• C H A P T E R • 16 •

AMINO ACID
METABOLISM
•
Nonessential Amino Acid Synthesis
Essential Amino Acids
Amino Acid Degradation
Generalities of Amino Acid Catabolism
Products of Amino Acid Degradation

• • • • • • • • • • • •

NONESSENTIAL AMINO ACID SYNTHESIS

AMINO ACID SYNTHETIC ROUTE

Ala From Pyruvate by transamination

Glu From -Ketoglutarate by transamination
Asp From Oxaloacetate by transamination
Gln Glu  NH4  ATP  Gln
Asn Asp  Gln  ATP  Asn  AMP  PPi  Glu
Ser Glucose  hydroxypyruvate  Ser
Glucose  phosphohydroxypyruvate  Ser
Gly Ser  THfolate  Gly  CH2-THfolate
Arg Glu  Glu-semialdehyde  ornithine  Arg
Pro Glu  Glu-semialdehyde  Pro
Tyr Phe  Tyr (phenylalanine hydroxylase, biopterin cofactor)
Cys Met  homoCys  Ser  cystathionine  Cys

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The other nine amino acids are essential and must be taken from the
diet. Notice that some of the amino acids require other amino acids for
their synthesis. Exam questions usually center on whether or not an
amino acid is essential and the metabolites that serve as precursors for
specific amino acids.

ESSENTIAL AMINO ACIDS

His, Ile, Leu, Lys, Met, Phe, Thr, Trp, Val

AMINO ACID DEGRADATION

Ketogenic: Leu, Lys
Degraded to acetyl-CoA.
Glucose cannot be made from
these.
Glucogenic and Ketogenic: Ile, Phe, Tyr, Trp
Goes both ways.
Glucogenic: Everything else
Degraded to pyruvate or a member
of the TCA cycle
Glucose can be made from these.

The complete catabolic pathways of the individual amino acids are

a complex set of pathways that are probably not worth remembering in
detail (this is obviously opinion). This doesn’t mean they’re not impor-
tant. In fact, there are diseases that are caused by inherited defects in
most of the pathways. The preceding table is a general guide that shows
where the amino acids go and points out significant intermediates.

GENERALITIES OF AMINO ACID CATABOLISM

If a vitamin or cofactor is involved in amino acid metabolism, it’s
most likely pyridoxal phosphate (B6), unless it involves serine,
and then it’s B6 and folic acid.
Nitrogen is dumped into the urea cycle by transamination to make
Asp or Glu or by deamination to make ammonia.

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• 188 • Basic Concepts in Biochemistry

PRODUCTS OF AMINO ACID DEGRADATION

Ala to pyruvate by transamination
Arg to urea and glutamate
Asp to oxaloacetate by transamination or to fumarate via urea cycle
Asn to Asp
Cys carbon to pyruvate, sulfur to sulfate
Glu to -ketoglutarate by transamination, then to glucose
Gln to glutamate by hydrolysis
Gly to glyoxylate or serine
His to glutamate and one-carbon pool
Met to propionyl-CoA via homocysteine  cystathionine 
ketobutyrate
Pro to glutamate
Ser to glycine and CH2THfolate
Thr to propionyl-CoA through ketobutyrate
Val to propionyl-CoA through transamination, decarboxylation, and
a bunch of rearrangements
Leu to acetoacetate and acetyl-CoA through transamination, decar-
boxylation, and a bunch of rearrangements
Ile to propionyl-CoA through transamination, decarboxylation, and
a bunch of rearrangements
Phe to Tyr, then to acetoacetate and fumarate
Tyr to acetoacetate and fumarate
Try to acetyl-CoA via ring oxidation and cleavage to ketoadipate
Lys to acetyl-CoA via transamination and deamination to ketoadi-
pate

The nitrogen contained in the amino acids is usually disposed of

through the urea cycle. One of the early, if not the first, steps in amino
acid catabolism involves a transamination using oxaloacetate or -
ketoglutarate as the amino-group acceptor. This converts the amino acid
into a 2-keto acid, which can then be metabolized further.

R—CH(NH  
3)CO 2  oxaloacetate ∆ R—(C“O)CO 2  Asp

These enzymes invariably involve a cofactor, pyridoxal phosphate

(vitamin B6). In addition, pyridoxal phosphate is also required for most
decarboxylations, racemizations, or elimination reactions in which an
amino acid is a substrate. Pyridoxal phosphate is not involved in decar-
boxylations in which the substrate is not an amino acid. So if a question

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asks something about an amino acid and a vitamin, the answer will most
likely be pyridoxal phosphate. There are a couple of exceptions in which
pyridoxal phosphate may not be the answer to a vitamins-amino acid
question. If the amino acid is serine, then the answer might also include
folic acid (the reaction here is the conversion of serine to glycine with
the formation of methylene tetrahydrofolic acid–see the section in Chap.
21 on one-carbon metabolism). The other place you might see a vitamin
other than pyridoxal phosphate is in the metabolism of propionyl-CoA,
a product of the catabolism of some amino acids. In this case, the vita-
min may be B12 (the conversion of methylmalonyl-CoA to succinyl-
CoA—see “-Oxidation Odd-Chain-Fatty Acids” in Chap. 13).
The nitrogen from the amino groups of most amino acids is transam-
inated into glutamate or aspartate at some point in the degradative
scheme. This nitrogen enters the urea cycle as glutamate, which is reduc-
tively deaminated by glutamate dehydrogenase to yield ammonia or by
the reaction of aspartate with citrulline to give argininosuccinate (urea
cycle).

BG McGraw-Hill: Gilbert, Basic Concepts in Biochemistry, JN 5036