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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.
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5-HTP is produced from the amino acid tryptophan through the action of the enzyme tryptophan hydroxylase. Tryptophan hydroxylase is one of the biopterin-dependent aromatic amino acid hydroxylases. Production of 5-HTP is the rate-limiting step in 5-HT (serotonin) synthesis. 5-HTP is normally rapidly converted to 5-HT by amino acid decarboxylase. [1]
Tryptophan 2,3-dioxygenase is a heme-containing cytosolic enzyme encoded by gene TDO2. [5] Crystallographic studies of Xanthomonas campestris TD) [13] and Ralstonia metallidurans TDO) [16] have revealed that their structures are essentially identical and are intimately associated homotetrameric enzymes. [17]
Familial hypertryptophanemia has an autosomal recessive pattern of inheritance.. Hypertryptophanemia is believed to be inherited in an autosomal recessive manner. [2] This means a defective gene responsible for the disorder is located on an autosome, and two copies of the defective gene (one inherited from each parent) are required in order to be born with the disorder.
The complete data for Tryptophan. General information. Chemical formula: C 11 H 12 N 2 O 2 ...
After preliminary investigation revealed that the outbreak was linked to intake of tryptophan, the U.S. Food and Drug Administration (FDA) recalled tryptophan supplements in 1989 and banned most public sales in 1990, [9] [33] [34] with other countries following suit. This FDA restriction was loosened in 2001, and fully lifted in 2005.
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]