Structural Basis for Catalysis by Tryptophan Synthase
- 1 January 1991
- book chapter
- Published by Wiley
- Vol. 64, 93-172
- https://doi.org/10.1002/9780470123102.ch3
Abstract
No abstract availableKeywords
This publication has 167 references indexed in Scilit:
- 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
- Studies of the function and location of two cysteines in the β2 subunit of tryptophan synthaseBiochemical and Biophysical Research Communications, 1978
- The protein data bank: A computer-based archival file for macromolecular structuresJournal of Molecular Biology, 1977
- A new type of pyridoxal-p enzyme catalyzed reaction: The conversion of β, γ-unsaturated amino acids to saturated α-keto acids by tryptophan synthaseBiochemical and Biophysical Research Communications, 1975
- Evidence that the essential, photosensitive histidyl residue in the β2 subunit of tryptophan synthetase is in the pyridoxyl peptideBiochemical and Biophysical Research Communications, 1974
- Nucleation, Rapid Folding, and Globular Intrachain Regions in ProteinsProceedings of the National Academy of Sciences, 1973
- The 8 protein of Escherichia coli tryptophan synthetase II. New β-elimination and β-replacement reactionsBiochemical and Biophysical Research Communications, 1971