Selected Solutions to End of Chapter 18 Problems

1. Transamination products: (you already know these structures)draw them here and then see
(remember the prof emphasized in the lecture amino-to-keto). Answer names:
a. Oxaloacetate.

b. -ketoglutarate.

c. pyruvate.

d. phenylpyruvate.

2. Note that the question says excess of pure lactate dehydrogenase and NADH. This is important
because alanine-transaminase will produce pyruvate which as soon as it is produced will be reduced
to lactic acid using NADH. NADH has a strong absorbance at 340 nm, so the rate of decrease in 340
nm absorbency is due to the rate of the transaminase present in a sample.

3. Blood contains all amino acids to supply protein synthesis in all tissues. It has an excess alanine
and glutamine because are the only amino acids used to transport amino groups from muscles and
all other organs to the liver.

4. No, alanine-transaminase can transfer amino group from alanine to oxaloacetate to make
aspartate. Aspartate is not an essential amino acid = amino acids our metabolism can not make
and must be in our daily diet.

5. Both alanine and lactate have to be converted to pyruvate.

From lactate, it is the lactate dehydrogenase reaction (1 NADH), then pyruvate gets oxidized
by pyruvate dehydrogenase (1 NADH) and one turn of the CAC: yielding 3NADH, 1FADH 2 and
1 GTP. Converting NADH and FADH2 to ATPs we use 1 NADH = 2.5 ATP and 1 FADH 2 = 1.5
ATP. So for one lactate: (3+1+1)(2.5 ATP) + 1.5 ATP + 1 ATP = 15 ATP.
From alanine, it is the transaminase reaction, then pyruvate gets oxidized by pyruvate
dehydrogenase (1 NADH) and one turn of the CAC: yielding 3NADH, 1FADH 2 and 1 GTP.
Converting NADH and FADH2 to ATPs we use 1 NADH = 2.5 ATP and 1 FADH2 = 1.5 ATP. So
for one alanine: (3+1)(2.5 ATP) + 1.5 ATP + 1 ATP = 12.5 ATP.
But now it will cost some ATP to get rid of the amino group: so it would be half the energy
requirement of the urea cycle starting in the mitochondria: carbamoyl phosphate synthetase
(-2 ATP), argininosuccinate synthetase (-2 ATP) = -4 ATP / 2 = -2 ATP. So the real net gain is
12.5 ATP + (-2 ATP) = 10.5 ATP (Please note the answer in the text is not correct).

8. Why is it that aspartate aminotransferase has the highest activity of all mammalian liver
aminotransferases? Easy right? Half of all urea nitrogens come from aspartate.

11. Genetic defect seen in the patient (a 2 year old child ) lagging in development. Urinanalysis:
Substance
Phenylalanine
Phenylpyruvate
Phenyllactate

Concentration (mM)
Patients urine
Normal Urine
7.0
0.01
4.8
0
10.3
0

It is obvious that the patients urine is abnormally high in phenylalanine, and products typical of
phenylketonuria: phenylpyruvate and phenyllactate. So:
a. Deficient or missing enzyme: phenylalanie hydroxylase. Treatment: life long diet low in
phenylalanine.
b. Phenylalanine can not be recycled and accumulates.
c. Blood phenylalanine is transaminated to phenylpyruvate, and phenylpyruvate is reduced to
phenyllactate.
d. The white patches in his hair were due to lack of sufficient tyrosine (precursor to melanin,
the dark pigment in hair). Tyrosine in the product of phenylalanie hydroxylase. So, while there
may be tyrosine in the diet, it is not enough for expression of totally dark hair.