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Coordinated Network Changes Across the Catalytic Cycle of Alpha Tryptophan Synthase

https://doi.org/10.2139/ssrn.3231858
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Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1016/0003-9861(92)90047-zopenalex-extracted
Thermal stabilities of mutant Escherichia coli tryptophan synthase α subunits
inferredcites →https://doi.org/10.1016/0040-6031(90)80386-dopenalex-extracted
Scanning calorimetric study of tryptophan synthase α-subunits from Escherichia coli, Salmonella typhimurium, and an interspecies hybrid
inferredcites →https://doi.org/10.1016/j.jmb.2006.12.005openalex-extracted
A Tightly Packed Hydrophobic Cluster Directs the Formation of an Off-pathway Sub-millisecond Folding Intermediate in the α Subunit of Tryptophan Synthase, a TIM Barrel Protein
inferredcites →https://doi.org/10.1016/s0021-9258(18)54910-3openalex-extracted
Enzymatic properties of mutant Escherichia coli tryptophan synthase alpha-subunits.
inferredcites →https://doi.org/10.1016/s0021-9258(18)66610-4openalex-extracted
In vitro mutagenesis and overexpression of the Escherichia coli trpA gene and the partial characterization of the resultant tryptophan synthase mutant alpha-subunits.
inferredcites →https://doi.org/10.1016/s0021-9258(18)68348-6openalex-extracted
Evidence that glutamic acid 49 of tryptophan synthase alpha subunit is a catalytic residue. Inactive mutant proteins substituted at position 49 bind ligands and transmit ligand-dependent to the beta subunit.
inferredcites →https://doi.org/10.1016/s0021-9258(19)76444-8openalex-extracted
Tryptophan synthase alpha subunit glutamic acid 49 is essential for activity. Studies with 19 mutants at position 49.
inferredcites →https://doi.org/10.1021/bi00072a011openalex-extracted
Mutagenic analysis of the interior packing of an .alpha./.beta. barrel protein. Effects on the stabilities and rates of interconversion of the native and partially folded forms of the .alpha. subunit of tryptophan synthase
inferredcites →https://doi.org/10.1021/bi00431a018openalex-extracted
Effects of multiple replacements at a single position on the folding and stability of dihydrofolate reductase from Escherichia coli
inferredcites →https://doi.org/10.1021/bi00548a004openalex-extracted
Effect of single amino acid substitutions on the thermal stability of the .alpha. subunit of tryptophan synthase
inferredcites →https://doi.org/10.1021/bi951726oopenalex-extracted
Mutagenic and Thermodynamic Analyses of Residual Structure in the α Subunit of Tryptophan Synthase
inferredcites →https://doi.org/10.1021/ja501602topenalex-extracted
Amino Acid Networks in a (β/α)8 Barrel Enzyme Change during Catalytic Turnover
inferredcites →https://doi.org/10.1110/ps.062704507openalex-extracted
Long‐range side‐chain–main‐chain interactions play crucial roles in stabilizing the (βα)8 barrel motif of the alpha subunit of tryptophan synthase
inferredcites →https://doi.org/10.1128/jb.173.6.1886-1893.1991openalex-extracted
Relative activities and stabilities of mutant Escherichia coli tryptophan synthase alpha subunits
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