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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.
The repressor protein binds to the operator in the presence of tryptophan (repressing transcription) and is released from the operon when tryptophan is absent (allowing transcription to proceed). The trp operon additionally uses attenuation to control expression of the operon , a second negative feedback control mechanism.
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.
Tryptophan repressor (or trp repressor) is a transcription factor involved in controlling amino acid metabolism. It has been best studied in Escherichia coli, where it is a dimeric protein that regulates transcription of the 5 genes in the tryptophan operon. [1]
Amino acid replacement is a change from one amino acid to a different amino acid in a protein due to point mutation in the corresponding DNA sequence. It is caused by nonsynonymous missense mutation which changes the codon sequence to code other amino acid instead of the original.
121278 216343 Ensembl ENSG00000139287 ENSMUSG00000006764 UniProt Q8IWU9 Q8CGV2 RefSeq (mRNA) NM_173353 NM_173391 RefSeq (protein) NP_775489 NP_775567 Location (UCSC) Chr 12: 71.94 – 72.19 Mb Chr 10: 114.91 – 115.02 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Tryptophan hydroxylase 2 (TPH2) is an isozyme of tryptophan hydroxylase found in vertebrates. In humans, TPH2 is ...