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Literature summary for 3.4.21.4 extracted from

  • Wahlgren, W.Y.; Pal, G.; Kardos, J.; Porrogi, P.; Szenthe, B.; Patthy, A.; Graf, L.; Katona, G.
    The catalytic aspartate is protonated in the Michaelis complex formed between trypsin and an in vitro evolved substrate-like inhibitor: a refined mechanism of serine protease action (2011), J. Biol. Chem., 286, 3587-3596.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
purified enzyme in complex with T5E/N18R/T20G/P21S/T22D/K31M mutant Schistocerca gregaria protease (trypsin) inhibitor 1, hanging drop vapor diffusion method, mixing of protein solution, containing 9.1 mg/ml protein complex in 0.5 mM MES, pH 6.0, and precipitant solution, containing 30% PEG 4000, 0.3 M ammonium acetate, 0.1 M sodium acetate, pH 4.6, in a 1:2.5 molar ratio, equilibration against precipitation solution, X-ray diffraction structure determination and analysis at 0.93 A resolution. modeling Bos taurus

Inhibitors

Inhibitors Comment Organism Structure
T5E/N18R/T20G/P21S/T22D/K31M mutant Schistocerca gregaria protease (trypsin) inhibitor 1 the mutant inhibitor is improved compared to the wild-type inhibitor protein Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
further purification of the commercial preparation by gel filtration Bos taurus

Reaction

Reaction Comment Organism Reaction ID
preferential cleavage: Arg-/-, Lys-/- catalytic mechanism involving both His57 and Asp102, overview Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
Bos taurus
-

General Information

General Information Comment Organism
additional information detailed geometry of the active site and the protonation state of catalytic residues, quantum chemical interpretation, overview Bos taurus