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Literature summary for 4.2.1.20 extracted from

  • Vadrevu, R.; Wu, Y.; Matthews, C.R.
    NMR analysis of partially folded states and persistent structure in the alpha subunit of tryptophan synthase: implications for the equilibrium folding mechanism of a 29-kDa TIM barrel protein (2008), J. Mol. Biol., 377, 294-306.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information hydrogen-to-deuterium exchange in alpha-tryptophan synthase Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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BL21(DE3)
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Subunits

Subunits Comment Organism
More (betaalpha)8 TIM barrel protein Escherichia coli

Synonyms

Synonyms Comment Organism
tryptophan synthase
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Escherichia coli