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Clinical Biochemistry of Domestic Animals (Sixth Edition) - UMK ...

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V. Vitamin-Like Compounds<br />

727<br />

4 . Taurine<br />

Although taurine is not generally considered a vitamin, the<br />

requirement for taurine by some animals is <strong>of</strong> the similar<br />

order as choline. Taurine, 2-aminoethanesulfonic acid,<br />

is present in all animal tissues and is one <strong>of</strong> the principal<br />

free amino acids. Some tissues such as the retina, olfactory<br />

bulb, and granulocytes have particularly high concentrations<br />

<strong>of</strong> taurine. Many animals use taurine or glycine as a<br />

conjugate for the bile acids. Some <strong>of</strong> the taurine excreted in<br />

the bile is returned to the liver in the enterohepatic circulation<br />

(MacDonald et al., 1984). Most animals can synthesize<br />

adequate amounts <strong>of</strong> taurine from the oxidation <strong>of</strong> cysteine;<br />

however, some animals, particularly domesticated and<br />

wild felids, and human infants do not synthesize adequate<br />

amounts <strong>of</strong> taurine. Dogs normally synthesize adequate<br />

amounts <strong>of</strong> taurine; however, when they are given low-sulfur<br />

amino acid diets, taurine may become limiting. Taurine deficiency<br />

occurs in cats when the diet does not contain adequate<br />

amounts <strong>of</strong> the amino acid. Defective synthesis in cats<br />

is a result <strong>of</strong> low activity <strong>of</strong> two enzymes in the synthetic<br />

pathway: cysteine dioxygenase and cysteine sulfinic acid<br />

decarboxylase and an obligatory requirement for taurine to<br />

conjugate bile acids. A wide array <strong>of</strong> clinical signs has been<br />

described in taurine-deficient cats including central retinal<br />

degeneration, reversible dilated cardiomyopathy, reproductive<br />

failure in queens, teratogenic defects, and abnormal<br />

brain development in kittens (MacDonald et al., 1984).<br />

Dietary concentrations <strong>of</strong> taurine required to maintain<br />

adequate levels in plasma and whole blood <strong>of</strong> cats are a<br />

function <strong>of</strong> type <strong>of</strong> diet, which affects the degree <strong>of</strong> microbial<br />

degradation that occurs in the enterohepatic circulation.<br />

For most expanded diets 1g taurine/kg is adequate,<br />

but canned diets may require concentrations up to 2.5 g<br />

taurine/kg dry matter.<br />

Plasma and whole blood concentrations <strong>of</strong> 40 and<br />

300 μ M <strong>of</strong> taurine appear to be adequate in cats for reproduction,<br />

which is the most demanding physiological state<br />

for taurine (MacDonald et al., 1984).<br />

B . Other Vitamin-Like Compounds<br />

The following compounds are highlighted because <strong>of</strong> their<br />

known role as coenzymes in prokaryotes and potential role<br />

as probiotics (growth- promoting substances) in higher animals.<br />

These compounds include queuosine coenzyme Q,<br />

pteridines (other than folic acid), such as biopterin and the<br />

pteridine c<strong>of</strong>actor for the Mo-Fe flavoproteins, lipoic acid,<br />

and pyrroloquinoline quinone (PQQ).<br />

1 . Queuosine<br />

Queuosine is included because it represents a known and novel<br />

product arising from a microbe-host interaction. Queuine is<br />

the nucleoside base, which is modified to queuosine.<br />

Queuosine resembles guanidine and is preferably utilized<br />

in some t-RNAs. The importance <strong>of</strong> this interaction has yet<br />

to be fully understood. Germ-free animals survive without<br />

a source <strong>of</strong> queuine or queuosine ( Farkas, 1980 ).<br />

2 . Coenzyme Q<br />

Although claims have been made for a nutrition requirement<br />

for coenzyme Q, more work is needed to fully clarify<br />

a true nutritional role for this compound. Ubiquinone<br />

or coenzyme Q is found in mitochondria. Coenzyme Q<br />

is structurally similar to vitamins E and K. As a quinone,<br />

coenzyme Q is ideally suited to interact with cytochromes<br />

to affect the flow <strong>of</strong> electrons in the mitochondrial respiratory<br />

chain. Coenzyme Q can be synthesized and is easily<br />

absorbed from the intestine by the same route as other fatsoluble<br />

vitamins. However, there is no known requirement<br />

for coenzyme Q in higher animals.<br />

Of the lipophilic substances with redox cycling capacity,<br />

the ubiquinones (coenzyme Q) are a group <strong>of</strong> ubiquitous<br />

2,3-dimethoxy-5-methyl benzoquinones substituted at the<br />

position 6 with terpenoid chains <strong>of</strong> varying lengths. In mitochondria,<br />

coenzyme Q causes two electron processes and<br />

helps initiate two single electron transfers through semiquinone<br />

intermediates. Coenzyme Q is found mainly in the<br />

mitochondrial intermembrane. Although there is no apparent<br />

dietary requirement, coenzyme Q is present in food and<br />

promoted for various putative health benefits. Coenzyme<br />

Q that is absorbed from the intestine is transported by the<br />

same transport system as vitamin E and vitamin K.<br />

3 . Pteridines<br />

In animals, tetrahydrobiopterin (commonly abbreviated<br />

BH 4 ) is an important redox c<strong>of</strong>actor, best known for its<br />

role at the catalytic site for phenylalanine and tyrosine<br />

hydroxylases. Tetrahydrobiopterin is made in sufficient<br />

quantities from pathways related to guanine synthesis. A<br />

related c<strong>of</strong>actor is the molybdenum c<strong>of</strong>actor, also in the<br />

pterin family, a c<strong>of</strong>actor for xanthine oxidase and aldehyde<br />

oxidase (important to purine metabolism) and sulfite oxidase<br />

(important in sulfur amino acid metabolism; see the<br />

Molybdenum section in Chapter 22 ) .<br />

4 . Lipoic Acid<br />

Lipoic acid (LA) is made in the liver <strong>of</strong> most animals. This<br />

coenzyme is linked by amide linkage to lysyl residues<br />

within transacetylases ( Fuchs and Zimmer, 1997 ). Lipoyl<br />

moieties functions in the transfer <strong>of</strong> electrons and activated<br />

acyl groups from the thiazole-moiety <strong>of</strong> thiamin pyrophosphate<br />

to CoASH. In this process, the disulfide bond is broken<br />

and dihydrolipoyl transiently generated. Reoxidation<br />

is required to reinitiate this cycle. Although most reactions<br />

in biological systems may be described as nucleophilic in

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