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Phenylalanine is a precursor for tyrosine, the monoamine neurotransmitters dopamine, norepinephrine (noradrenaline), and epinephrine (adrenaline), and the biological pigment melanin. It is encoded by the messenger RNA codons UUU and UUC. Phenylalanine is found naturally in the milk of mammals.
Its role in maintaining the balance of these aromatic amino acids in the cell is vital. [2] This is the single known example of a naturally occurring enzyme catalyzing a pericyclic reaction. [2] [nb 1] Chorismate mutase is only found in fungi, bacteria, and higher plants. Some varieties of this protein may use the morpheein model of allosteric ...
In plants, all phenylpropanoids are derived from the amino acids phenylalanine and tyrosine. Phenylalanine ammonia-lyase (PAL, a.k.a. phenylalanine/tyrosine ammonia-lyase) is an enzyme that transforms L-phenylalanine and tyrosine into trans-cinnamic acid and p-coumaric acid, respectively.
The enzyme phenylalanine ammonia lyase (EC 4.3.1.24) catalyzes the conversion of L-phenylalanine to ammonia and trans-cinnamic acid.: [1] L -phenylalanine = trans -cinnamate + NH 3 Phenylalanine ammonia lyase (PAL) is the first and committed step in the phenyl propanoid pathway and is therefore involved in the biosynthesis of the polyphenol ...
A cellular model is a mathematical model of aspects of a biological cell, for the purposes of in silico research. Developing such models has been a task of systems biology and mathematical biology .
In the experiment, an extract was prepared from bacterial cells that could make protein without the presence of intact living cells. An artificial form of RNA consisting entirely of uracil-containing nucleotides (polyuridylic acid or poly-U) was added to the extract, causing it to form a protein composed entirely of the amino acid phenylalanine.
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.
The classic FFAT motif was defined on the basis of finding the sequence EFFDAxE in 16 different eukaryotic cytoplasmic proteins (where E = glutamate, F = phenylalanine, D = aspartate, A = alanine, x = any amino acid, according to the single letter amino acid code (see Table of standard amino acid abbreviations and properties in amino acids).