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Biochemistry Lecture PPT 7

Protein and amino acids are broken down in the body through a multi-step process. Most dietary nitrogen is consumed as protein, which must be broken down into amino acids by proteolytic enzymes in the stomach, pancreas, and small intestine before being absorbed. Amino acids undergo transamination and deamination reactions to produce ammonia and keto acids. Ammonia is toxic if not removed, so the liver converts it into urea through the urea cycle for excretion in urine. This process allows the body to reuse the nitrogen from amino acids while removing waste.

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129 views16 pages

Biochemistry Lecture PPT 7

Protein and amino acids are broken down in the body through a multi-step process. Most dietary nitrogen is consumed as protein, which must be broken down into amino acids by proteolytic enzymes in the stomach, pancreas, and small intestine before being absorbed. Amino acids undergo transamination and deamination reactions to produce ammonia and keto acids. Ammonia is toxic if not removed, so the liver converts it into urea through the urea cycle for excretion in urine. This process allows the body to reuse the nitrogen from amino acids while removing waste.

Uploaded by

Chiranjeevi Joshi
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© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Protein & Amino acid metabolism

Most of the nitrogen in the diet is consumed in the form of


protein, typically amounting from 70 to 100g/day
Proteins are generally too large to be absorbed by the
intestine
They must, therefore, be hydrolyzed to yield their
constituent amino acids, which can be absorbed
Proteolytic enzymes responsible for degrading proteins are
produced by three different organs:
• Stomach Pepsin
• Pancreas (pancreatic peptidases)
• Small intestine
Overview : Protein & Amino acid metabolism

Amino N2

* Ketogenic AAs

Glucogenic AAs *
Transamination: the tunneling of amino groups to glutamate
• The transfer of an amino (- NH2) group from one amino acid to a keto acid is known as
• transamination
• This process involves the interconversion of a pair of amino acids and a pair of keto acids,
catalyzed by a group of enzymes called aminotransferase
• All aminotransferase require pyridoxal phosphate (PLP), a coenzyme derived from vit. B6
• There is no free NH3 liberated, and is a reversible rxn
• Transamination is very important for production of nonessential amino acids
• Transamination
diverts the excess
amino acids towards
energy generation
• All amino acids except
lysine, threonine,
proline and
participate
 ALT and AST are clinically
significant aminotransferases.
ALT/ sGPT Both are markers of liver
disease; however, ALT is more
liver specific than AST
 Increased levels are found in
AST/ sGOT hepatitis, cirrhosis, obstructive
jaundice and other hepatic
diseases
 Slight elevation of ALT enzymes
is also seen in myocardial
infraction
 High AST levels may also be a
sign of heart problems or
pancreatitis
DEAMINATION
• The removal of amino group from the amino acids as NH3 is deamination
• Deamination results in the liberation of ammonia (for urea synthesis)
• The carbon skeleton of amino acids is converted to keto acids
• Deamination may be either oxidative or non-oxidative

Oxidative deamination is the liberation of free ammonia from the amino group of amino
acids coupled with oxidation
• This takes place mostly in liver and kidney
• The purpose of oxidative deamination is to provide NH3 for urea synthesis and keto acids
for a variety of reactions, including energy generation
1. Glutamate dehydrogenase (GDH) occupies a central position in Nitrogen metabolism
2. Amino acid oxidases
Non Oxidative deamination
Some of the amino acids can be deaminated to liberate NH3 without undergoing oxidation
E.g. Amino acid dehydrase/dehydratases
Oxidative deamination by GDH
• Transamination tunnels the amino groups to glutamate
• Glutamate rapidly undergoes oxidative deamination,
catalyzed by glutamate dehydrogenase (GDH) to liberate
Aminotransferases
ammonia
• This enzyme is unique in that it can utilize either NAD+
or NADP+ as a coenzyme
GLUTAMATE
DEHYDROGENASE

• Mostly transamination and deamination occur simultaneously, often involving


glutamate as the central molecule
• For this reason, the sequence of reaction is often termed as transdeamination
Oxidative deamination by amino acid oxidases
• L-Amino acid oxidase and D-amino acid oxidase are flavoproteins, possessing FMN
and FAD, respectively
• They act on the corresponding amino acids( L or D) to produce keto acids and NH3
• D-Amino acids are not present in the mammalian protein, however they are taken
regularly in diet through plants and microorganisms
Non Oxidative deamination by
• Amino acid dehydrases:
Serine, Threonine are the hydroxy amino acids
They undergo non-oxidative deamination catalyzed by PLP-dependent dehydrase or dehydratase

• Amino acid desulfhydrases:


The sulfur amino acids, namely cysteine undergo deamination coupled with desulfhydration
to give keto acid
Metabolism of ammonia
• The production of NH3 occurs from the amino acids (deamination) , biogenic amines,
amino group of purines and pyrimidines and by the action of intestinal bacteria
• Despite a regular and constant production of NH3 from various tissues, its concentration in
the circulation is surprisingly low (normal plasma 10-20 mg/dl)
• This is mostly because the body has an efficient mechanism for NH3 transport and its
• immediate utilization for urea synthesis
• The transport of ammonia between various tissues and the liver mostly occurs in the form
of glutamine (storehouse of NH3)
• Glutamine serves as a storage and transport form of NH3
Release of ammonia from glutamine and glutamate
Toxicity of ammonia
• Even a marginal elevation in the blood ammonia concentration is harmful to the brain
• Ammonia, when it accumulates in the body, results in slurring of speech and blurring
of the vision and causes tremors
• Hyperammonemia: It may lead to coma and, finally, death

Disposal of ammonia
• The animals must detoxify ammonia by converting it into a relatively-nontoxic form
• Nitrogenous waste is excreted in different forms by different species
• These include (a) ammonia, (b) urea, and (c) uric acid

Ammoniotelic Ureotelic Uricotelic


Overview : Protein & Amino acid metabolism

Amino N2

* Ketogenic AAs

Glucogenic AAs *
Urea cycle
• Urea is the end product of protein metabolism (amino acid metabolism)
• The nitrogen of amino acids, converted to ammonia is toxic to the body
• It is converted to urea and detoxified
• Urea accounts for 80-90% of the nitrogen containing substances excreted in urine
• Urea is synthesized in liver and transported to kidneys for excretion in urine
• Urea cycle is the first metabolic cycle that was elucidated by Hans Krebs and Kurt
Henseleit (1932), hence it is known as Krebs-Henseleit cycle
• The individual reactions however, were described by Ratner and Cohen
• Urea synthesis is a five-step cyclic process, with five distinct enzymes
• The first two enzymes are present in mitochondria while the rest are localized in
cytosol
UREA/ TCA bicycle
Multiple pathways where carbon
skeleton of various aa joins TCA cycle

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