Structure and Function of the Tryptophan Synthase α2β2 Complex
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چکیده
منابع مشابه
Structure and Function of the Tryptophan Synthase a2b2 Complex
To probe the structural and functional roles of activesite residues in the tryptophan synthase a2b2 complex from Salmonella typhimurium, we have determined the effects of mutation of His in the b subunit. His is located adjacent to b subunit Lys, which forms an internal aldimine with the pyridoxal phosphate and catalyzes the abstraction of the a-proton of L-serine. The replacement of His by leu...
متن کاملThe 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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15 صفحه اولThe 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...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1999
ISSN: 0021-9258
DOI: 10.1074/jbc.274.51.36439