फेनिलॅलानिन,

phenylalanine's Usage Examples:

These enzymes primarily hydroxylate the amino acids L-phenylalanine, L-tyrosine, and L-tryptophan, respectively.

biosynthesis of cinnamaldehyde begins with deamination of L-phenylalanine into cinnamic acid by the action of phenylalanine ammonia lyase (PAL).

Five more are both ketogenic and glucogenic: phenylalanine, isoleucine, threonine, tryptophan and tyrosine.

amino acid hydroxylase enzymes, used in the degradation of amino acid phenylalanine and in the biosynthesis of the neurotransmitters serotonin (5-hydroxytryptamine.

that catalyzes a reaction converting L-phenylalanine to ammonia and trans-cinnamic acid.

Individuals with phenylketonuria (PKU) must keep their intake of phenylalanine - an essential amino.

of the O-O bond to yield the ferryl oxo hydroxylating intermediate Fe(IV)O attack on Fe(IV)O to hydroxylate phenylalanine substrate to tyrosine.

L-Tyrosine or tyrosine (symbol Tyr or Y) or 4-hydroxyphenylalanine is one of the 20 standard amino acids that are used by cells to synthesize proteins.

(Cys-Tyr-Phe-Gln-Asn-Cys-Pro-Arg-Gly-NH2, with isoleucine-3 of AVT changed to phenylalanine) and lysine vasopressin (isoleucine-3 changed to phenylalanine and arginine-8.

HGD appears in the metabolic pathway of tyrosine and phenylalanine degradation once the molecule homogentisate.

racemase, phenylalanine racemase (adenosine triphosphate-hydrolysing), gramicidin S synthetase I) is the enzyme that acts on amino acids and derivatives.

It is a methyl ester of the aspartic acid/phenylalanine dipeptide with the trade names NutraSweet, Equal, and Canderel.

classified as a hydrophobic amino acid, it is more hydrophilic than phenylalanine.

Synonyms:

essential amino acid,