Deamination

AMINO ACIDS
 Deamination
Deamination is the removal of an amino group from a molecule.
Enzymes that catalyze this reaction are called deaminases.
In the human body, deamination takes place primarily in the liver,
however it can also occur in the kidney.
 Deamination

Deaminase
Amino acid Keto acid
NH3
 Oxidative Deamination
 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 α-keto acids for a variety of reactions, including
energy generation.
 In the process of transamination the amino groups of most amino
acids are transferred to α-ketoglutarate to produce glutamate.
Donor of NH3 Product Acceptor of NH3 Product Enzyme

Aspartate Oxaloacetate a-Ketoglutarate Glutamate SGOT

Alanine Pyruvate a-Ketoglutarate Glutamate SGPT
 Oxidative Deamination
 Thus, glutamate serves as a collection centre for amino groups in
the biological system.
 Glutamate rapidly undergoes oxidative deamination, catalysed by
glutamate dehydrogenase (GDH) to liberate ammonia.
 This enzyme is unique in that it can utilize either NAD+ or NADP+ as
a coenzyme.
 Regulation of GDH activity
 Glutamate dehydrogenase is a zinc containing mitochondrial enzyme.
 lt is a complex enzyme consisting of six identical units with a
molecular weight of 56,000 each.
 GDH is controlled by allosteric regulation. GTP and ATP inhibit
whereas GDP and ADP activate-glutamate dehydrogenase.
 Steroid and thyroid hormones inhibit GDH.
 After ingestion of a protein-rich meal, liver glutamate level is
elevated.
 lt is converted to α-ketoglutarate with liberation of NH3.
 When the cellular energy levels are low, the degradation of glutamate
is increased to provide α-ketoglutarate which enters TCA cycle to
 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 α-keto
acids and NH3; and, oxygen is reduced to H2O2, which is later
decomposed by catalase.
 The activity of L-amino acid oxidase is much low while that of D-
amino acid oxidase is high in tissues (mostly liver and kidney).
 L –Amino acid oxidase does not act on glycine and dicarboxylic
acids.
 This enzyme, due to its very low activity, does not appear to play any
significant role in the amino acid metabolism.
L-amino acid
 Non-oxidative deamination
Amino acid dehydrases: Serine, threonine and homoserine are the
hydroxy amino acids. They undergo non-oxidative deamination
catalysed by PLP-dependent dehydrases (dehydratase
 Non-oxidative deamination
Amino acid desulfhydrases: The sulphur amino acids, namely cysteine
and homocysteine, undergo deamination coupled with desulfhydration
to give keto acids.
 Non-oxidative deamination
Deamination of histidine : The enzyme Histidase acts on histidine to
liberate NH3 by a non-oxidative deamination process.
Other types of deamination
CLASSIFICATION OF PROTEIN
According to According to the According to Aminoacid Sequence
shape: biological value: structure: and 3D structure
Proteins of high Simple
Fibrous Primary
biological value

Proteins of low Complex

Globular Secondary
biological value

Membrane Derived Tertiary

Quaternary
 DIGESTION OF PROTEIN
 Proteins can be informally divided into three main classes, which correlate with
typical tertiary structures: globular proteins, fibrous proteins, and membrane
proteins.
 Almost all globular proteins are soluble and many are enzymes.
 Fibrous proteins are often structural, such as collagen, the major component
of connective tissue, or keratin, the protein component of hair and nails.
 Membrane proteins often serve as receptors or provide channels for polar or
charged molecules to pass through the cell membrane.
 Thus proteins are very important in our diets. Several dietary sources of proteins
include nuts, beans/legumes, skim milk, egg whites, and meat.
Protein digestion begins in the stomach, where the action of gastric
juice hydrolyzes about 10% of the peptide bonds.
Gastric juice is a mixture of water (more than 99%), inorganic ions,
hydrochloric acid, and various enzymes and other proteins.

The hydrochloric acid (HCl) in gastric juice is secreted by glands in

the stomach lining.
The pH of freshly secreted gastric juice is about 1.0, but the contents
of the stomach may raise the pH to between 1.5 and 2.5.
HCl helps to denature food proteins; that is, it unfolds the protein
molecules to expose their chains to more efficient enzyme action.
 DISEASE OF PROTEIN
METABOLISM
 Kwashiorkor
 Marasmus