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Literature summary for 4.2.1.20 extracted from

  • Asada, Y.; Sawano, M.; Ogasahara, K.; Nakamura, J.; Ota, M.; Kuroishi, C.; Sugahara, M.; Yutani, K.; Kunishima, N.
    Stabilization mechanism of the tryptophan synthase alpha-subunit from Thermus thermophilus HB8: X-ray crystallographic analysis and calorimetry (2005), J. Biochem., 138, 343-353.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BL21(DE3) Thermus thermophilus

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of alpha-subunit of tryptophan synthase, oil batch method, discussion of the thermostabilization mechanism of the tryptophan synthase alpha-subunit on the basis of crystal structures and DSC data of the alpha-subunit orthologs from mesophilic, extreme thermophilic, and hyperthermophilic organisms Thermus thermophilus

Organism

Organism UniProt Comment Textmining
Thermus thermophilus Q5SJC0 HB8
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Thermus thermophilus HB8 / ATCC 27634 / DSM 579 Q5SJC0 HB8
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Purification (Commentary)

Purification (Comment) Organism
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Thermus thermophilus