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Essay / Research Paper Abstract
A 5 page review of the genteic and enzymatic causes for this potentially catastrophic condition. The author oulines the interventional techniques currently being employed. Caused by either a deficiency in the PAH enzymatic activity or a genetic mutation this condition, if left untreated, can result in brain damage and mental retardation in infants born to PAH mothers. Bibliography lists 5 sources.
Page Count:
5 pages (~225 words per page)
File: AM2_PPpheny2.rtf
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Unformatted sample text from the term paper:
potential for severe physiological impacts. An autosomal recessive genetic disorder, Phenylketonuria can result in brain damage and mental retardation if left untreated (Erlandsen, Patch, Gamez, Straub, and Stevens 385).
The condition is characterized by an enzyme deficiency that results in the bodys inability to metabolize phenylalanine to tyrosine. As a consequence, phenylalanine builds up adversely impacting physiological
function. In individuals without this condition, phynylalanine hydroxulase (PAH) (the enzyme that is deficient in individuals with Phenylketonuria):
"converts the essential amino acid L-phenylalanine (L-Phe) into L-tyrosine using the co-factor (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH^sub 4^) and molecular oxygen".
In normal physiological processes the catalysis provided by this iron-dependent enzyme results in the degradation of dietary L-Phe and accounts. This
process is responsible for an estimated seventy-five percent of the L-Phe that is discarded by the body (Erlandsen, Patch, Gamez, Straub, and Stevens, 2003).
In actuality, Phenylketonuria can be caused by either a deficiency in the PAH enzymatic activity or a genetic mutation (Erlandsen, Patch, Gamez, Straub, and Stevens 385).
Some four hundred mutations, in fact, are currently linked to Phenylketonuria or its milder form hyperphynylalaninemia (HPA) (Erlandsen, Patch, Gamez, Straub, and Stevens 385).
Structurally, phynalanine hydroxulase is quite varied as well. Truncated, three dimensional forms of phynylalanine hydroxulase (PAH) have been discovered with the use of X-ray crystallographic techniques (Erlandsen,
Patch, Gamez, Straub, and Stevens 385). Further understanding the various forms that phynalanine hydorxulase can take is helpful in that it will undoubtedly be useful in helping researchers predict
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