The document discusses the biosynthesis of amino acids. It notes that all 20 standard amino acids are derived from intermediates in glycolysis, the citric acid cycle, or the pentose phosphate pathway, with nitrogen entering via glutamate and glutamine. The pathways range from simple one-step processes to more complex multi-step pathways, especially for aromatic amino acids. While bacteria and plants can synthesize all 20, mammals can only synthesize around half and must obtain the rest from food. The pathways are largely irreversible to ensure a continuous supply of amino acids.
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
Biosynthesis of different types of amino acids.pptxlaija s. nair
Amino acids are the building blocks of proteins, playing a crucial role in various biological processes. They are categorized into essential and non-essential amino acids based on the body's ability to synthesize them. While essential amino acids must be obtained through the diet, non-essential amino acids can be synthesized by the body.
General Pathway of Amino Acid Biosynthesis:
Amino acid biosynthesis involves complex metabolic pathways that differ for each amino acid. However, a general overview can be provided:
Carbon Skeleton Formation:
Amino acids are composed of a central carbon atom (alpha carbon) bonded to a hydrogen atom, an amino group (NH2), a carboxyl group (COOH), and a side chain (R group) specific to each amino acid.
The carbon skeletons of amino acids are derived from intermediates of glycolysis, citric acid cycle, and pentose phosphate pathway.
Transamination:
A crucial step in amino acid biosynthesis is the transamination reaction, where an amino group is transferred from an amino acid donor to an alpha-keto acid acceptor.
This reaction is catalyzed by aminotransferases or transaminases, and pyridoxal phosphate (PLP) acts as a cofactor.
Specific Pathways for Essential Amino Acids:
Essential amino acids, which cannot be synthesized de novo by the body, have specific biosynthetic pathways.
For example, lysine and methionine biosynthesis involve the aspartate family pathway, while valine, leucine, and isoleucine biosynthesis occur through the branched-chain amino acid (BCAA) pathway.
Non-Essential Amino Acid Biosynthesis:
Non-essential amino acids can be synthesized by the body through various pathways.
For instance, glutamate serves as a precursor for the synthesis of several amino acids, including proline, arginine, and ornithine.
Specific Amino Acid Biosynthesis Pathways:
Serine and Glycine Biosynthesis:
Serine is derived from 3-phosphoglycerate and can be converted to glycine.
The enzyme serine hydroxymethyltransferase plays a key role in interconverting serine and glycine.
Histidine Biosynthesis:
Histidine biosynthesis involves a unique pathway that starts with phosphoribosyl pyrophosphate (PRPP) and includes several enzymatic steps.
Tyrosine and Phenylalanine Biosynthesis:
The shikimate pathway is essential for the biosynthesis of aromatic amino acids, including tyrosine and phenylalanine.
Chorismate is a key intermediate in this pathway.
Arginine Biosynthesis:
Arginine biosynthesis involves the urea cycle and the ornithine biosynthetic pathway.
Citrulline serves as a key intermediate in these processes.
Proline Biosynthesis:
Proline is derived from glutamate through a two-step reduction process involving pyrroline-5-carboxylate (P5C).
Regulation of Amino Acid Biosynthesis:
Amino acid biosynthesis is tightly regulated to maintain a balance between the body's requirements and energy conservation.
Feedback inhibition and genetic regulation play key roles in controlling the activity of enzymes involved in these p
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
Biosynthesis of different types of amino acids.pptxlaija s. nair
Amino acids are the building blocks of proteins, playing a crucial role in various biological processes. They are categorized into essential and non-essential amino acids based on the body's ability to synthesize them. While essential amino acids must be obtained through the diet, non-essential amino acids can be synthesized by the body.
General Pathway of Amino Acid Biosynthesis:
Amino acid biosynthesis involves complex metabolic pathways that differ for each amino acid. However, a general overview can be provided:
Carbon Skeleton Formation:
Amino acids are composed of a central carbon atom (alpha carbon) bonded to a hydrogen atom, an amino group (NH2), a carboxyl group (COOH), and a side chain (R group) specific to each amino acid.
The carbon skeletons of amino acids are derived from intermediates of glycolysis, citric acid cycle, and pentose phosphate pathway.
Transamination:
A crucial step in amino acid biosynthesis is the transamination reaction, where an amino group is transferred from an amino acid donor to an alpha-keto acid acceptor.
This reaction is catalyzed by aminotransferases or transaminases, and pyridoxal phosphate (PLP) acts as a cofactor.
Specific Pathways for Essential Amino Acids:
Essential amino acids, which cannot be synthesized de novo by the body, have specific biosynthetic pathways.
For example, lysine and methionine biosynthesis involve the aspartate family pathway, while valine, leucine, and isoleucine biosynthesis occur through the branched-chain amino acid (BCAA) pathway.
Non-Essential Amino Acid Biosynthesis:
Non-essential amino acids can be synthesized by the body through various pathways.
For instance, glutamate serves as a precursor for the synthesis of several amino acids, including proline, arginine, and ornithine.
Specific Amino Acid Biosynthesis Pathways:
Serine and Glycine Biosynthesis:
Serine is derived from 3-phosphoglycerate and can be converted to glycine.
The enzyme serine hydroxymethyltransferase plays a key role in interconverting serine and glycine.
Histidine Biosynthesis:
Histidine biosynthesis involves a unique pathway that starts with phosphoribosyl pyrophosphate (PRPP) and includes several enzymatic steps.
Tyrosine and Phenylalanine Biosynthesis:
The shikimate pathway is essential for the biosynthesis of aromatic amino acids, including tyrosine and phenylalanine.
Chorismate is a key intermediate in this pathway.
Arginine Biosynthesis:
Arginine biosynthesis involves the urea cycle and the ornithine biosynthetic pathway.
Citrulline serves as a key intermediate in these processes.
Proline Biosynthesis:
Proline is derived from glutamate through a two-step reduction process involving pyrroline-5-carboxylate (P5C).
Regulation of Amino Acid Biosynthesis:
Amino acid biosynthesis is tightly regulated to maintain a balance between the body's requirements and energy conservation.
Feedback inhibition and genetic regulation play key roles in controlling the activity of enzymes involved in these p
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
Protein is a macronutrient that is essential to building muscle mass. It is commonly found in animal products, though is also present in other sources, such as nuts and legumes. There are three macronutrients: protein, fats and carbohydrates. Macronutrients provide calories, or energy.
in this slide u are able to well known about the introduction of hormones.
categories, classification, function, structure, regulation, location, mechanism of action, how hormone regulates our body function, how it maintains the homeostasis condition.
structure of hormones.
these clearance test plays an very important role in determining the functioning capacity and working status of kidney.
and we estimate how amount of compund is excreted in the urine and absorption too.
and i also attached the mathematical caluculation to identify the metabolic valuve of urea, creatinine, inulin clearance by kidney.
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
Protein is a macronutrient that is essential to building muscle mass. It is commonly found in animal products, though is also present in other sources, such as nuts and legumes. There are three macronutrients: protein, fats and carbohydrates. Macronutrients provide calories, or energy.
in this slide u are able to well known about the introduction of hormones.
categories, classification, function, structure, regulation, location, mechanism of action, how hormone regulates our body function, how it maintains the homeostasis condition.
structure of hormones.
these clearance test plays an very important role in determining the functioning capacity and working status of kidney.
and we estimate how amount of compund is excreted in the urine and absorption too.
and i also attached the mathematical caluculation to identify the metabolic valuve of urea, creatinine, inulin clearance by kidney.
its the introduction about kidney function, glomerular filtrate, tubular reabsorption mechanism, in this slide u may able to clearly know about the basics.
if you want to know about the basic property of kisney nephron it is very easy yo obxerve
Multi-source connectivity as the driver of solar wind variability in the heli...Sérgio Sacani
The ambient solar wind that flls the heliosphere originates from multiple
sources in the solar corona and is highly structured. It is often described
as high-speed, relatively homogeneous, plasma streams from coronal
holes and slow-speed, highly variable, streams whose source regions are
under debate. A key goal of ESA/NASA’s Solar Orbiter mission is to identify
solar wind sources and understand what drives the complexity seen in the
heliosphere. By combining magnetic feld modelling and spectroscopic
techniques with high-resolution observations and measurements, we show
that the solar wind variability detected in situ by Solar Orbiter in March
2022 is driven by spatio-temporal changes in the magnetic connectivity to
multiple sources in the solar atmosphere. The magnetic feld footpoints
connected to the spacecraft moved from the boundaries of a coronal hole
to one active region (12961) and then across to another region (12957). This
is refected in the in situ measurements, which show the transition from fast
to highly Alfvénic then to slow solar wind that is disrupted by the arrival of
a coronal mass ejection. Our results describe solar wind variability at 0.5 au
but are applicable to near-Earth observatories.
A brief information about the SCOP protein database used in bioinformatics.
The Structural Classification of Proteins (SCOP) database is a comprehensive and authoritative resource for the structural and evolutionary relationships of proteins. It provides a detailed and curated classification of protein structures, grouping them into families, superfamilies, and folds based on their structural and sequence similarities.
Slide 1: Title Slide
Extrachromosomal Inheritance
Slide 2: Introduction to Extrachromosomal Inheritance
Definition: Extrachromosomal inheritance refers to the transmission of genetic material that is not found within the nucleus.
Key Components: Involves genes located in mitochondria, chloroplasts, and plasmids.
Slide 3: Mitochondrial Inheritance
Mitochondria: Organelles responsible for energy production.
Mitochondrial DNA (mtDNA): Circular DNA molecule found in mitochondria.
Inheritance Pattern: Maternally inherited, meaning it is passed from mothers to all their offspring.
Diseases: Examples include Leber’s hereditary optic neuropathy (LHON) and mitochondrial myopathy.
Slide 4: Chloroplast Inheritance
Chloroplasts: Organelles responsible for photosynthesis in plants.
Chloroplast DNA (cpDNA): Circular DNA molecule found in chloroplasts.
Inheritance Pattern: Often maternally inherited in most plants, but can vary in some species.
Examples: Variegation in plants, where leaf color patterns are determined by chloroplast DNA.
Slide 5: Plasmid Inheritance
Plasmids: Small, circular DNA molecules found in bacteria and some eukaryotes.
Features: Can carry antibiotic resistance genes and can be transferred between cells through processes like conjugation.
Significance: Important in biotechnology for gene cloning and genetic engineering.
Slide 6: Mechanisms of Extrachromosomal Inheritance
Non-Mendelian Patterns: Do not follow Mendel’s laws of inheritance.
Cytoplasmic Segregation: During cell division, organelles like mitochondria and chloroplasts are randomly distributed to daughter cells.
Heteroplasmy: Presence of more than one type of organellar genome within a cell, leading to variation in expression.
Slide 7: Examples of Extrachromosomal Inheritance
Four O’clock Plant (Mirabilis jalapa): Shows variegated leaves due to different cpDNA in leaf cells.
Petite Mutants in Yeast: Result from mutations in mitochondrial DNA affecting respiration.
Slide 8: Importance of Extrachromosomal Inheritance
Evolution: Provides insight into the evolution of eukaryotic cells.
Medicine: Understanding mitochondrial inheritance helps in diagnosing and treating mitochondrial diseases.
Agriculture: Chloroplast inheritance can be used in plant breeding and genetic modification.
Slide 9: Recent Research and Advances
Gene Editing: Techniques like CRISPR-Cas9 are being used to edit mitochondrial and chloroplast DNA.
Therapies: Development of mitochondrial replacement therapy (MRT) for preventing mitochondrial diseases.
Slide 10: Conclusion
Summary: Extrachromosomal inheritance involves the transmission of genetic material outside the nucleus and plays a crucial role in genetics, medicine, and biotechnology.
Future Directions: Continued research and technological advancements hold promise for new treatments and applications.
Slide 11: Questions and Discussion
Invite Audience: Open the floor for any questions or further discussion on the topic.
Nutraceutical market, scope and growth: Herbal drug technologyLokesh Patil
As consumer awareness of health and wellness rises, the nutraceutical market—which includes goods like functional meals, drinks, and dietary supplements that provide health advantages beyond basic nutrition—is growing significantly. As healthcare expenses rise, the population ages, and people want natural and preventative health solutions more and more, this industry is increasing quickly. Further driving market expansion are product formulation innovations and the use of cutting-edge technology for customized nutrition. With its worldwide reach, the nutraceutical industry is expected to keep growing and provide significant chances for research and investment in a number of categories, including vitamins, minerals, probiotics, and herbal supplements.
What is greenhouse gasses and how many gasses are there to affect the Earth.moosaasad1975
What are greenhouse gasses how they affect the earth and its environment what is the future of the environment and earth how the weather and the climate effects.
Richard's entangled aventures in wonderlandRichard Gill
Since the loophole-free Bell experiments of 2020 and the Nobel prizes in physics of 2022, critics of Bell's work have retreated to the fortress of super-determinism. Now, super-determinism is a derogatory word - it just means "determinism". Palmer, Hance and Hossenfelder argue that quantum mechanics and determinism are not incompatible, using a sophisticated mathematical construction based on a subtle thinning of allowed states and measurements in quantum mechanics, such that what is left appears to make Bell's argument fail, without altering the empirical predictions of quantum mechanics. I think however that it is a smoke screen, and the slogan "lost in math" comes to my mind. I will discuss some other recent disproofs of Bell's theorem using the language of causality based on causal graphs. Causal thinking is also central to law and justice. I will mention surprising connections to my work on serial killer nurse cases, in particular the Dutch case of Lucia de Berk and the current UK case of Lucy Letby.
Earliest Galaxies in the JADES Origins Field: Luminosity Function and Cosmic ...Sérgio Sacani
We characterize the earliest galaxy population in the JADES Origins Field (JOF), the deepest
imaging field observed with JWST. We make use of the ancillary Hubble optical images (5 filters
spanning 0.4−0.9µm) and novel JWST images with 14 filters spanning 0.8−5µm, including 7 mediumband filters, and reaching total exposure times of up to 46 hours per filter. We combine all our data
at > 2.3µm to construct an ultradeep image, reaching as deep as ≈ 31.4 AB mag in the stack and
30.3-31.0 AB mag (5σ, r = 0.1” circular aperture) in individual filters. We measure photometric
redshifts and use robust selection criteria to identify a sample of eight galaxy candidates at redshifts
z = 11.5 − 15. These objects show compact half-light radii of R1/2 ∼ 50 − 200pc, stellar masses of
M⋆ ∼ 107−108M⊙, and star-formation rates of SFR ∼ 0.1−1 M⊙ yr−1
. Our search finds no candidates
at 15 < z < 20, placing upper limits at these redshifts. We develop a forward modeling approach to
infer the properties of the evolving luminosity function without binning in redshift or luminosity that
marginalizes over the photometric redshift uncertainty of our candidate galaxies and incorporates the
impact of non-detections. We find a z = 12 luminosity function in good agreement with prior results,
and that the luminosity function normalization and UV luminosity density decline by a factor of ∼ 2.5
from z = 12 to z = 14. We discuss the possible implications of our results in the context of theoretical
models for evolution of the dark matter halo mass function.
3. 24-05-2022 3
BIOSYNTHESIS OF AMINO ACIDS:
All the 20 protein amino acids are derived from intermediates in glycolysis, citric acid cycle or the
pentose phosphate pathway. Nitrogen enters these pathways by way of glutamate and glutamine.
The pathways for 10 amino acids are simple and are only one or a few enzymatic steps removed
from their precursors, whereas the pathways for others (such as aromatic amino acids) are more
complex.
Different organisms have varied capacity to synthesize these 20 amino acids. Whereas most
bacteria and plants can synthesize all the 20 amino acids, mammals including man can
synthesize only about half of them. These are termed as nonessential amino acids and the
remaining ones, which must be obtained from food, as the essential amino acids.
Most pathways are essentially irreversible (i.e., they proceed with a substantial loss of free
energy) and as such a continuous supply of all the amino acids is ensured.
5. 24-05-2022 5
Glutamate:
Reductive amidation of α-ketoglutarate is catalyzed by
glutamate dehydrogenase. This reaction constitutes the first step in
biosynthesis of the “glutamate family” of amino acids.
Synthesis of Amino Acids of a-ketoglutarate Precursor Family:
Glutamine:
The amidation of glutamate to glutamine catalyzed by glutamine
synthetase involves the intermediate formation of γglutamyl phosphate.
Following the ordered binding of glutamate and ATP, glutamate attacks
the γ-phosphorus of ATP, forming γ-glutamyl phosphate and ADP.
NH4+ then binds, and as NH3, attacks γ-glutamyl phosphate to form a
tetrahedral intermediate.
Release of Pi and of a proton from the γ-amino group of the tetrahedral
intermediate then facilitates release of the product, glutamine
6. 24-05-2022 6
PROLINE:
The synthesis of proline, a cyclized
derivative of glutamate is depicted in tis
picture.
In the first reaction, the γ-carboxyl
group of glutamate is phosphorylated
using ATP to form an acylphosphate,
which is then reduced by NADPH to
form glutamate γ -semialdehyde.
This intermediate ultimately undergoes
cyclization and further reduction to
form proline
7. 24-05-2022 7
Arginine:
Arginine is synthesized from glutamate via ornithine
and the urea cycle.
Ornithine could also be synthesized from glutamate γ-
semialdehyde by transamination but cyclization of the
semialdehyde in the proline pathway is a rapid
spontaneous reaction so that only a little amount of
this intermediate is left for ornithine synthesis.
The biosynthetic pathway for ornithine therefore
parallels some steps of the proline pathway but
includes 2 additional steps to chemically block the
amino group of glutamate γ-semialdehyde and prevent
cyclization.
8. 24-05-2022 8
2)Synthesis of Amino Acids of 3- phosphoglycerate
Precursor Family
SERINE:
Serine is the precursor of glycine and cysteine. The 2-
carbon glycine is produced from its precursor 3-carbon
amino acid serine through removal of its side chain β
carbon atom by serine hydroxymethyl transferase
In the first step, the hydroxyl group of 3-
phosphoglycerate is oxidized by NAD+ to produce an 3-
phosphohydroxypyruvate.
This is the committed step in the serine biosynthetic
pathway and is catalyzed by the enzyme 3-
phosphoglycerate dehydrogenase .
Transamination of 3-phosphohydroxypyruvate (an α-keto
acid) from glutamate produces 3-phosphoserine, which
upon hydrolysis by phosphoserine phosphatase yields free
serine
9. 24-05-2022 9
GLYCINE:
Serine is the precursor of glycine and cysteine. The 2-
carbon glycine is produced from its precursor 3- carbon
amino acid serine through removal of its side chain β
carbon atom by serine hydroxymethyl transferase .
CYSTEINE:
In mammals, cysteine is produced from two other amino
acids, namely Met which provides the sulfur atom and
Ser which furnishes the carbon atom.
10. 24-05-2022 10
3) Synthesis of Amino Acids of Oxaloacetate and Pyruvate Precursor Families
Alanine and aspartate are synthesized from pyruvate and oxaloacetate respectively, by transamination from
glutamate. Asparagine is then synthesized by amidation of aspartate; the NH4 + being donated by glutamine.
These are all nonessential amino acids and their simple biosynthesis occurs in all organisms.
The biosynthetic pathways for the 6 of the essential amino acids, viz., methionine, threonine, lysine,
isoleucine, valine and leucine, are complex and interlinked.
Aspartate gives rise to lysine, methionine and threonine. Branch points occur at aspartate β-semialdehyde, an
intermediate in all three pathways and at homoserine, a precursor of methionine and threonine.
Threonine, in turn, is one of the precursors of isoleucine. The isoleucine and valine pathways have 4
common enzymes. These two pathways begin with the condensation of 2 carbons of pyruvate with either
another mole of pyruvate (valine pathway) or with α-ketobutyrate (isoleucine path).
The α-ketobutyrate is derived from threonine in a reaction that requires pyridoxal phosphate (PLP). The α -
ketoisovalerate, an intermediate in the valine pathway, is the starting point for a 4-step branch pathway which
leads to the production of leucine.
18. 24-05-2022 18
An aromatic amino acid is an amino acid that contains an aromatic ring.
Among the 20 standard amino acids, the following are aromatic:
• Phenylalanine,
• Tryptophan
• Tyrosine
In addition, while histidine contains an aromatic ring,
its basic properties cause it to be predominantly classified
as a polar amino acid; however, the compound is still
aromatic.
histidine
19. 24-05-2022 19
• The biosynthesis of tryptophan, tyrosine and phenylalanine takes place by pathways that share a
number of early steps.
• The first 4 steps lead to the production of shikimate whose 7 carbon atoms are derived from
phosphoenolpyruvate and erythrose-4- phosphate.
• Shikimate is then converted to chorismate through 3 more steps that include the addition of 3 more
carbon atoms from another molecule of phosphoenolpyruvate .
• Chorismate is the first branch point, with one branch leading to tryptophan and the other to
tyrosine and phenylalanine through prephenate, the other branch point.
22. 24-05-2022 22
Tryptophan is synthesized from chorismate in a 5-step process .
Chorismate acquires an amino group from the side chain of glutamine and releases pyruvate to
form anthranilate.
Anthranilate then undergoes condensation with phosphoribosyl pyrophosphate (PRPP), an
activated form of ribose phosphate.
The C-1 atom of ribose 5-phosphate becomes bonded to the nitrogen atom of anthranilate in a
reaction that is driven by the hydrolysis of pyrophosphate.
The ribose moiety of ribosylanthranilate undergoes rearrangement to yield enol-1-o-
carboxylphenylamino-1- deoxyribulose-5-phosphate.
This intermediate is dehydrated and then decarboxylated to indole-3- glycerol phosphate, which
reacts with serine to form tryptophan.
24. 24-05-2022 24
Tyrosine and phenylalanine are synthesized from chorismate in plants and microorganisms via
simpler pathways.
A mutase converts chorismate into prephenate, the immediate precursor of the aromatic ring of
tyrosine and phenylalanine .
Prephenate is oxidatively decarboxylated to 4-hydroxyphenyl-pyruvate.
Alternatively, dehydration followed by decarboxylation yields phenylpyruvate.
These α-keto acids are then transaminated, with glutamate as amino group donor, to form tyrosine
and phenylalanine, respectively.
Tyrosine can also be made by animals directly from phenylalanine via hydroxylation at C-4 of the
phenyl group by phenyl hydroxylase.
26. 24-05-2022 26
1. Histidine is derived from 3 precursors.
(a)PRPP contributes 5 carbon atoms
(b) the purine ring of ATP contributes a nitrogen and a carbon
(c) glutamine contributes the second ring nitrogen.
2. The key steps of histidine biosynthesis are:
(a) the condensation of ATP and PRPP (step 1 )
(b) purine ring opening that ultimately leaves N-1 and C-2 linked to the ribose (Step 2 )
(c) formation of the imidazole ring in a reaction during which glutamine donates a nitrogen (Step 3 ).
30. 24-05-2022 30
• Biosynthesis of Porphyrins:
Glycine acts as a major precursor of porphyrins, which are constituents of haemoglobin, the cytochromes, and
chlorophyll.
The porphyrins are formed from four moles of the monopyrrole derivative, porphobilinogen .
In the first reaction, glycine reacts with succinyl-CoA to yield α-amino-βketoadipate, which is then
decarboxylated to produce δaminolevulinate. This reaction is catalyzed by δ-aminolevulinate synthase, a PLP
enzyme in mitochondria.
Two moles of δ-aminolevulinate condense to form porphobilinogen, the next intermediate.
This dehydration reaction is catalyzed by α-aminolevulinate dehydrase
Four moles of porphobilinogen come together to form protoporphyrin, through a series of complex enzymatic
reactions.
The iron atom is incorporated after the protoporphyrin has been assembled.
40. 24-05-2022 40
Other products:
Glycine, the smallest of all amino acids, is a precursor for the largest number of such products.
Special products of Glycine:
Glycine participates in generation of several important products:
1. Hippuric acid: (biomarker) It is formed by an amide linkage between the carboxyl group of
benzoic acid and the amino group of glycine.
2. Bile salts: Glycine becomes conjugated with bile acids to form conjugated bile salts.
3. Heam: Glycine combines with succinyl CoA in the first step of the Heam biosynthetic
pathways.
