The tryptophan synthase β-subunit paralogs TrpB1 and TrpB2 inThermococcus kodakarensisare both involved in tryptophan biosynthesis and indole salvage
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A Novel Tryptophan Synthase -Subunit from the Hyperthermophile Thermotoga maritima
Tryptophan synthase catalyzes the last two steps in the biosynthesis of the amino acid tryptophan. The enzyme is an complex in mesophilic microorganisms. The -subunit (TrpA) catalyzes the cleavage of indoleglycerol phosphate to glyceraldehyde 3-phosphate and indole, which is channeled to the active site of the associated -subunit (TrpB1), where it reacts with serine to yield tryptophan. The Trp...
متن کاملTrpB2 enzymes are O-phospho-l-serine dependent tryptophan synthases.
The rapid increase of the number of sequenced genomes asks for the functional annotation of the encoded enzymes. We used a combined computational-structural approach to determine the function of the TrpB2 subgroup of the tryptophan synthase β chain/β chain-like TrpB1-TrpB2 family (IPR023026). The results showed that TrpB2 enzymes are O-phospho-l-serine dependent tryptophan synthases, whereas Tr...
متن کاملSynthesis of β-Branched Tryptophan Analogues Using an Engineered Subunit of Tryptophan Synthase.
We report that l-threonine may substitute for l-serine in the β-substitution reaction of an engineered subunit of tryptophan synthase from Pyrococcus furiosus, yielding (2S,3S)-β-methyltryptophan (β-MeTrp) in a single step. The trace activity of the wild-type β-subunit on this substrate was enhanced more than 1000-fold by directed evolution. Structural and spectroscopic data indicate that this ...
متن کاملCooperative fluctuations and subunit communication in tryptophan synthase.
Tryptophan synthase (TRPS), with linearly arrayed subunits alphabetabetaalpha, catalyzes the last two reactions in the biosynthesis of L-tryptophan. The two reactions take place in the respective alpha- and beta-subunits of the enzyme, and the intermediate product, indole, is transferred from the alpha- to the beta-site through a 25 A long hydrophobic tunnel. The occurrence of a unique ligand-m...
متن کاملThe Subunit Structure of Tryptophan Synthase from Neurospora crassa*
Tryptophan synthase of Neurospora crassa was purified to electrophoretic homogeneity from the wild type strain 74A which had been derepressed by the presence of 0.5 rnr,r indoleacrylic acid in the growth medium. The isolated material migrated as a single symmetrical peak in the ultracentrifuge with a sedimentation constant of 6.0 S. Gel filtration on Sephadex G-ZOO and conventional sedimentatio...
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ژورنال
عنوان ژورنال: FEBS Journal
سال: 2014
ISSN: 1742-464X
DOI: 10.1111/febs.12845