Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium.
Open Access
- 1 November 1988
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 263 (33) , 17857-17871
- https://doi.org/10.1016/s0021-9258(19)77913-7
Abstract
No abstract availableThis publication has 83 references indexed in Scilit:
- Identification of three sites of proteolytic cleavage in the hinge region between the two domains of the .beta.2 subunit of tryptophan synthase of Escherichia coli or Salmonella typhimuriumBiochemistry, 1986
- Comparison of the folding of 2-Keto-3-deoxy-6-phosphogluconate aldolase, triosephosphate isomerase and pyruvate kinaseJournal of Molecular Biology, 1982
- Kinetics of renaturation and self-assembly of intermediates on the pathway of folding of the β2-subunit of Escherichia coli tryptophan-synthetaseJournal of Molecular Biology, 1982
- The spatial organization of the active sites of the bifunctional oligomeric enzyme tryptophan synthase: Cross-linking by a novel methodBiochemical and Biophysical Research Communications, 1981
- Nucleotide sequence of the trpB gene in Escherichia coli and Salmonella typhimuriumJournal of Molecular Biology, 1980
- Dynamics of ligand binding to heme proteinsJournal of Molecular Biology, 1979
- The protein data bank: A computer-based archival file for macromolecular structuresJournal of Molecular Biology, 1977
- Atomic coordinates for triose phosphate isomerase from chicken muscleBiochemical and Biophysical Research Communications, 1976
- The exclusion of free indole as an intermediate in the biosynthesis of tryptophan in Neurospora crassaBiochimica et Biophysica Acta, 1958
- Furan MercurialsJournal of the American Chemical Society, 1933