trypsinogen has been researched along with valylvaline* in 2 studies
2 other study(ies) available for trypsinogen and valylvaline
| Article | Year |
|---|---|
Binding of the Ile-Val and Val-Val effector dipeptides to the binary adducts of bovine trypsinogen with Kunitz and Kazal inhibitors as well as the acylating agent p-nitrophenyl p-guanidinobenzoate. A thermodynamic and kinetic study.
Thermodynamics and kinetics of binding of the Ile-Val and Val-Val effector dipeptides to the binary adducts of bovine trypsinogen with the bovine basic pancreatic trypsin inhibitor (BPTI, Kunitz inhibitor), the porcine pancreatic secretory inhibitor (PSTI, Kazal inhibitor) and the acylating agent p-nitrophenyl p-guanidinobenzoate have been investigated at pH 7.4 and 21(+/- 0.5) degrees C. The affinity of both effector dipeptides for bovine trypsinogen: BPTI and bovine trypsinogen: PSTI binary adducts is higher than that observed for the formation of the dipeptide: bovine trypsinogen: p-guanidinobenzoate ternary complexes; moreover, the affinity of Ile-Val for the zymogen binary adducts is higher than that observed for Val-Val association. Binding of Ile-Val and Val-Val to the bovine trypsinogen binary complexes conforms to the induced-fit model, which consists of a fast pre-equilibrium followed by intramolecular isomerization change(s), the latter fast pre-equilibrium followed by intramolecular isomerization change(s), the latter representing the rate-limiting first-order process. For the three bovine trypsinogen systems considered, the rate of the intramolecular isomerization change(s) is essentially independent of the nature of the dipeptide and of the proenzyme binary complex. Topics: Animals; Aprotinin; Benzoates; Cattle; Dipeptides; Kinetics; Thermodynamics; Trypsin Inhibitor, Kazal Pancreatic; Trypsin Inhibitors; Trypsinogen | 1987 |
The refined 2.2-A (0.22-nm) X-ray crystal structure of the ternary complex formed by bovine trypsinogen, valine-valine and the Arg15 analogue of bovine pancreatic trypsin inhibitor.
Large orthorhombic crystals of the complex formed by bovine trypsinogen and a semisynthetic homologous bovine pancreatic trypsin inhibitor with the reactive-site lysine residue replaced by an arginine residue [( Arg15]PTI) have been obtained which are isomorphous with the crystals of PTI-trypsinogen [Bode, W., Schwager, P. and Huber, R. (1978) J. Mol. Biol. 118, 99-112]. The X-ray crystal structure of the ternary complex of trypsinogen-[Arg15]PTI with the dipeptide Val-Val has been determined by X-ray data to 2.2-A (0.22-nm) resolution by means of difference Fourier methods and has been crystallographically refined to a final R-value of 0.17. Replacement of the reactive-site Lys15 by an arginine residue is accompanied in the complex by small movements of polar side groups of trypsin and enclosed solvent molecules within the specificity pocket. Only solvent molecule 414 OH which mediates the hydrogen bond interactions between Lys15 NZ and Asp189 carboxylate is expelled, thus allowing the bulkier guanidyl group to approach this carboxylate. The dipeptide Val-Val binds in the pocket accepting the Ile-Val N-terminus in trypsin. The cavity left by the CD-methyl group of Ile16 upon replacement by a valine residue is only partially filled by slight rearrangements of neighbouring peptide side chains. Part of the positive free energy change observed upon replacement of Ile-Val may allow for the maintenance of this cavity. Topics: Animals; Aprotinin; Binding Sites; Cattle; Dipeptides; Models, Molecular; Protein Binding; Trypsinogen; X-Ray Diffraction | 1984 |