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Protein Catabolism
Breakdown of protein into amino acids
Liver cells convert amino acids into
substances that can enter the Krebs cycle
deamination removes the amino group
(NH2)
converts it to ammonia (NH3) & then
urea
urea excreted in the urine
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Protein Anabolism
Production of new proteins by
formation of peptide bonds
between amino acids
10 essential amino acids are
ones we must eat because we
can not synthesize them
nonessential amino acids can be
synthesized by transamination
(transfer of an amino group to a
substance to create an amino
acid)
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Protein Anabolism
Occurs on ribosomes in almost every
cell
Stimulated by insulinlike growth
factor, thyroid hormone, insulin,
estrogen & testosterone
Large amounts of protein in the diet
do not cause the growth of muscle,
only weight-bearing exercise
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Amino acid pool
No storage facility for amino acids
Amino acids incorporated into functional
proteins
Amino acids in blood and extracellular
fluid represent an amino acid pool
Amino acids move through this pool
Average 60 kg woman
10 kg protein
170 g free amino acids in pool
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Fate of amino acids
If not required for protein synthesis amino
groups removed
For most amino acids occurs primarily in liver
For certain amino acids (leucine, isoleucine, valine)
occurs primarily in skeletal muscle)
amino groups transferred to form alanine and taken to
liver for disposal via glucose-alanine cycle
Carbon skeletons used for:
Gluconeogenesis (in liver)
Oxidised in Krebs Cycle
Amino groups used for:
Synthesis of nonprotein nitrogen compounds
Disposed of via Urea Cycle
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GLUCOSE-ALANINE CYCLE
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FATE OF AMINO ACIDS
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Amino acid metabolism
Transamination
Deamination
Formation of urea
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Transamination reactions
Amino group removed from one amino acid and
transferred to another
Catalysed by aminotransferase enzymes
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Deamination reactions
Amino group (and H) removed
Forms ammonia (NH3)
Carbon skeleton left can be
oxidised in Krebs Cycle
used for gluconeogenesis
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Amino Acid Biosynthesis
Plants and microorganisms can make all 20
amino acids and all other organisms need N
metabolites
In these organisms, glutamate is the source
of N, via transamination (aminotransferase)
reactions
Mammals can make only 10 of the 20 amino
acids
The others are classed as "essential" amino
acids and must be obtained in the diet
All amino acids are grouped into families
according to the intermediates that they are
made from
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The -Ketoglutarate Family
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The glutamate synthase reaction
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Glutamate-dependent transamination - primary mechanism for
amino acid synthesis
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Proline biosynthesis from glutamate
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Synthesis of ornithine from glutamate - a step in
arginine biosynthesis
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The Aspartate Family
Asp, Asn, Lys, Met, Thr, Ile
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Asp + Gln --> Asn + Glu
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Transamination of oxaloacetate yields
aspartate
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The Pyruvate Family
Ala, Val, Leu
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ALANINE BIOSYNTHESIS
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3-Phosphoglycerate Family
Ser, Gly, Cys
3-Phosphoglycerate dehydrogenase
diverts 3-PG from glycolysis to amino
acid paths
Transamination by Glu gives 3-P- serine
Phosphatase yields serine
A piridoxal phosphate-dependent
enzyme makes Cys
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Biosynthesis of
serine from 3-
phosphoglycerate
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Glycine biosynthesis from serine
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Cysteine biosynthesis
Sulfhydration of O-acetylserine
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The Phosphoenolpyruvate Family
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BIOSYNTHESIS TYROSINE
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Degradation of Amino Acids
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Degradation of
amino acids
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Degradation of Ala,
Ser, Cys, Gly and Trp
and Thr to pyruvate
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Urea cycle
Ammonia is toxic
Readily ionises to ammonium ion NH4+
NH4+ converted to urea in liver (urea
cycle)
Urea contains 2 x NH2
One from NH4+
One from aspartate
Urea excreted in urine
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UREA CYCLE
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Urea Cycle
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