Thermodynamic analysis reveals structural rearrangement during the acylation step in human trypsin 4 on 4-methylumbelliferyl 4-guanidinobenzoate substrate analogue*

HIGHLIGHTS

• who: Ju̕lia To̕th from the Júlia Tóth, Linda Gombos, Zoltán Simon, Péter Medveczky, László Szilágyi, László Gráf, and András Málnási-Csizmadia, From the Department of Biochemistry, Eötvös Loránd University, Pázmány Péter sétány, C, Budapest, Hungary Human trypsin , is an unconventional serine protease that possesses an arginine at position , in place of the highly conserved glycineAlthough this single amino acid substitution does not affect steady-state activity on small synthetic substrates, it has dramatic effects on zymogen . . .
  

   

  

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