Tryptophan synthase or tryptophan synthetase is an enzyme (EC 4.2.1.20) that catalyses the final two steps in the biosynthesis of tryptophan. It is commonly found in Eubacteria, Archaebacteria, Protista, Fungi, and Plantae. However, it is absent from Animalia. It is typically found as an α2β2 tetramer. The α subunits … See more Subunits: Tryptophan synthase typically exists as an α-ββ-α complex. The α and β subunits have molecular masses of 27 and 43 kDa respectively. The α subunit has a TIM barrel conformation. The β subunit has a fold type II … See more Tryptophan synthase is commonly found in Eubacteria, Archaebacteria, Protista, Fungi, and Plantae. It is absent from animals such as … See more As humans do not have tryptophan synthase, this enzyme has been explored as a potential drug target. However, it is thought that … See more Tryptophan synthase was the first enzyme identified that had two catalytic capabilities that were extensively studied. It was also the first identified to utilize substrate channeling. As such, this enzyme has been studied extensively and is the subject of great interest. See more α subunit reaction: The α subunit catalyzes the formation of indole and G3P from a retro-aldol cleavage of IGP. The αGlu49 and αAsp60 are … See more Tryptophan synthetase is also known to accept indole analogues, e.g., fluorinated or methylated indoles, as substrates, generating the corresponding tryptophan analogues. See more It is thought that early in evolution the trpB2 gene was duplicated. One copy entered the trp operon as trpB2i allowing for its expression with trpA. TrpB2i formed transient complexes … See more WebMar 1, 2007 · Tryptophan synthase beta chain 1, chloroplastic (UniProt - P14671) Similar Articles . To arrive at the top five similar articles we use a word-weighted algorithm to …
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WebFeb 20, 2013 · My independent research at the National Institutes of Health (NIH) since 1966 has focused on the bacterial tryptophan synthase α2β2 complex. The β subunit catalyzes … WebAug 6, 2015 · The Trp-independent route was originally based on data from Trp auxotrophs that have mutations in genes encoding either the α- or β-subunits of Trp synthase. The α … books mla format
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