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All 20 of The Amino Acids Present in Proteins Are Essential For Health

The document discusses amino acid metabolism in the human body. It states that the 20 amino acids found in proteins are essential to human health but are not stored by the body, so they must be obtained through diet, biosynthesis, or protein degradation. It then describes the two-phase catabolic process where amino groups are removed and carbon skeletons are converted to metabolic intermediates to be used for energy, glucose, or other biomolecules. Transamination reactions transfer amino groups between amino acids and are important in both synthesis and degradation.

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Deepu Chaurasiya
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63 views9 pages

All 20 of The Amino Acids Present in Proteins Are Essential For Health

The document discusses amino acid metabolism in the human body. It states that the 20 amino acids found in proteins are essential to human health but are not stored by the body, so they must be obtained through diet, biosynthesis, or protein degradation. It then describes the two-phase catabolic process where amino groups are removed and carbon skeletons are converted to metabolic intermediates to be used for energy, glucose, or other biomolecules. Transamination reactions transfer amino groups between amino acids and are important in both synthesis and degradation.

Uploaded by

Deepu Chaurasiya
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Download as PDF, TXT or read online on Scribd
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 All 20 of the amino acids present in proteins are

essential for health.


 Unlike fats and carbohydrates, amino acids are not stored
by the body.
 That is, no protein exists whose sole function is to
maintain a supply of amino acids for future use.
 Therefore, amino acids must be obtained from the diet,
synthesized de novo, or produced from normal protein
degradation.
 Any amino acids in excess of the biosynthetic needs of the
cell are rapidly degraded.
 The first phase of catabolism involves the removal of the α-
amino groups (usually by transamination and subsequent
oxidative deamination), forming ammonia and the
corresponding α-keto acids, the “carbon skeletons” of amino
acids.
 A portion of the free ammonia is excreted in the urine, but most
is used in the synthesis of urea, which is quantitatively the most
important route for disposing of nitrogen from the body.
 In the second phase of amino acid catabolism, described in , the
carbon skeletons of the α-keto acids are converted to common
intermediates of energy-producing metabolic pathways.
 These compounds can be metabolized to CO2 and water,
glucose, fatty acids, or ketone bodies by the central
pathways of metabolism.
 Transamination involves the transfer of an amino group
from one amino acid (which is converted to its
corresponding α-ketoacid) to an α-ketoacid (which is
converted to its corresponding α-amino acid). Thus, the
nitrogen from one amino acid appears in another amino
acid.
 The enzymes that catalyze transamination reactions are
known as transaminases or aminotransferases.
 Transamination reactions are readily reversible and
can be used in the synthesis or the degradation of amino
acids.
 Most amino acids participate in transamination reactions.
Lysine is an exception; it is not transaminated.
 Pyridoxal phosphate (PLP) serves as the cofactor for
transamination reactions. PLP is derived from vitamin B6.
 Oxidative deamination reactions result in the
liberation of the amino group as free ammonia.
 These reactions occur primarily in the liver and kidney.
They provide α- keto acids that can enter the central
pathways of energy metabolism and ammonia, which is a
source of nitrogen in hepatic urea synthesis.
 Amino acids fall into three categories: glucogenic,
ketogenic, or glucogenic and ketogenic.
 Glucogenic amino acids are those that give rise to a net
production of pyruvate or TCA cycle intermediates, such as
2-oxoglutarate (α-ketoglutarate) or oxaloacetate, all of
which are precursors to glucose via gluconeogenesis.
 All amino acids except lysine and leucine are at least partly
glucogenic.
 Lysine and leucine are the only amino acids that are
solely ketogenic, giving rise only to acetyl-CoA or
acetoacetyl-CoA, neither of which can bring about net
glucose production.
 A small group of amino acids comprised of isoleucine,
phenylalanine, threonine, tryptophan, and tyrosine give rise
to both glucose and fatty acid precursors and are thus,
characterized as being glucogenic and ketogenic.
Amino acid requirements of humans.
Single-letter or three-letter nomenclature of amino acids.
 NUTRITIONALLY NONESSENTIAL AMINO
ACIDS HAVE SHORT BIOSYNTHETIC
PATHWAYS.

 The enzymes glutamate dehydrogenase, glutamine


synthetase, and aminotransferases occupy central positions in
amino acid biosynthesis.

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