METABOLISM OF AMINO

ACIDS AND PROTEINS

HBC 202

Ms M. Mombeshora
HBC 202 Lecture 01
 Incorporation of
nitrogen into amino
acids

Ms M. Mombeshora
HBC 202 Lecture 01
Nitrogen the abundant gas

Oxygen Carbon dioxide

21 % 0.004 %

Other gases
Nitrogen ˂1%
78 %
 Nitrogen metabolism
• Nitrogen important constituent of cellular
components
Examples of N-containing compounds
alkaloids amides amino acids
proteins DNA RNA
enzymes vitamins hormones
 Key constituent of proteins and nucleic acids
 Remember nucleic acids control cellular activities
 Amino acids meet several cellular
needs
• Amino acids produced by digestion of dietary
protein and during protein turnover in the body
cells become part of the body’s amino acid pool

• The amino acid pool is the total quantity of free

amino acids present in tissue cells, plasma and
other body fluids

• The amino acids of amino acid pool are available

for several cellular needs
 The nitrogen cycle, nitrogen fixation
and amino acids

The total amount of nitrogen fixed annually in the

biosphere exceeds 4x10 11 kg
 Nitrogen the abundant gas
• Not all organisms possess the ability to utilise
molecular N2 directly
• Certain bacteria, blue green algae and few
fungi, can utilise N2 directly and fix it
• Most plants are capable of utilising other
forms of nitrogen with ease
 Introduction of nitrogen into plants
• Nitrogen enters roots as NO3- or NH4+

• Nitrate reduction results in the production of

NH4+ called Nitrogen fixation

• NH4+ first incorporated into amino acids via

the glutamine synthetase (GS) reaction
 Introduction of nitrogen into plants
• The NH4+ is incorporated into amino acids in
roots and leaves

• The amino acids get integrated into proteins

• The main if not sole function of some proteins

is to provide a store of amino acids
Introduction of nitrogen into plants
 Introduction of nitrogen into plants
• Ammonical form of N is available in soil in the
form of urea or NH4+ in free-state
• Urea, if present, is first split into NH4+ and CO2,
and NH4+
• NH4+ is utilised directly by metabolic pathways
in higher plants
• But recent studies indicate that urea can be
directly used up by metabolic pathways in
certain plants
 Nitrogen compounds
• The decay of dead plants and animals releases
nitrogen compounds e.g
– amino acids
– nucleotides e.t.c
– nitrate compounds constitute organic form of N
• The same are absorbed by the root system and
utilized directly
• Thus the decaying organic matter acts as the rich
source of organic nitrogen that can be used by higher
plants and micro-organisms
Recall structure of amino acid
Non-polar groups
Groups with S
Polar OH groups
Polar amide groups
Charged (-) acidic
Charged (+) basic
Aromatic groups
 The synthesis of ammonia

• The cyanobacteria ,
Azotobacter and other
nitrogen-fixing bacteria
live as symbiont the
root nodules of
leguminous plants are
capable of fixing
atmospheric nitrogen

Nitrogen-fixing nodules
 Ammonia to amino acids
• Free NH3 is the only utilisable
form of N directly
incorporated into amino acids
• Every source of nitrogen, first
it has to be converted to NH3
and fixed into amino acid
• Conversion or transfer to other
forms by various pathways
that operate in living systems
 Nitrogen to amino acids
• NO3 -、NO2 - reduced to NH3

nitrate reductase nitrite reductase

NO3 - NO2 - NH3
 Nitrogen reduction to ammonia
• Molecular N is reduced on the surface of the
enzyme nitrogenase in a multistep process

• The intermediate products remain bound to

the enzyme surface and only the final product
i.e NH4+ is released from the enzyme
 Assimilation of NH3 into amino acids

• All organisms assimilate ammonia via two

main reactions catalyed by:

– glutamate dehydrogenase giving rise to Glu

– glutamine synthetase giving rise to Gln

• The amino nitrogen in Glu and Gln are then

used in further biosynthetic reactions to give
rise to other amino acids
 Assimilation of NH3 into amino acids

• Once ammonia has been formed via nitrogen

fixation, the nitrogen can be incorporated into
either glutamate or glutamine for further use
Assimilation of NH3 into amino acids
 Assimilation of NH3 into amino acids
• Glu is the source of amino groups for synthesis
of most amino acids
• Gln is the source of amino groups for synthesis
of most other nitrogen-containing molecules
(e.g., nucleotides)
 Assimilation of NH3 into amino acids
• Formation of Glu: reductive amination of α-KG
via glutamate dehydrogenase
 Assimilation of NH3 into amino acids
• Formation of Gln: glutamine synthetase
reaction
 Allosteric control of glutamine
synthetase

• Complex
control with
many allosteric
regulators(end
products of Gln
metabolism)
 Transamination reactions
Amino acids part with their amino groups by
transamination reactions
• Many of the reactions of amino acid metabolism
require that amino acids first lose their alpha amino
group
• The most common way for this to occur is by
transamination — the transfer of an amino group from
one molecule to another
• An intermediate of the citric acid cycle, α-ketoglutarate
is the usual acceptor of the amino group
• The products of the reaction are an α-keto acid and
glutamic acid.
 Transamination reactions
• The amino group of
glutamate can be
transferred to many α-
keto acids

• Reactions catalysed by
enzymes known as
transaminases or
aminotransferases
Transamination reactions
Transamination reactions
 Transamination
• Amino acids that don't participate in
transamination:
• Lysine, threonine, proline
• Transamination is reversible
 Transamination reactions
• Transamination reactions are catalysed by
transaminases
• Transaminases are the indicators of disease or
trauma that affects tissues
• The principal transaminase of liver is glutamic-
pyruvic transaminase (GPT), an enzyme that
catalyses the formation of pyruvate from
alanine
 Transamination reactions
• The principal transaminase of the heart
muscle is glutamic-oxalacetate transaminase
(GOT), an enzyme that catalyses the formation
of oxaloacetate, one of the intermediates of
the citric acid cycle, from aspartic acid