Amino Acid Synthesis

Download as pdf or txt
Download as pdf or txt
You are on page 1of 16

SYNTHESIS OF AMINO ACIDS.

• SYNTHESIS OFAMINO ACIDS.

1. Reduction of N2 to NH4.
2. Transamination.
3. Synthesis of amino acids by metabolic
precursors.
INTRODUCTION
• Amino acids are organic compounds containing amine (-NH2)
and carboxyl (-COOH) functional groups, along with a side
chain(R group) specific to each amino acid.
CLASSIFICATION
• Nonpolar/hydrophobic aminoacids
glycine,alanine,valine,leucine,methionine,phenyalalanine,
proline

• polar/hydrophilic amino acids


serine, cysteine, tyrosine, glutamicacid, asparaticacid,
lysine,arginine

• Sulphur containing amino acids


Cystine, methionine, cysteine
List of essential and non essential amino acids

Nutritionally essential Nutritionally non-essential


amino acids amino acids
Arginine Alanine
Histidine Asparagine
Isoleucine Aspartic acid
Leucine Cysteine
Lysine Glutamic acid
Methionine Glutamine
Phenylalanine Glycine
Threonine Proline
Tryptophan Serine
Valine Tyrosine
SYNTHESIS OF AMINO ACIDS

• Amino acid synthesis is the set of biochemical processes


(metabolic pathways) by which the various amino acids are
produced from other compounds.
STEPS….
1. Reduction of N2 to NH4.

2. Transamination.

3. Synthesis of amino acids by metabolic precursors.


1) REDUCTION OF N2 TO NH4
• It is the first step during synthesis of amino acids.

• In which reduction of N2 TO NH4 takes place.

• The conversion of nitrogen to ammonia is a reduction reaction


which is exergonic in nature

• Biological fixation of nitrogen is carried out by a highly


conserved complex of proteins called nitrogenase complex.
2) TRANSAMINATION
 Transamination, a chemical reaction that transfers an amino
group to a ketoacid to form new amino acids.
 This pathway is responsible for the deamination of most amino
acids.
 This is one of the major degradation pathways which
convert essential amino acids to nonessential amino
acids (amino acids that can be synthesized de novo by the
organism).
 Transamination in biochemistry is accomplished by enzymes
called transaminases or aminotransferases.
FOR EXAMPLE

 α-ketoglutarate acts as the predominant amino-group


acceptor and produces glutamate as the new amino acid.

 Aminoacid + α-ketoglutarate ↔ α-keto acid + Glutamate

Glutamate's amino group, in turn, is transferred to oxaloacetate


in a second transamination reaction yielding aspartate.

 Glutamate+ oxaloacetate ↔ α- ketoglutarate + aspartate


Aminotransfer reaction between an amino
acid and an alpha-keto acid

Keto acids (also called oxo acids or oxoacids)


are organic compounds that contain a carboxylic
acid group and a ketone group.
3) SYNTHESIS OF AMINO ACIDS
BY METABOLIC PRECURSORS

• 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.

• It is believed that the pathways in higher plants and animals


are similar, but comparatively less is known of the enzymes
involved.
AN OVERVIEW OF AMINO ACID BIOSYNTHESIS
Ribose-5-phosphate Pyruvate α-ketoglutarate
3-phosphoglycerate
Glutamate
Alanine Serine
Histidine
Glutamine
Valine Cysteine
Proline
Oxaloacetate Leucine Glycine
Arginine
Aspartate
SYNTHESIS OF AMINO ACIDS BY METABOLIC
Asparagine PRECURSORS

Methionine

Phosphoenolpyruvate and erythrose-4-phosphate


Threonine

Phenylalanine
Isoleucine
Tyrosine
Lysine Tryptophan
AMINO ACIDS CHEMICAL STRUCTURES

You might also like

pFad - Phonifier reborn

Pfad - The Proxy pFad of © 2024 Garber Painting. All rights reserved.

Note: This service is not intended for secure transactions such as banking, social media, email, or purchasing. Use at your own risk. We assume no liability whatsoever for broken pages.


Alternative Proxies:

Alternative Proxy

pFad Proxy

pFad v3 Proxy

pFad v4 Proxy