Subunit Assembly in the Tryptophan Synthase α2β2 Complex
نویسندگان
چکیده
منابع مشابه
The tryptophan synthase α2β2 complex: a model for substrate channeling, allosteric communication, and pyridoxal phosphate catalysis.
I reflect on my research on pyridoxal phosphate (PLP) enzymes over fifty-five years and on how I combined research with marriage and family. My Ph.D. research with Esmond E. Snell established one aspect of PLP enzyme mechanism. My postdoctoral work first with Hans L. Kornberg and then with Alton Meister characterized the structure and function of another PLP enzyme, l-aspartate β-decarboxylase....
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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...
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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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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...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1995
ISSN: 0021-9258
DOI: 10.1074/jbc.270.14.7944