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Literature summary for 3.4.21.4 extracted from

  • Page, M.J.; Carrell, C.J.; Di Cera, E.
    Engineering protein allostery: 1.05 A resolution structure and enzymatic properties of a Na+-activated trypsin (2008), J. Mol. Biol., 378, 666-672.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
FX99 mutant of trypsin, hanging drop vapour diffusion method, using 1.6 M ammonium sulfate Streptomyces griseus

Protein Variants

Protein Variants Comment Organism
additional information the FX99 mutant is constructed using 19 replacements in wild type trypsin with residues present in FXa; i.e. N95T/G96K/T97E/insertionT98/insertionY99 in the 99-loop, A171S/Y172S/G173S/N174F/E175I/E180M in the 170-loop, DELTAP185/G186K/G187Q/V188E in the 186-loop, and Y217E/P222K/Y224K/P225Y in the 220-loop Streptomyces griseus

Metals/Ions

Metals/Ions Comment Organism Structure
Na+ Na+ activation is interwoven with substrate selectivity in the trypsin scaffold Streptomyces griseus

Organism

Organism UniProt Comment Textmining
Streptomyces griseus
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