1. Protein metabolism involves the breakdown of amino acids into ammonia and carbon skeletons, and the reuse of these components for new protein synthesis or energy production. Amino acids undergo transamination, deamination, and are metabolized through the urea cycle to dispose of ammonia.
2. The urea cycle is a series of chemical reactions that converts ammonia into urea for excretion. It occurs primarily in the liver and involves five enzymatic steps to incorporate ammonia and carbon into the relatively non-toxic urea molecule.
3. Defects in protein metabolism can cause inborn errors such as phenylketonuria, maple syrup urine disease, and defects in the urea cycle, which
Protein metabolism denotes the various biochemical processes responsible for the synthesis of proteins and amino acids (anabolism), and the breakdown of proteins by catabolism. ... In humans, non-essential amino acids are synthesized from intermediates in major metabolic pathways such as the Citric Acid Cycle.
Protein metabolism denotes the various biochemical processes responsible for the synthesis of proteins and amino acids (anabolism), and the breakdown of proteins by catabolism. ... In humans, non-essential amino acids are synthesized from intermediates in major metabolic pathways such as the Citric Acid Cycle.
Metabolism of amino acids (general metabolism)Ashok Katta
Metabolism of amino acids (general metabolism).
Part - I of amino acid metabolism.
This presentation covers Transamination, deamination, formation and Transport of Ammoniaand etc.
Digestion of proteins, absorption of amino acids, synthesis of amino acids, catabolism of amino acids and synthesis of specialised non-protein compounds from amino acids for undergraduates
Metabolism of amino acids (general metabolism)Ashok Katta
Metabolism of amino acids (general metabolism).
Part - I of amino acid metabolism.
This presentation covers Transamination, deamination, formation and Transport of Ammoniaand etc.
Digestion of proteins, absorption of amino acids, synthesis of amino acids, catabolism of amino acids and synthesis of specialised non-protein compounds from amino acids for undergraduates
Fate of Glucogenic and Ketogenic amino acid
Amino acid are the currency of of nitrogen and protein economy of the host, hence they are used in many pathways beyond protein synthesis, including energy production and neurotransmitter synthesis.
All amino acid are comprised of an amino group and a carbon skeleton. During metabolism these two parts are separated as they have different ‘fates’
Of the liberated amino acid approximately 75% are utilized while remainder serve as precursors for important biological compound and those not utilized are degraded to amphibolic intermediates
The pathway of amino acid catabolism is quite similar in most organism
Overview of amino acid anabolism and catabolism and fate of ammonia in amino acid metabolism. This is targeted for MBBS, MD, BDS and general Biochemistry students
Protein metabolism is more appropriately learnt as metabolism of Amino acid. The proteins on degradation(proteolysis) release individual amino acids. The amount of free amino acids distributed throught the body is called Amino acid pool. The amino acids undergo certain common reactions like transamination followed by deamination for the liberation of ammonia. The amino group of amino acids utilized for the formation of urea, which is the end product of protein metabolism
This PPT is on Amino acid metabolism. And the topics covered under this ppt are Transamination, deamination
Book referred: https://www.amazon.in/Biochemistry-2019-Satyanarayana-Satyanarayana-Author/dp/B07WGHCTKZ/ref=sr_1_1?dchild=1&qid=1591608419&refinements=p_27%3AU+Satyanarayana&s=books&sr=1-1
Introduction to protein , Structure of Amino acid, Asymmetric carbon, Nomenclature of amino acid, Classification of amino acid, Properties & functions of amino acids, Definition of protein, Peptide bond
Tom Selleck Health: A Comprehensive Look at the Iconic Actor’s Wellness Journeygreendigital
Tom Selleck, an enduring figure in Hollywood. has captivated audiences for decades with his rugged charm, iconic moustache. and memorable roles in television and film. From his breakout role as Thomas Magnum in Magnum P.I. to his current portrayal of Frank Reagan in Blue Bloods. Selleck's career has spanned over 50 years. But beyond his professional achievements. fans have often been curious about Tom Selleck Health. especially as he has aged in the public eye.
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Introduction
Many have been interested in Tom Selleck health. not only because of his enduring presence on screen but also because of the challenges. and lifestyle choices he has faced and made over the years. This article delves into the various aspects of Tom Selleck health. exploring his fitness regimen, diet, mental health. and the challenges he has encountered as he ages. We'll look at how he maintains his well-being. the health issues he has faced, and his approach to ageing .
Early Life and Career
Childhood and Athletic Beginnings
Tom Selleck was born on January 29, 1945, in Detroit, Michigan, and grew up in Sherman Oaks, California. From an early age, he was involved in sports, particularly basketball. which played a significant role in his physical development. His athletic pursuits continued into college. where he attended the University of Southern California (USC) on a basketball scholarship. This early involvement in sports laid a strong foundation for his physical health and disciplined lifestyle.
Transition to Acting
Selleck's transition from an athlete to an actor came with its physical demands. His first significant role in "Magnum P.I." required him to perform various stunts and maintain a fit appearance. This role, which he played from 1980 to 1988. necessitated a rigorous fitness routine to meet the show's demands. setting the stage for his long-term commitment to health and wellness.
Fitness Regimen
Workout Routine
Tom Selleck health and fitness regimen has evolved. adapting to his changing roles and age. During his "Magnum, P.I." days. Selleck's workouts were intense and focused on building and maintaining muscle mass. His routine included weightlifting, cardiovascular exercises. and specific training for the stunts he performed on the show.
Selleck adjusted his fitness routine as he aged to suit his body's needs. Today, his workouts focus on maintaining flexibility, strength, and cardiovascular health. He incorporates low-impact exercises such as swimming, walking, and light weightlifting. This balanced approach helps him stay fit without putting undue strain on his joints and muscles.
Importance of Flexibility and Mobility
In recent years, Selleck has emphasized the importance of flexibility and mobility in his fitness regimen. Understanding the natural decline in muscle mass and joint flexibility with age. he includes stretching and yoga in his routine. These practices help prevent injuries, improve posture, and maintain mobilit
ARTIFICIAL INTELLIGENCE IN HEALTHCARE.pdfAnujkumaranit
Artificial intelligence (AI) refers to the simulation of human intelligence processes by machines, especially computer systems. It encompasses tasks such as learning, reasoning, problem-solving, perception, and language understanding. AI technologies are revolutionizing various fields, from healthcare to finance, by enabling machines to perform tasks that typically require human intelligence.
Anti ulcer drugs and their Advance pharmacology ||
Anti-ulcer drugs are medications used to prevent and treat ulcers in the stomach and upper part of the small intestine (duodenal ulcers). These ulcers are often caused by an imbalance between stomach acid and the mucosal lining, which protects the stomach lining.
||Scope: Overview of various classes of anti-ulcer drugs, their mechanisms of action, indications, side effects, and clinical considerations.
Ozempic: Preoperative Management of Patients on GLP-1 Receptor Agonists Saeid Safari
Preoperative Management of Patients on GLP-1 Receptor Agonists like Ozempic and Semiglutide
ASA GUIDELINE
NYSORA Guideline
2 Case Reports of Gastric Ultrasound
The prostate is an exocrine gland of the male mammalian reproductive system
It is a walnut-sized gland that forms part of the male reproductive system and is located in front of the rectum and just below the urinary bladder
Function is to store and secrete a clear, slightly alkaline fluid that constitutes 10-30% of the volume of the seminal fluid that along with the spermatozoa, constitutes semen
A healthy human prostate measures (4cm-vertical, by 3cm-horizontal, 2cm ant-post ).
It surrounds the urethra just below the urinary bladder. It has anterior, median, posterior and two lateral lobes
It’s work is regulated by androgens which are responsible for male sex characteristics
Generalised disease of the prostate due to hormonal derangement which leads to non malignant enlargement of the gland (increase in the number of epithelial cells and stromal tissue)to cause compression of the urethra leading to symptoms (LUTS
These lecture slides, by Dr Sidra Arshad, offer a quick overview of physiological basis of a normal electrocardiogram.
Learning objectives:
1. Define an electrocardiogram (ECG) and electrocardiography
2. Describe how dipoles generated by the heart produce the waveforms of the ECG
3. Describe the components of a normal electrocardiogram of a typical bipolar leads (limb II)
4. Differentiate between intervals and segments
5. Enlist some common indications for obtaining an ECG
Study Resources:
1. Chapter 11, Guyton and Hall Textbook of Medical Physiology, 14th edition
2. Chapter 9, Human Physiology - From Cells to Systems, Lauralee Sherwood, 9th edition
3. Chapter 29, Ganong’s Review of Medical Physiology, 26th edition
4. Electrocardiogram, StatPearls - https://www.ncbi.nlm.nih.gov/books/NBK549803/
5. ECG in Medical Practice by ABM Abdullah, 4th edition
6. ECG Basics, http://www.nataliescasebook.com/tag/e-c-g-basics
Title: Sense of Smell
Presenter: Dr. Faiza, Assistant Professor of Physiology
Qualifications:
MBBS (Best Graduate, AIMC Lahore)
FCPS Physiology
ICMT, CHPE, DHPE (STMU)
MPH (GC University, Faisalabad)
MBA (Virtual University of Pakistan)
Learning Objectives:
Describe the primary categories of smells and the concept of odor blindness.
Explain the structure and location of the olfactory membrane and mucosa, including the types and roles of cells involved in olfaction.
Describe the pathway and mechanisms of olfactory signal transmission from the olfactory receptors to the brain.
Illustrate the biochemical cascade triggered by odorant binding to olfactory receptors, including the role of G-proteins and second messengers in generating an action potential.
Identify different types of olfactory disorders such as anosmia, hyposmia, hyperosmia, and dysosmia, including their potential causes.
Key Topics:
Olfactory Genes:
3% of the human genome accounts for olfactory genes.
400 genes for odorant receptors.
Olfactory Membrane:
Located in the superior part of the nasal cavity.
Medially: Folds downward along the superior septum.
Laterally: Folds over the superior turbinate and upper surface of the middle turbinate.
Total surface area: 5-10 square centimeters.
Olfactory Mucosa:
Olfactory Cells: Bipolar nerve cells derived from the CNS (100 million), with 4-25 olfactory cilia per cell.
Sustentacular Cells: Produce mucus and maintain ionic and molecular environment.
Basal Cells: Replace worn-out olfactory cells with an average lifespan of 1-2 months.
Bowman’s Gland: Secretes mucus.
Stimulation of Olfactory Cells:
Odorant dissolves in mucus and attaches to receptors on olfactory cilia.
Involves a cascade effect through G-proteins and second messengers, leading to depolarization and action potential generation in the olfactory nerve.
Quality of a Good Odorant:
Small (3-20 Carbon atoms), volatile, water-soluble, and lipid-soluble.
Facilitated by odorant-binding proteins in mucus.
Membrane Potential and Action Potential:
Resting membrane potential: -55mV.
Action potential frequency in the olfactory nerve increases with odorant strength.
Adaptation Towards the Sense of Smell:
Rapid adaptation within the first second, with further slow adaptation.
Psychological adaptation greater than receptor adaptation, involving feedback inhibition from the central nervous system.
Primary Sensations of Smell:
Camphoraceous, Musky, Floral, Pepperminty, Ethereal, Pungent, Putrid.
Odor Detection Threshold:
Examples: Hydrogen sulfide (0.0005 ppm), Methyl-mercaptan (0.002 ppm).
Some toxic substances are odorless at lethal concentrations.
Characteristics of Smell:
Odor blindness for single substances due to lack of appropriate receptor protein.
Behavioral and emotional influences of smell.
Transmission of Olfactory Signals:
From olfactory cells to glomeruli in the olfactory bulb, involving lateral inhibition.
Primitive, less old, and new olfactory systems with different path
Pulmonary Thromboembolism - etilogy, types, medical- Surgical and nursing man...VarunMahajani
Disruption of blood supply to lung alveoli due to blockage of one or more pulmonary blood vessels is called as Pulmonary thromboembolism. In this presentation we will discuss its causes, types and its management in depth.
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New Directions in Targeted Therapeutic Approaches for Older Adults With Mantl...i3 Health
i3 Health is pleased to make the speaker slides from this activity available for use as a non-accredited self-study or teaching resource.
This slide deck presented by Dr. Kami Maddocks, Professor-Clinical in the Division of Hematology and
Associate Division Director for Ambulatory Operations
The Ohio State University Comprehensive Cancer Center, will provide insight into new directions in targeted therapeutic approaches for older adults with mantle cell lymphoma.
STATEMENT OF NEED
Mantle cell lymphoma (MCL) is a rare, aggressive B-cell non-Hodgkin lymphoma (NHL) accounting for 5% to 7% of all lymphomas. Its prognosis ranges from indolent disease that does not require treatment for years to very aggressive disease, which is associated with poor survival (Silkenstedt et al, 2021). Typically, MCL is diagnosed at advanced stage and in older patients who cannot tolerate intensive therapy (NCCN, 2022). Although recent advances have slightly increased remission rates, recurrence and relapse remain very common, leading to a median overall survival between 3 and 6 years (LLS, 2021). Though there are several effective options, progress is still needed towards establishing an accepted frontline approach for MCL (Castellino et al, 2022). Treatment selection and management of MCL are complicated by the heterogeneity of prognosis, advanced age and comorbidities of patients, and lack of an established standard approach for treatment, making it vital that clinicians be familiar with the latest research and advances in this area. In this activity chaired by Michael Wang, MD, Professor in the Department of Lymphoma & Myeloma at MD Anderson Cancer Center, expert faculty will discuss prognostic factors informing treatment, the promising results of recent trials in new therapeutic approaches, and the implications of treatment resistance in therapeutic selection for MCL.
Target Audience
Hematology/oncology fellows, attending faculty, and other health care professionals involved in the treatment of patients with mantle cell lymphoma (MCL).
Learning Objectives
1.) Identify clinical and biological prognostic factors that can guide treatment decision making for older adults with MCL
2.) Evaluate emerging data on targeted therapeutic approaches for treatment-naive and relapsed/refractory MCL and their applicability to older adults
3.) Assess mechanisms of resistance to targeted therapies for MCL and their implications for treatment selection
Ethanol (CH3CH2OH), or beverage alcohol, is a two-carbon alcohol
that is rapidly distributed in the body and brain. Ethanol alters many
neurochemical systems and has rewarding and addictive properties. It
is the oldest recreational drug and likely contributes to more morbidity,
mortality, and public health costs than all illicit drugs combined. The
5th edition of the Diagnostic and Statistical Manual of Mental Disorders
(DSM-5) integrates alcohol abuse and alcohol dependence into a single
disorder called alcohol use disorder (AUD), with mild, moderate,
and severe subclassifications (American Psychiatric Association, 2013).
In the DSM-5, all types of substance abuse and dependence have been
combined into a single substance use disorder (SUD) on a continuum
from mild to severe. A diagnosis of AUD requires that at least two of
the 11 DSM-5 behaviors be present within a 12-month period (mild
AUD: 2–3 criteria; moderate AUD: 4–5 criteria; severe AUD: 6–11 criteria).
The four main behavioral effects of AUD are impaired control over
drinking, negative social consequences, risky use, and altered physiological
effects (tolerance, withdrawal). This chapter presents an overview
of the prevalence and harmful consequences of AUD in the U.S.,
the systemic nature of the disease, neurocircuitry and stages of AUD,
comorbidities, fetal alcohol spectrum disorders, genetic risk factors, and
pharmacotherapies for AUD.
2. AMINO ACIDS
Any molecule that contains the amino and
carboxylic acid functional groups.
Or
Organic acids containing amino groups
are known as amino acids.
3. STRUCTURE OF AMINO ACID
A central carbon atom to which 4 diff groups
of atoms are attached:
An Amino group (NH2)
A Carboxylic acid group (COOH)
A Hydrogen atom (H)
A Radical or R group: H, CH3, CH3-CH2 etc.
4. CONTD
The acidic and basic properties of NH2 &
COOH groups make the AA molecule
“Amphoteric”
5. FATE OF ABSORBED AMINO ACIDS
Anabolic fates:
Synthesis of:
Tissue protein
(structural/enzyme/hormone)
NPN subs
FA, ketone bodies, Steroids (via
acetyl co A, end product of catabolism
of AA C skeleton)
Glucose/glycogen (via pyruvate & TCA
cycle intermediates).
6. CONTD.
Catabolic fates:
Through transamination and deamination,
each AA produces NH3 & their
corresponding C-skeleton (α-keto acid).
NH3 is converted to urea via urea cycle in
liver & then excreted with urine.
7. CONTD.
C-skeleton is catabolized to –
1. Pyruvate & TCA cycle intermediates (if
glucogenic AA)
2. Acetyl co A /Aceto acetyl co A ( if
ketogenic AA)
3. CO2, H2O & ATP through oxidation in
TCA cycle.
8. PROTEIN TURNOVER
It is the rate at which proteins are
constantly being degraded & again
resynthesized. It is 150-300gm/D (i.e.1-
2% of total body protein) in adult.
[Total body protein in 70kg adult is 12-
14kg]
9. CONTD
If a cell takes up as much AA as it loses, it is
in a state of dynamic equilibrium.
If the loss is greater, the cell wastes & if the
gain is greater, the cell grows.
Not only the proteins, practically, all the
materials in the body, even the depot fat, are
in a state of dynamic equilibrium.
10. AMINO ACID POOL
It is the free amino acid content
distributed throughout the
extracellular fluid/body.
Quantitatively, it is about 100 gm in an
adult individual . Plasma AA level
varies throughout the day fm 4-
8mg/dl.
11. CONTD
It is constantly undergoing depletion
due to disposal of AA through diff
metabolic processes usually at a rate
equal to the rate by which AA feeds
the pool.
It is always being reestablished by AA
coming from three sources- dietary
protein, endogenous AA synthesis &
endogenous protein break down.
12.
13. SOURCES OF AA IN AA POOL
1. Dietary protein
2. break down of tissue proteins
3. biosynthesis of NEAAs.
14. FATE OF AA IN AA POOL
Biosynthesis of :
structural protein, e.g. tissue proteins
Functional proteins, e.g. Hb,
myoglobin, enz, protein hormones.
Small peptides of biological
importance, e.g. glutathione, endorphins
& encephalin.
NPN subs, e.g. urea, uric acid,
creatinine, ammonia.
Catabolism of AA to give α-keto acids &
ammonia.
15. INTERMEDIARY METABOLISM OF
AMINO ACIDS
Protein synthesis & synthesis of NPN
substance
Transamination & Deamination
Urea cycle
Catabolism of AA C-skeleton &
synthesis of glucose, FA, steroids,
ketone bodies, etc.
Oxidation of AA C-skeleton via TCA
cycle
16. NITROGEN BALANCE
It is the diff b/w N-intake & N-
loss/excretion
N-intake occurs in the form of
protein/AA
N-excretion occurs through urine,
sweat & stool
17. CONTD
3 types :
N-equilibrium: seen in normal
individual, where intake equals to
excretion.
Positive N balance: seen during
growth, pregnancy, etc , where intake
is more than loss.
Negative N balance: seen in DM, TB,
malignancy, surgery, starvation,
trauma, etc, where loss is more than
intake.
18. 1. TRANSAMINATION
It is the transfer of amino group from
an AA to a keto acid with
simultaneous production of a
corresponding keto acid & AA
respectively.
Site: cytoplasm of liver, kidney, heart,
sk. Muscle, brain.
19. CONTD
All AAs except Lys, Thr & Pro undergo
transamination.
Usually 3 keto acids mostly participate
in transamination. These are α-KG (keto
acid of Glu), OA ( keto acid of Asp),
pyruvate (keto acid of Ala).
All reactions are reversible & are
catalyzed by aminotransferases
/transaminases. It needs pyridoxal PO4
as co-enzyme.
21. ROLE OF PYRIDOXAL PO4 IN
TRANSAMINATION
It acts as an intermediate carrier of an
NH2 group. It accepts the -NH2 group
from AA to form pyridoxamine PO4 ,
which in turn gives the -NH2 group to
α-keto acid.
23. IMPORTANCE OF TRANSAMINATION
Funneling of NH2 group of diff AAs
ultimately to α-KG to form Glu & Glu is
the major AA that undergoes oxidative
deamination to liberate free NH3,
which is converted to urea.
Biosynthesis of NEAA by adding NH2
group to their corresponding keto
acid (C-skeleton), thus equalize the
quantities of NEAA.
24. CONTD
Formation of C-skeleton (keto acid) of
AAs that later on can be
catabolized/oxidized.
Provides a link b/w carbohydrate,
protein & fat metabolism, since the
keto acids generated by
transamination of AA can form
compounds common to their
metabolic cycle.
25. 2. DEAMINATION
Deamination means removal of –NH2
group from an AA in the form of NH3
with simultaneous formation of its
corresponding keto acid.
Mitochondria of Liver and kidney are
the main site of deamination. It also
may occur in heart, sk. Muscle etc.
It may be oxidative/non-oxidative.
26. A) OXIDATIVE DEAMINATION
An oxidation (dehydrogenation)
process, where an amino acid is
converted into the corresponding keto
acid by the removal of the amine
functional group as ammonia .The
ammonia eventually goes into the urea
cycle.
It is catalyzed by one of the following
enzymes:
L-AA oxidase / D-AA oxidase /Glu DH.
28. CONTD
Oxidative deamination occurs
primarily on Glu because Glu is the
end product of many transamination
reactions.
If this is true, then how are the other
amino acids deaminated? The answer
is that a combination of
transamination and deamination of
Glu occurs which is a recycling type
of reaction for Glu. The original amino
acid loses its amine group in the
process.
29. B) NON-OXIDATIVE DEAMINATION
-NH2 groups of serine, homoserine,
threonine, etc are removed non-
oxidatively by a group of
dehydratases to release ultimately
NH3 & corresponding keto acids.
It is catalyzed by one of the following
enzymes: dehydratases or
Desulfhydrases.
30. DIFF B/W TRANS DEAMINATION
Transamination Oxidative deamination
It is the transfer of amino
group from an AA to a keto
acid with simultaneous
production of a
corresponding keto acid &
AA respectively.
Reactions are catalyzed
by aminotransferases
/transaminases. It needs
pyridoxal PO4 as co-
enzyme.
An oxidation
(dehydrogenation) process,
where an amino acid is
converted into the
corresponding keto acid by
the removal of the amine
functional group as
ammonia .
It is catalyzed by L-AA
oxidase / D-AA oxidase /Glu
DH.
31. DIFF B/W TRANS DEAMINATION
Transamination Oxidative deamination
The most usual and major
keto acid involved with
transamination reactions is
α-KG, an intermediate in the
citric acid cycle.
A specific example is the
transamination of alanine to
make pyruvic acid and
glutamic acid.
Oxidative deamination
occurs primarily on
glutamic acid because
glutamic acid was the end
product of many
transamination reactions.
A specific example is the
deamination of glutamic
acid to make NH3 and α-KG
32.
33. METABOLISM OF AMMONIA
Source:
1. Deamination of amino acids
2. Glutamine by glutaminase enzyme
in kidney.
3. Catabolism of purine & pyrimidine
4. Bacterial degradation of urea in to
NH3 in intestinal lumen (action of
bacterial urease).
34. CONTD
Disposal of NH3:
1. formation of urea through urea cycle and
its excretion with urine.
2. Excretion of NH3 with urine as NH4+.
3. Formation of glutamate in liver. (NH3 is
added with α-KG to form glutamate).
4. Formation of glutamine in liver, kidney,
muscle, brain. (Glutamine is the temporary
non-toxic storage & transport form of NH3.
NH3 is added with glutamate to form
glutamine).
35. NH3 INTOXICATION (HEPATIC
ENCEPHALOPATHY)
Toxicity resulting from
hyperammonemia. (Normal P/NH3
conc. 10-80 µg/dl or 5-50 µmol/L)
Occurs due to hepatic dysfunction
leading to impairment of urea cycle
and/or deficiency of urea cycle
enzymes.
36. CONTD
Brain tissue is mostly affected & there
is reduced cerebral activity. In neuron,
excess NH3 converts α-KG to Glu,
then to Glutamine. This causes rapid ↓
of α-KG, leading to suppression of
TCA cycle. There is ATP depletion ,
ultimately producing s/s like tremor,
slurring of speech, blurring of vision,
coma, death.
37. 3. UREA CYCLE
The urea cycle (Ornithine cycle) is a
cycle of biochemical reactions
occurring in many animals that
produces urea ((NH 2)2CO) from
ammonia (NH3 )
It occurs in liver
Consists of five reactions: two
mitochondrial and three cytosolic
38. 3. UREA CYCLE
The cycle converts two amino groups
(one from NH4
+ and one from Asp) and
a carbon atom (from HCO3
−) to the
relatively nontoxic excretion product ,
urea at the cost of four "high-energy"
phosphate bonds (3 ATP hydrolyzed
to 2 ADP and one AMP)
Ornithine is the carrier of these
carbon and nitrogen atoms.
39. Step Reactants Products Catalyzed by Location
1 NH4
+ + HCO3
− + 2ATP
carbamoyl
phosphate +
2ADP+ Pi
CPS1
(carbamoyl
PO4 synthase
1)
mitochondri
a
2 carbamoyl phosphate
+ Ornithine
Citruline + Pi OTC (ornithine
transcarbamy-
lase)
mitochondri
a
3 citrulline + aspartate +
ATP
Arginosuccin
-ate+AMP+
PPi
ASS
(arginosuccinat
e synthetase)
cytosol
4
arginosuccinate
Arg+
fumarate
ASL (AS lyase) cytosol
5 Arg +H2O Ornithine+
urea
ARG1 (arginase
1)
cytosol
40.
41. INBORN ERROR OF PROTEIN
METABOLISM
Alkaptonuria
Homocystinuria
Phenylketonuria
Albinism
Maple syrup urine disease
Hyperhomocysteinemia
Defects in urea cycle