Characterization of the putative tryptophan synthase β-subunit from Mycobacterium tuberculosis
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چکیده
منابع مشابه
A small-molecule allosteric inhibitor of Mycobacterium tuberculosis tryptophan synthase.
New antibiotics with novel targets are greatly needed. Bacteria have numerous essential functions, but only a small fraction of such processes-primarily those involved in macromolecular synthesis-are inhibited by current drugs. Targeting metabolic enzymes has been the focus of recent interest, but effective inhibitors have been difficult to identify. We describe a synthetic azetidine derivative...
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 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...
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 mM 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-200 AND CONVENTIONAL SEDIMENTATION E...
متن کاملA 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...
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ژورنال
عنوان ژورنال: Acta Biochimica et Biophysica Sinica
سال: 2009
ISSN: 1745-7270,1672-9145
DOI: 10.1093/abbs/gmp017