. transulfation 3. Homocysteine--- only Sulfur Serine - - - rest of molecule 4. Homocysteine -aggregation of LDL particlez - reactive free radicals - interfering with collagen cross links 5. hyper homocysteinemia - - - - neural tube defects in fetus 6. Administratons of: Folic acid Vitamin B12 Vitamin B6 7. Cysteic acid from Cysteine degradation 8. Cysteine (from PAPS 3-Phosphoadenosine 5-phosphosulfate

Chp 15; Metabolism Of Amino Acids Flashcards by Anonymous Reader

At physiological pH ammonia exists as?
Storehouse for ammonia? Storage & transport?
To transport ammonia from muscle to liver
Synthesis of glutamine occurs in?
Glutamine is formed by?
Which enzyme?
Glutamine is degraded by?
Normal plasma concentration of ammonia?

Ammonium ion NH4+
Glutamine
Alanine
Liver
Brain
Muscle
From glutamate & ammonia
By
Glutamate synthase
Glutaminase
15-45 ug/dl

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When ammonia accumulate it causes?
What happens when ammonia combine to a-ketoglutarate?
Explain why ammonia is toxic to brain?
Which frugs are used when elevated plasma level of ammonia?
What happens in hepatic coma?
End product of protein metabolism?
What accounts for 80-90% of nitrogen excreted in urine?
Management of hepatic coma includes?

1
Slurring of speech
Blurring of vision
Tremors

Forms glutamate
(Reversed by glutamate dehydrogenase)
In the rxn catalysed by glutamate dehydrogenase
If ammonia increases——more glutamate—–less a ketoglutarate so more of it is taken from TCA cycle —- impaired—- less ATP—-impairs brain
Intravenous administration of;
Sodium benozoate
Phenyllactate
(Form water soluble product with glutamate)
Hepatic encephalopathy
Liver disease—-affects brain
Urea
Urea
Restrict protein diet
antibioticsfor bowel infections
acid-bace balance
Avoid hepatotoxic drugs

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Phenylalanine is structurally related to what amino acid?
And they aliphatic or aromatic?
Essential / Non?
Fuction of phenylalanine?
Fuctions of tyrosine?
Why these both arr glucogenic & ketogenic?
Phenylalanine is converted to tyrosine by which enyzme?
Coenzyme? Which ring? Structurally related to what?
Active form of biopterin is?
Oxidized by phenylalanine hydroxylase to?
BH4 is regenerated by ______ dependent enzyme?
Reaction requires?

Tyrosine
- aromatic
- Phenyl alanine - - - - essential
Tyrosine - - - non essential
Incorporated into proteins
- converted into tyrosine
For the synthesis of:
Dopamine
Epinephrine
Norepinephrine
Melanin
Thyroid hormone (T3 & T4)
glucogenic

Fumarate is formed - - - - converted into glucose
& used in TCA cycle

KETOGENIC

acetoacetate - - - - into fat

Phenylalanine hydroxylase
- coenzyme : biopterin
(pteridine ring)
- structurally related to folate
Tertrahydrobiopterin (BH4)
Oxidised to BH2
NADPH dependent dihydrobiopterin reductase
Molecular O2

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Deficiency of which enzyme causes?
Phenylketonuria
Tyrosinemia II
Neonatal Tyrosinemia
Alkaptonuria
Tyrosinemia I (tyrosinosis)
Albinism

Phenylketonuria - - - - Phenylalanine Hydroxylase

Tyrosinemia II - - - - - Tyrosine transaminase

Neonatal Tyrosinemia - - - - P-HydroxyPhenyl Pyruvate

Alkaptonuria - - - - - - Homogentisate oxidase

Tyrosinemia I (tyrosinosis) - - - -
fumarylacetoacetate Hydroxylase
maleylacetoacetate isomerase

Albinism - - - - - Tyrosinase

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Clinical manifestation of albinism?
Localized hypermigmentation leads to?
What is piebaldism?
Main difference between leucoderma and vitiligo?
Both are example of _____ hypopigmentation?
An example of diffused hypopigmentation!
Liver can fail in which disorder?
Which disorder is called black urine disease?

Sensitive to light
Susceptible to skin cancer
Photophobia (intolerance to light bcz lack of eyepigment)
But normal eyesight
moles bcz of hyperactivity of melanocytes
Grey forelock of hair, scattered normal pigmented and hypopigmented areas on forehead
- related to melanocytes

leucoderma - - - hypopigmentation starts from hands
vitiligo - - - around mouth, nose, eyes, nipple
localized hypomigmentation

Oculocutaneous albinism
Tyrosinosis/ Tyrosinemia I
Alkaptonuria (homogentisate - - - - oxidized to quinone - - - black color)

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Patients with alkatonuria give which positive tests and wh?
Cabbage like odour is associated with which disorder?
Ochronosis and arthritis arr associated with which disorder?
In which disorder, tge patient responds to ascorbic acid?
Dermatitis, eye lesion are characteristics of which disorder?
This disease is also known as?
Why is it called catechol?
Difference between epinephrine and Norepinephrine is only?
Norepinephrine is methylated by what to give epinephrine?

Positive ;
Ferric chloride
Silver nitrate
Benedicts test
(because of strong reducing activity of Homogentisate
Tyrosinosis or Tyrosinemia I
Alkaptonuria
(Homogentisate - - - - - Benzoquinone acetate - - - - Alkaptone (deposit in tissues bones and organs)
Neonatal Tyrosinemia
(substrate inhibition is overcome)
- bcz ascorbic acid is used as coenzyme by P-HydroxyPhenyl Pyruvate dioxygenase
Tyrosinemia type II
Richnert Hanhart syndrome
Because of dihydroxylated Phenyl ring
A methyl group
(nor epinephrine has No methyl)
S-adenosyl methonine

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Name Dopa analogs given yo parkinsons patients? And why?
Which 2 enzymes convert tyrosine to DOPA?
Precursor of melanin in synthesis from tyrosine is?
Black melanin is formed by?
And red pigment?
Tyrosinase is a ___ containing oxygenase?
What type of protein is Homogentisate oxidase?
Ascorbic acid is needed by which enzyme in tyrosine metabolism?

1.
Carbidopa
a-Methyldopa
Bcz Dopamine can’t cross blood brain barrier so it’s administration is useless
So L-DOPA is used

tyrosinase (melanin synthesis)
Tyrosine hydroxylase (catecholamines synthesis)
dopaquinone
- black - - -.
  melanochromes formed from indole quinone - - - polymerization—-black melanin

red

Cysteine condenses with dopaquinone - - - red pigment

Copper
iron metalloprotein
P-HydroxyPhenyl Pyruvate dioxygenase (hydroxylase)

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Kinureninase is a ______ dependant enzyme?
Sensitive to?
In vitamin B6 deficiency what will form from 3-hydroxykynurenine?
Kinurenine hydroxylase is inhibited by? So what happens
Immediate precursor for
NAD+
Acetyl coA
Cats have high activity of? So they are dependent on niacin?
How tryptophan is gluconeogenic and ketogenic?
Quinolinate is converted to nicotinamide mononucleotide by which enyzme?

Pyridoxal phosphate (PLP)
- vitamin B6 deficiency
xanthurenate
(elevates levels in urine— indication of B6 deficiency)
Estrogen
So No NAD (Niacin) formed
So women are more Susceptible to pallegra

4.
NAD+ - - - - quinolinate
Acetyl coA - - - - glutaryl coA (from 2 aminomuconate)

picolinate carboxylase
(competes with formation of quinolinate (so No NAD+ can be formed from tryptophan, so they have to rely on Niacin vitamin for NAD+)
Products formed:
Alanine - - - - glucose
Acetyl coA - - - - fat
Quinolinate phosphoribosyl transferase (QPRT)

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Serotonin is degraded by? And product?
Largest amount of serotonin is synthesized in?
Name the drugs that elevate / depress serotonin levels?
Name a phsychic stimulant?
How it works
Serotinin producing cells of GIT? And their uncontrolled growth leads to?
Melatonin is synthesized from serotinin by?
Rate limiting enzyme in melatonin synthesis?
Which amino acid is a sleep inducing amino acid?

MonoAmine oxidase (MAO)
- product 5HIA (5-HydroxyIndole Acetate)
Intestinal cells
Elevate:
iproniazid
(inhibits MAO)
-antidepressant

Depress:
Reserpine
-( inc. Degradation of serotinin)
- depressant drug

psychic stimulant
Lysergic acid diethylamide (LSD)
(Activates serotinin receptors)
argentaffin cells

argentaffinomas (malignant carcinoid syndrome)

Methylation
(SAM) s-adenosyl methionine
serotinin N-acetylase
(serotinin - - - - N-acetyl serotinin)
Tryptohan

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Structure of tryptophan?
Chemical name?
Tryptophan is precursor for?
Name 2 pathways in which tryptophan is metabolized?
Which enzyme first acts?
And what dependent enzymes)
Which enzyme in Kynurenine-anthranilate pathway is NADPH dependent?
Which is PLP dependent
Alanine is produced bt action of which enzyme?
Serotinin is also called?
Platelet contain high conc of ____ but donot synthesise it?

Indole ring (5-membered)
-a-amino B-indole propionic acid
NAD+ & NADP+ (niacin coenzymes)
Serotinin
Melatonin
Gluconeogenic
Ketogenic
Kynurenine-anthranilate pathway
- Tryptophan pyrrolase (iron containing)

Serotinin pathway
- tryptophan hydoxylase
(BH4)

Kynurenine Hydroxylase
(NADPH)
Kynureninase
(PLP)
Kynureninase on 3-hydroxykynurenine
5- hydoxytryptamine (5HT)
5HT (Serotinin)

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Name sulphur containing amino acids?
Precursor for cysteine and cystine?
Which amino acid can spare the requirrment of methionine?
Active form of methionine?
Define transmethylation?
What type of compound is SAM?
How many ATPS are consumed in formation of SAM?

Methionine
Cysteine
Cystine
Methionine
Cysteine
S-adenosylmethionine (SAM)
Transfer of methyl group from active methionine to an accepter
Sulfonium compound
(S+) (So highly reactive due to positive charge)
3 ATPs

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Homocysteine can be rementhylated to methionine by which enzyme?
And deficiency of this leads to?
Which enzyme require vitaminB12 and THF?
Prrcursor for methionine?
Carbon fragment of SAM is involved in synthesis of?
Precursor for a plant hormone, ethylene is?
Precursor for cysteine?
Enzyme involved in synthesis of cyateine from homocysteine?
And uses what?
It’s deficiency leada to?

N5 - Methyl Tetrahydrofolate Homocysteine Methyl Transferase
— deficiency leads to homocystinuria III
Homocysteine methyltransferase
Homocysteine (which is derived from methionie itself so methionine is broken down… Its a cycle) that’s why methionine is essential amino acid
(polyamines)
Spermidine
Spermine
SAM (S-adenosylmethionine)
- this hormone causes growth of plants and ripening of fruits
Homocysteine (intermediate formed from methionie)
Cystathione B-synthase (CBS)
(PLP dependent)
- vitamin B6
- serine
Deficiency:
homocystinuria I

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2 products from Cystathione (from homocysteine)?
What type of rxn is formation of cysteine from homocysteine?
What part of cysteine come from
Homocysteine
Serine
Which amino acid is elevated in heart attacks or coronary artery disease?
-how it causes?
How homocysteine affects pregnancy?
How plasma homocysteine level is lowered?
Taurocholate (taurine) which conjugates with bike acids is produced by?
Mucopolysaccharide is produced ny whivh amino acid?

Cysteine
Succinyl coA
transulfation

3.
Homocysteine— only Sulfur
Serine - - - rest of molecule

Homocysteine
-aggregation of LDL particlez
- reactive free radicals
- interfering with collagen cross links
hyper homocysteinemia - - - - neural tube defects in fetus
Administratons of:
Folic acid
Vitamin B12
Vitamin B6
Cysteic acid from Cysteine degradation
Cysteine (from PAPS 3-Phosphoadenosine 5-phosphosulfate

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Cysteine on degradation will give?
Which amjno acid is a component of tripeptide glutathione?
COAL in urine is exhibited in which disorder? And what characteristics?
What test is done for it?
Clinical manifestation of patients of homocystinuria?
Enzyme defects in:
Homocystinuria I
Homocystinuria II
Homocystinuria III
Homocystinuria IV
Cystinosis
Cystinuria
Coenzyme A is formed from whicj amino acid?

Sulfur (H2S)
Ammonia
Pyruvate
Cysteine
Cystinuria
(defective reabsorption from kidney tubule PCT)
- cystine stones in kidneys and UT
- Cyanide Nitroprusside Test
High levels of Homocysteine
- Myocardial infarction
- Stroke
- pulmonary embolism

4.
Homocystinuria I - - - - cystathione synthase

Homocystinuria II - - - - N5-N10____ Methylene THF reductase

Homocystinuria III - - - N5_____Methyl THF homocysteine Methyltransferase

Homocystinuria IV - - - - not enzyme.. defect in intestinal absorption of vitamin B12

Cystinosis - - - - cystine reductase (renal failure)
(deposition of cystine in tissues)

Cystinuria - - - - defect in reabsorption from kidney tubule PCT
(increased excretion of cysteine (COAL) In urine)

Cysteine - - - - decarboxylation - - - - mercaptoethanol amine (with vitamin pentothenic acid) - - - - CoA

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ONE carbon metabolism involves what essentials?
One carbon unit covalently binds to what position of THF?
After release of methyl group, methionine is converted into?
Regulatory enzyme for Branched chain amino acid metabolism is?
Comparaple to which enzyme?
Which of these is
Glycogenic/ketogenic?
Valine
Leucine
Isoleucine
Maple syrup urine disease is due to deficiency of which enzyme?
These patients respond to?
Partial blockage of a-keto acid dehydrogenase leads to?
Isovaleric acidemia is due to deficieny of?
Disorder of?
Cheesy ordour in vreath is present in?

Vitamin B9 (Folic acid) (Tetrahydrofolate)
Vitamin B12
S-adenosylmethionine (SAM)
N5 Or N10 or both
Homocysteine
a-ketoacid dehydrogenase
- pyruvate dehydrogenase
(5 coenzymes)

5.
Valine - - - glucogenic (converted to propionyl coA - - - glucose)

Leucine- - - ketogenic (converted to acetyl coA & acetate - - - fatty acid synthesis)

Isoleucine - - - - both

a-keto acid dehydrogenase
(branched chain amino acid disorder)
- thiamine
Intermittent branched chain ketonuria
Isovaleryl coA dehydrogenase
- leucine
Isovaleric acidemia

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Name the 3 amino acids that have a common product glutamate?
Histidine form which one carbon unit?
Deficiency of which enYme will cause histidinemia?
Characterized by?
Defect in which enzyme will cause
Hyperprolinemia type 1
Hyperprolinemia type 2
High conc of citrulline in human brajn is due to?
Arginine is a precursor for?

HAP
Histidine
Arginine
Proline
Formimino group
histidase
(cleaves ammonia off Histidine)
- defective speech

4.
Hyperprolinemia type 1 - - - proline oxidase/dehydrogenase

Hyperprolinemia type 2 - - - - hydroxyproline metabolism

Nitric oxide synthesis
Urea & ornithine
NO & citrulline
Creatine

Deficiency of folate will have elevated levels of what in urine?
Which step in histidine metabolism requires folate (Tetrahydrofolate)?
Histamine is produced from?
Its functions?
Name antihistamine drugs?
Therapeutic drug to treat angina pectoris has which compound in it?
Endothelium derived releasing factor which causes smooth muscle relaxation is?
Mechanism of action of NO?
What is Agmatine?

FIGLU formiminoglutamate
FIGLU - - - - - glutamate
(enzyme: glutamate formiminotransferase)
Decarboxylation of histidine
- HCL secretion
- causes asthma & allergic rxn
Omeprazole
Rantidine
Cimetidine
(bind & block histamine receptors)
Nitric oxide (NO)
in the form of
Nitroglycerin
Amylnitrate
Nitric oxide
cGMP
Protein kinase G
Derivative of Arginine
- antihypertensive
- produced in brain

Which amino acid doesnot take part in transamination?
What group of lysine maintains structural conformation of protein?
- is lysine glucogenic?
An immediate precursor for synthesis of glutamate in TCA?
Glutathione is a tripeptide containing?
Glutamate is present in which clotting factors? As?
What is GABA shunt?
GABA is synthesized from?
Vitamin b6 deficiency will affect GABA as?

Lysine
E-amino group
- no, ketogenic
a-ketoglutarate
Glutamate
Cysteine
Glycine
2,7,9,10
As y-carboxyglutamate
Bypass route for glutamate to enter TCA cycle
Decarboxylation of glutamate
By glutamate decarboxylase
(pyrridoxal phosphate (B6) dependant)
Reduced
- hyperexcitability & convulsions

Ammonia is temporarily stored in the form of?
Donor of nitrogen in purine and pyrinidine synthesis?
Which aminoacid is responsible for synthesis of carnitine?
Acid base balance is maintained by which amino acid? And which takes part in conguagatjion rxns?
Immediate precursor for carnitine synthesis?
Stiff person syndrome (SPS) is caused due to?
Chief source of ammonia in kidney?
_______ is an allosteric regulator of __________, the fiest enzyme in urea synthesis?

Glutamine
Glutamine
Lysine
Glutamine
trimethyllysine (from protein degradation)
(not free lysine)
Impaired synthesis of GABA
- Bcz of high glutamic acid decarboxylase (GAD) ** antibodies**
Glutamine
(ammonia fornation buffers H+ - - - - acid/base balance)
B-acetylglutamate
- first enzyme carbomyl phosphate synthase 1

What are polyamines?
Give examples?
Precursors for polyamine synthesis?
Which enzyme regulates polyamine synthesis?
Excretion of polyamines is elevated in?
Which polyamine is an ideal marker for cell proliferation?
Which polyamine is suitable for assessment of cell destruction?
The drug, Irrrversible suicide inhibitor of ornithine decarboxylase (ODC) ?

Posses multiple Amino groups (-NH2)
E.g
putrescine
Spermine
Spermidine
Ornitine & SAM (only 4-Carbon moeity not methyl group)
ornithine decarboxylase
All types of cancers
Putrescine
Spermidine
(DFMO) Difuoro methyl ornithine

Which drug is used for treatment of african sleeping sickness? How?
How cancer can be prevented in humans thru polyamines?
Rare example of an enzyme that doesn’t use pyrridoxal phosphate as a Coenzyme? What does it use then?
Putrescine is converted to Spermidine and Spermine by which enzymes?
Among the mammalian enzyme which one has the shortest half-life?
Its activity increased by what hormones?

DFMO (Difuoro methyl ornithine)
Selectively inhibits ornithine decarboxylase (ODC) of parasite trypanosoma
By inhibiting ODC and reducing polyamine synthesis, cell division and growth is blocked
SAM decarboxylase
- uses amino acid residue bound to Pyruvate as a cofactor
SAM (decarboxylated)
ornithine decarboxylase
(10 minutes)
- by
Growth hormone
Corticosteroids

Name essential hydroxy amino acid?
Dehydrogenation and decarboxylation of threonine results in formation of what, is converted to Pyruvate or lactate?

3.. Serine is interconvertivle with?
And is synthesized from?

Serine is involved in one carbon metavolisma nd gives ______ moeity to?
Serine undegoes deamination to produce?
On decarboxylation?
Seribe reacts with homocysteine to give?
And ehat parts of it are donated?
21st amino acid found in certain proteins?

Threonine
Amino acetone
Glycine
- from 3-phosphoglycerate
Methylene (-CH2) moeity
To Tetrahydrofolate
Deamination - - - - Pyruvate
Decarboxylation - - - ethanol amine (forms choline)
Cysteine
- entire cysteine from serine (only sulphur from homocysteine)
selenocysteine

Sphingomyelins and cephalins are formed from which amino acid?
Amino acid actibg as phosphate carriers in protein structure?
People with higher alanin in urine have?
Which amino acid is a constituent of vitamin pentothenic acid and thus Coenzyme A?
2 imp functions of alanine?

Serine

2.. Serine
Threonine

High BP
B-alanine
(* cysteine forms coA
B-alanine is constitient)

5.
Incorporation into proteins
Transamination & NH3 transport (alanine-pyruvate shuttle for carrying nitrogen)

Aspartate is formed from?
Aspartate transaminase is an imp enzyme for interconversion of?
2 amino grouos of urea come from?
Connecting link betseen urea cycle & TCA cycle is formed by which amino acid?
Asparagine is synthesized from ?

6.which amino acid is used for synthesis of purines & pyrinidine?

oxaloacetate (TCA cycle) by transamination
Glutamate & aspartate
1 from ammonia directly
1 from aspartate
Aspartate
(via oxaloacetate)
Aspartate
(irreversible ATP dependant rxn)
Aspartate
purines - - - N1, NH2 at 6th position
pyrimidine - - - - N3, C4, C5 & C6 atoms)

1. Moat abundant amino acid? 2. Glycine is synthesized from which amino acids? 3. 3. Collagen content of glycine? 4. Glycine undergoes oxidative deamination to liverate? 5. Which bile acids are congugated with glycine? 6. Give 1 function of glycine as a detoxifying agent?

1. **Glycine** 2. Serine (reversibly) Threonine (sometimes) 3. 30% 4. NH4 CO2 one carbon fragment (N5, N10 - Methylene THF 5. Cholic acid - - - - **glycocholic acid** Chenodeoxycholic acid - - - - **glycochenodeoxycholic acid** 6. Detoxify **benzoic acid** (common food preservative) to **hippuric acid**

1. Difference bwtwen creatinine and creatine? Which one is excreted in urine? 2. Which amino acid is precursor for synthesis of heme? 3. Name 3 amino acids for creatine formation? 4. What is Lohmann rxn? Enzyme? 5. Diagbostic test fir kidney function? 6. Glycinuria? 7. Primary hyperoxaluria? Enzyme defecet?

1. Creatinine is an **anhydride** of creatine - **creatinine** - - - - excreted 2. **Glycine** (glycine + succinyl coA - - - - ALA - - - - - heme) 3. GAM Glycine Arginibe Methionine 4. Creatine is reversibly phosphorylated to **phosphocreatine** by **creatin kinase** 5. **Serum creatinine** 6. Normal serum glycine **High amount excreted** - **defective renal absorption** - more **oxalate stone** formation **BUT normal urinary oxalate** 7. **Increased urinary oxalate** - oxalate stones - **oxalosis** (deposition of oxalate stones in tissues) - enzyme defect: **glycine transaminase**

1. Creatinine coefficient? Normal value? 2. Creatinuria? Observed in? 3. Levels of what is elevated in vitamin B6 deficiency? 4. In formation of purine, glycine is utilized at what positions of purine? 5. What type of neurotransmitter is gkycine? And used for synthesis of? 6. The term Garrod's tetrad refers to?

1. "mg of creatinine & creatine excreted per kg bodyweight / day" - value Man - - **24-26 mg/kg** Woman--**20-22 mg/kg** 2. Increased output of creatine in urine -in Muscular dystrophy Diabetes mellitus Hyperthyroidism Starvation 3. Urinary oxalate 4. 4 & 5 of carbon 7 of nitrogen 5. **inhibitory** - heme -purine - creatinine 6. CAPA Cystinuria Alkaptonuria Pentosuria Albinism

1. What is transamination? 2. What is deamination? How do both differ? 3. Aspartate transaminate (AST) is raised in? Serum alanine transaminase (ALT) is elevated in? 4. Only amino acid that undergoes oxidative deamination ti liberate free NH3 for urea synthesis? 5. Which amino acids donot take part in transamination? 6. Protein degradation is facikitated by? (proteins are tagged by? 7. Excretory end product of protein metabolism? -storage form of amino acid? 8. Initiation point for amino acid metabolism?

1. Transfer of amino **(-NH2)** group from and amino acid to a **ketoacid** 2. Transamination - - - only **shuffling of - NH2** group Deamination - - - - **removal of - NH2** group + **liberation of NH3 (ammonia)** 3. **AST**---- **Cardiac** disorder (**Myocardial infarction**) **ALT**----- **Liver** disease (**viral hepatitis**) 4. **glutamate** 5. (let them prove him) **L**ysine **T**hreonine **P**roline **H**ydroxyproline 6. **ubiquitin** (Ubiquinone is Coenzyme Q) 7. Urea - none (unlike carbs & lipids) 8. Transamination

1. All transaminases require what! 2. What is a schiff base? What type of linkage? 3. Ping pong bi bi mechanism for transamination involves? 4. Collection centre for amino groups? 5. What tyoe of amino acids are found in plants & micrognisms? 6. L-amino acid oxidase does not act on? 7. Importance of D-amino acid oxidase?

1. **pyrridoxal phosphate (PLP)** (a Coenzyme derived from vitamin B6) 2. Aldehyde of **PLP** is linked with E-amino group of **lysine** at the active site of enzyme - **imine** linkage 3. Aldimines Ketimines 4. Glutamate 5. **D-amino acids** 6. Glycine & dicarboxylic acid 7. - initiates first step in converting Unnatural D amino acids to L-amino acids

1. Enzyme responsible for oxidative deamination of glutamate to liverate ammonia? Importance of this rxn? 2 glutamate dehydrogenase is a _____ containing enzyme found in? How many subunits? Which hormones inhibits it? 3. How is GDH unique? 4. Conversion of glutamate to a-ketoglutarate occurs thru firmation of an intermediate? 5. Transamination & deamination occur simultaneously involving what central molecule? 6. Name non-oxidative deamination rxns? 7. Name hydroxy amino acids? 8. Adult has abt ______g of free amino acid as amino acid pool? - kidneys fikter how much?

1. **Glutamate dehydrogenase (GDH)** - links glutamate metabolism with **TCA** thru **a-ketoglutarate** 2. **zinc** -mitochondria -6 identical subunits (56,000 each) - inhibitex by: **steroid & thyroid** hormones 3. Can utilize either **NAD+** or **NADP+** as Coenzyme 4. **a-iminoglutarate**. 5. **Glutamate** 6. Amino acid **dehydrases** (serine, homoserine, threonine) Amino acid **desulfhydrases** (cysteine, homocysteine) Deamination of histidine by **histadase** 7. Serine Homoserine Threonine 8. 100g - 50g

1. Rate limiting step in urea synthesis? -enzyme? - consumes how many atp? 2. Urea synthesis occurs in? Also called? 3. 2 amino group of urea are derived from? 4. CPS I requires what for its acrivity? Required for? Present in? Receives amino group from? 5. CPS II is present in? Requires what for its acrivity? Required for? Receives amino group from? 6. Deficiency of what enzyme in: Hyperammonemia type I Hyperammonemia type II Citrullinemia Arginosuccinic aciduria Hyperargininemia 3.

1. Carbamoyl phosphate synthase I **(CPS I)** (NH4+ + CO2------- **carbamoyl phosphate**) - 2 ATP consumed 2. Liver - krebs-hensleit/ornithine cycle 3. 1---- **NH3** 1------**Aspartate** 4. **NAG** N-acetyl glutamate -urea synthesis -mitochondria - **ammonia** 5. Cytosol - does not require NAG -**pyrimidine** synthesis -- **glutamine** (unlike CPS I---ammonia ) 6. Hyperammonemia type I ---- **CPS I** Hyperammonemia type II -----**Ornitine transcarbomyase** Citrullinemia-----**argininosuccinate synthase** Arginosuccinic aciduria -----**arginosuccinase** Hyperargininemia -----**arginase**

1. Immediate precursor for urea? 2. Ornithine & ______ compete with arginine? (competitive inhibitor? 3. ATP produced in TCA cycle ATP consumed in urea synthesis? 4. Kidney renal function by blood urea is estimated by which 2 methods? 5. Uremia vs azotemia? 6. Concentration of non protein nitrogen NPN in blood? Blood urea Nitrogen (BUN)? 7. Normal ammonia concentration?

1. Arginine 2. Lysine 3. TCA----- 10 ATP produced Urea synthesis------ 4 consumed 4. Blood urease **(DAM) Diacetyl Monoaxime** 5. **uremia** - - - increased blood urea due to **renal failure** **azotemia** - - - - increased blood urea/ nitrigen metabolities (**may or may not be** associated with renal disease) 6. **20-40mg** - 28 g 7. 15-45 ug/dl