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Literature summary for 4.2.1.20 extracted from

  • Wintrode, P.L.; Rojsajjakul, T.; Vadrevu, R.; Matthews, C.R.; Smith, D.L.
    An obligatory intermediate controls the folding of the alpha-subunit of tryptophan synthase, a TIM barrel protein (2005), J. Mol. Biol., 347, 911-919.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Renatured (Commentary)

Renatured (Comment) Organism
the refolding of urea-denatured alpha-subunit of tryptophan synthase from Escherichia coli is monitored by pulse-quench hydrogen exchange mass spectrometry. An intermediate builds up rapidly and decays slowly over the first 100 seconds of folding, obligatory nature of the intermediate, the latter stages of the folding reaction of alpha-subunit of tryptophan synthase are under thermodynamic control Escherichia coli