Amino Acid Metabolism

LAGAMAYO, Linear Larie B.

CCE - 4

Amino Acid Breakdown for

Energy

Amino Acid Catabolism

Importance
Potential Source of Energy and especially

during fasting of glucose

Incomplete metabolism of a number of
amino acids results in the accumulation of
toxic amino acid breakdown intermediates

Fasting State
Within one hour of a meal the blood glucose level begins to fall.
The

insulin concentration also begins to fall and the glucagon

concentration begins to rise. These changes in hormone concentrations
trigger the release of metabolic fuels from the body stores.

Glucagon stimulates glycogenolysis, the break down of liver glycogen to

maintain the blood glucose concentration.

Glucagon also stimulates gluconeogenesis, synthesizing glucose from

lactate, alanine, and glycerol. As fasting progresses, gluconeogenesis

becomes more important to maintain the blood glucose concentration.
After 30 hours of fasting, the liver glycogen stores are depleted, and

gluconeogenesis is generating all of the blood glucose.

Only the glycerol moiety of triacylglycerols can be used as source of
glucose. Glucagon also stimulates the break down of proteins and the
catabolism of amino acids. This generates ammonia which the liver
converts into urea to be excreted.

Fasting State
During fasting the triacylglycerols stored in the adipose

tissue become the major energy source. The glycerol

component is used for gluconeogenesis and the fatty
acids released are oxidized by tissues such as muscle
and heart tissue. The liver absorbs these fatty acids and
converts them into ketone bodies which are released in
the blood. These ketone bodies can fuel the muscles and
heart saving glucose for the brain.

Degradation
Two Classes of Degradation
Glucogenic (production of glucose)
Ketogenic

Carbon Families
C3 Family Amino Acids convertible to

pyruvate
Alanine

Serine

Side Note: Ethanol and

Acetaldehyde
Ethanol and Acetaldehyde

Carbon Families
Cysteine

Threonine

Carbon Families
C4

Families
oxaloacetate
Asparagine

Aspartate

Amino

Acids

convertible

to

Carbon Families
C5
Family Amino Acids convertible to

Ketoglutarate
Glutamate

Glutamine

Carbon Families
Arginine
Proline
Histidine

Carbon Families

Branched Chain Amino

Acids
Leucine
Valine
Isoleucine

Branched Chain Amino Acids

Aromatic Amino Acids

Phenylalanine
Tyrosine
Tryptophan

Aromatic Amino Acids

Aromatic Amino Acids

Tryptophan
Lysine

Methionine

Summary
Amino acids are a major energy source, especially during

conditions in which glucose availability is limited.

Amino acids may be either glucogenic or ketogenic.
The C3 family (alanine, serine, glycine,threonine, and
cysteine) can all be converted to the 3-carbon a - ketoacid
pyruvate, although some are converted to other
molecules under appropriate conditions.
The C4 family (aspartate and asparagine) are converted to

the 4-carbon compounds oxaloacetate or fumarate.

The C5 family (glutamate, glutamine, histidine, proline,
and arginine) are all converted to glutamate, and then to
a - ketoglutarate.

Summary
The branched-chain amino acids (leucine, isoleucine, and

valine) are broken down by a series of common enzymes into

coenzyme A derivatives. These are then metabolized by
separate pathways depending on the structure of the original
compound. Leucine is converted into HMG-CoA, the substrate
for ketone body production, and is exclusively ketogenic.
Valine is converted to propionyl-CoA and is exclusively
glucogenic. Isoleucine is converted to acetyl-CoA and
propionyl-CoA, and is therefore both ketogenic and glucogenic.
The aromatic amino acids phenylalanine and tyrosine result in

formation of acetoacetate and fumarate, while tryptophan

results in formation of acetoacetate and (via alanine)
pyruvate. Each of these compounds is therefore both
ketogenic and glucogenic.

Summary
Lysine is broken down by a pathway that is related to that

for the tryptophan indole ring, and forms acetoacetate.

Methionine is used to produce a variety of biosynthetic
intermediates; it can be converted into propionyl-CoA, and
is therefore glucogenic.

Amino Acid Biosynthesis

Amino Acid Biosynthesis

Nitrogen source is needed.
In animals, glutamate and glutamine play

the pivotal roles.

Glutamate is synthesized from ammonia
and -ketoglutarate by the action of
glutamate dehydrogenase

Amino Acid Biosynthesis

The regulation of glutamine synthetase plays a

crucial role in controlling nitrogen metabolism.

The dynamic duo of glutamate dehydrogenase
and glutamine synthetase are found in all
living organisms.