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Tryptophan (symbol Trp or W) [3] is an α-amino acid that is used in the biosynthesis of proteins.Tryptophan contains an α-amino group, an α-carboxylic acid group, and a side chain indole, making it a polar molecule with a non-polar aromatic beta carbon substituent.
Tryptophan synthase or tryptophan synthetase is an enzyme (EC 4.2.1.20) that catalyzes the final two steps in the biosynthesis of tryptophan. [1] [2] It is commonly found in Eubacteria, [3] Archaebacteria, [4] Protista, [5] Fungi, [6] and Plantae. [7] However, it is absent from Animalia. [8] It is typically found as an α2β2 tetramer.
An aromatic amino acid is an amino acid that includes an aromatic ring. Phenylalanine Among the 20 standard amino acids , histidine , phenylalanine , tryptophan , tyrosine , are classified as aromatic.
The reaction relies on the interaction between glyoxylic acid and the indole ring of the amino acid tryptophan, a structural feature found in most proteins. When proteins are exposed to concentrated sulfuric acid and glyoxylic acid, the indole group undergoes a reaction that produces a highly colored compound.
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Pistachios. Pistachios have 6 grams of protein per ounce, and hold the distinction of being the only nut that’s a complete protein.Complete proteins contain all nine essential amino acids the ...
Structure of the trp operon. The trp operon is a group of genes that are transcribed together, encoding the enzymes that produce the amino acid tryptophan in bacteria. The trp operon was first characterized in Escherichia coli, and it has since been discovered in many other bacteria. [1]
Indole is produced via anthranilate and reacts further to give the amino acid tryptophan. As an intercellular signal molecule , indole regulates various aspects of bacterial physiology, including spore formation, plasmid stability, resistance to drugs , biofilm formation, and virulence . [ 11 ]