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Download QR code; Print/export ... The complete data for Tryptophan ... Structure. Crystal data: Spectral data. UV-Vis: IR: NMR: MS
Tryptophan ball and stick model spinning. 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.
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]
Tryptophan hydroxylase (TPH) is an enzyme (EC 1.14.16.4) involved in the synthesis of the monoamine neurotransmitter serotonin. Tyrosine hydroxylase , phenylalanine hydroxylase , and tryptophan hydroxylase together constitute the family of biopterin-dependent aromatic amino acid hydroxylases .
A data structure known as a hash table.. In computer science, a data structure is a data organization and storage format that is usually chosen for efficient access to data. [1] [2] [3] More precisely, a data structure is a collection of data values, the relationships among them, and the functions or operations that can be applied to the data, [4] i.e., it is an algebraic structure about data.
Later studies proposed that the reaction involves a condensation process, where glyoxylic acid combines with the indole group of tryptophan to form a complex quinonoid structure. This process explains the strong color change observed in the test and has been key to understanding tryptophan's chemical properties and its function in proteins.
TPH1 was first discovered to support serotonin synthesis in 1988 by converting tryptophan into 5-hydroxytryptophan. [6] It was thought that there only was a single TPH gene until 2003. A second form was found in the mouse ( Tph2 ), rat and human brain ( TPH2 ) and the original TPH was then renamed to TPH1.
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.