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Phenylalanine ball and stick model spinning. Phenylalanine (symbol Phe or F) [3] is an essential α-amino acid with the formula C 9 H 11 NO 2.It can be viewed as a benzyl group substituted for the methyl group of alanine, or a phenyl group in place of a terminal hydrogen of alanine.
Six amino acids are non-essential (dispensable) in humans, meaning they can be synthesized in sufficient quantities in the body. These six are alanine , aspartic acid , asparagine , glutamic acid , serine , [ 2 ] and selenocysteine (considered the 21st amino acid).
This metabolic pathway is nonexistent in the healthy body, but becomes important after peripheral l-DOPA administration in patients with Parkinson's disease or in the rare cases of patients with AADC enzyme deficiency. [11] l-Phenylalanine, l-tyrosine, and l-DOPA are all precursors to the biological pigment melanin.
Tyrosine (and its precursor phenylalanine) are precursors of the catecholamine neurotransmitters dopamine, epinephrine and norepinephrine and various trace amines. Phenylalanine is a precursor of phenethylamine and tyrosine in humans. In plants, it is a precursor of various phenylpropanoids, which are important in plant metabolism.
Since they are not synthesized in the human body, they must be derived from the diet. Tyrosine is semi-essential; therefore, it can be synthesized by the animal, but only from phenylalanine. Phenylketonuria, a genetic disorder that occurs as a result of the inability to breakdown phenylalanine, is due to a lack of the enzyme phenylalanine ...
In mammals it is created from -lactate and L-phenylalanine by the cytosol nonspecific dipeptidase (CNDP2) protein. [1] It is classified as N-acyl-alpha-amino acid and pseudodipeptide. [11] It has also been reported that as an additive, N-L-lactoyl phenylalanine improves the taste of food, conferring an umami flavor [12].
Phenylalanine: F Phe Essential for humans, phenylalanine, tyrosine, and tryptophan contain a large, rigid aromatic group on the side chain. These are the biggest amino acids. Like isoleucine, leucine, and valine, these are hydrophobic and tend to orient towards the interior of the folded protein molecule. Phenylalanine can be converted into ...
Phenylalanine hydroxylase (PAH) (EC 1.14.16.1) is an enzyme that catalyzes the hydroxylation of the aromatic side-chain of phenylalanine to generate tyrosine.PAH is one of three members of the biopterin-dependent aromatic amino acid hydroxylases, a class of monooxygenase that uses tetrahydrobiopterin (BH 4, a pteridine cofactor) and a non-heme iron for catalysis.