Metabolism of essential and

non-essential amino acids

Prepared by: Ms.Atiya Kaleem
Amino acids
Amino acids are organic compounds composed mainly of
nitrogen, carbon, hydrogen, and oxygen.
Your body needs 20 different amino acids to grow and
function properly. While all 20 of these are important for
your health, only 9 are classified as essential
Essential aminoacids
Essential amino acids cannot be made by the body. As
a result, they must come from food.
The 9 essential amino acids are: histidine, isoleucine,
leucine, lysine, methionine, phenylalanine, threonine,
tryptophan, and valine.
Non-essential
Nonessential amino acids support tissue growth and
repair, immune function, red blood cell formation, and
hormone synthesis. However, unlike essential amino
acids, a healthy body can create these proteins
Nonessential amino acids include: alanine, arginine,
asparagine, aspartic acid, cysteine, glutamic acid,
glutamine, glycine, proline, serine, and tyrosine.
Conditionally essential aminoacids

Several nonessential amino acids are classified as

conditionally essential.
These are essential only under specific circumstances,
such as during illness, pregnancy, infancy, or trauma.
For example, arginine is considered nonessential, but your
body can’t make as much as you need when you’re
healing from a serious injury or fighting certain diseases,
such as cancer.
That’s why, in certain situations, people may take arginine
supplements to meet their bodies’ needs.
Structure of Aminoacids
Glucogenic/Ketogenic?
glucogenic amino acid is an amino acid that can be
converted into glucose through gluconeogenesis. Their
catabolism yields pyruvate or one of the intermediates of the
citric acid cycle.
 ketogenic amino acids, which are converted into ketone
bodies. Amino acids whose catabolism yields either
acetoacetate or one of its precursor (acetyl CoA or
acetoacetyl CoA)
 Biosynthesis of Non-essential aminoacids
A. Synthesis from α-keto acids
Alanine, aspartate, and glutamate are synthesized by transfer of an amino group to the
α-keto acids pyruvate, oxaloacetate, and α-ketoglutarate, respectively. These
transamination reactions are the most direct of the biosynthetic pathways. Glutamate
is unusual in that it can also be synthesized by the reverse of oxidative deamination,
catalyzed by glutamate dehydrogenase, when ammonia levels are high.
B. Synthesis by amidation

 
1. Glutamine: This amino acid, which contains an amide linkage with
ammonia at the γ-carboxyl, is formed from glutamate by glutamine
synthetase .The reaction is driven by the hydrolysis of ATP. In addition
to producing glutamine for protein synthesis, the reaction also serves as
a major mechanism for the transport of ammonia in a nontoxic form.
 
2. Asparagine: This amino acid, which contains an amide linkage with
ammonia at the β-carboxyl, is formed from aspartate by asparagine
synthetase, using glutamine as the amide donor. Like the synthesis of
glutamine, the reaction requires ATP and has an equilibrium far in the
direction of amide synthesis.
C. Proline

 Glutamate via glutamate semialdehyde is converted to proline

by cyclization and reduction reactions.
D. Serine, glycine, and cysteine

1. Serine: This amino acid arises from 3-phosphoglycerate, an intermediate in glycolysis, which

is first oxidized to 3-phosphopyruvate and then transaminated to 3-phosphoserine. Serine is
formed by hydrolysis of the phosphate ester.
Serine can also be formed from glycine through transfer of a hydroxymethyl group by serine
hydroxymethyltransferase using N5,N10-methylene-THF as the one-carbon donor.
2.  Glycine: This amino acid is synthesized from serine by removal of a hydroxymethyl group,
also by serine hydroxymethyltransferase (see Figure 20.6A). THF is the one-carbon acceptor.
3. Cysteine: This amino acid is synthesized by two consecutive reactions in which Hcy
combines with serine, forming cystathionine, which, in turn, is hydrolyzed to α-ketobutyrate
and cysteine. (Hcy is derived from methionine) Because methionine is an essential amino acid,
cysteine synthesis can be sustained only if the dietary intake of methionine is adequate.
E. Tyrosine

 Tyrosine is formed from phenylalanine by phenylalanine hydroxylase. The

reaction requires molecular oxygen and the coenzyme tetrahydrobiopterin
(BH4), which is synthesized from guanosine triphosphate. One atom of
molecular oxygen becomes the hydroxyl group of tyrosine, and the other
atom is reduced to water. During the reaction, BH4 is oxidized to
dihydrobiopterin (BH2). BH4 is regenerated from BH 2 by NADH-
requiring dihydropteridine reductase. Tyrosine, like cysteine, is formed
from an essential amino acid and is, therefore, nonessential only in the
presence of adequate dietary phenylalanine.
Summary of synthesis of Aminoacids