Subunit-subunit interaction of tryptophan synthase from hyperthermophile
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چکیده
منابع مشابه
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 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 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 کاملTryptophan Synthetase ,& Subunit
Radioactivity incorporated into an e-N-5’-phosphopyridoxyllysine residue of the /3 chain by reduction of the flZ holoenzyme with tritiated sodium borohydride appears in two tryptic peptides. These pyridoxyl peptides differ by only a single arginyl residue. As expected, tryptic digests of normal protein contain two peptides that together make up the pyridoxyl peptide region. The primary structur...
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ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 2000
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.40.s118_1