Phenylalanine in a sentence

Biosynthesis As an essential amino acid, phenylalanine is not synthesized de novo in humans and other animals, who must ingest phenylalanine or phenylalanine-containing proteins.

DL -Phenylalanine is a mixture of D -phenylalanine and L -phenylalanine.

Phenylalanine and phenylketonuria High levels of the naturally-occurring essential amino acid phenylalanine are a health hazard to those born with phenylketonuria (PKU), a rare inherited disease that prevents phenylalanine from being properly metabolized.

A small amount of D -phenylalanine appears to be converted to L -phenylalanine.

Individuals who cannot metabolize phenylalanine must monitor their intake of protein to control the buildup of phenylalanine as their bodies convert protein into its component amino acids.

Some research on causes of TD suggests phenylalanine may trigger the muscle movements that characterize TD.

As with methanol and phenylalanine, intake of aspartic acid from aspartame is less than would be expected from other dietary sources.

Cancer cells take up these molecules at an increased rate because of an upregulation of transporters in the cancer cell, in this case amino acid transporters will bring in the L-arginine and L-phenylalanine functional groups of the fullerenes.

Concerns about the safety of phenylalanine from aspartame center largely on hypothetical changes in neurotransmitter levels as well as ratios of neurotransmitters to each other in the blood and brain that could lead to neurological symptoms.

Consumption of the protein substitute formulas can actually reduce phenylalanine levels, probably because it stops the process of protein catabolism from releasing Phe stored in the muscles and other tissues into the blood.

Dietary requirements and sources A recommended daily intake for phenylalanine and tyrosine is 25 mg per kilogram of body weight, or 11 mg per pound.

However, a blood test can reveal elevated phenylalanine levels after one or two days of normal infant feeding.

However, if PKU is diagnosed early enough, an affected newborn can grow up with normal brain development by managing and controlling phenylalanine ("Phe") levels through diet, or a combination of diet and medication.

However, if there is not enough of the PAH enzyme or its cofactor, then phenylalanine can build up in the blood and brain to toxic levels, affecting brain development and function.

If phenylalanine is in excess in the blood, it will saturate the transporter.

If this reaction does not take place, phenylalanine accumulates and tyrosine is deficient.

In Arabidopsis thaliana it can be synthesized via a phenylalanine-independent pathway.

In Lophophora williamsii ( Peyote ), dopamine converts into mescaline in a biosynthetic pathway involving m-O-methylation and aromatic hydroxylation. citation Tyrosine and phenylalanine serve as the metabolic precursors to synthesis of mescaline.

In people without PKU, the PAH enzyme breaks down any excess phenylalanine from these sources beyond what is needed by the body.

Lab results may report phenylalanine levels in different units, including mg/dL and μmol/L.