3.4.21.4: trypsin

P00760

95461

analysis of membrane crystallization technique of benzamidine inhibited enzyme. Study on parameters to gain high control on the final properties of the crystalline material

670043

batch crystallization method, with 4 mM CaCl2, 90 mM benzamidine and 2.1 M ammonium sulfate

679658

comparison of five crystals of bovine trypsin obtained under analogous conditions. The Calpha and backbone atoms of the structures superpose very well. The occupancy of ligands in regions of low thermal motion is reproducible, whereas solvent molecules containing heavier atoms (such as sulfur) or those located on the surface can differ significantly. The coordination lengths of the calcium ion are conserved. A large proportion of the multiple conformations refine to similar occupancies and the residues adopt similar orientations. The protonation states of histidine residues and carboxylate moieties is consistent for all of the models. However, several features of residues or ligands located in flexible parts of the macromolecule may vary significantly, such as side-chain orientations and the occupancies of certain fragments

P00760

731053

crystal structure of cancer chemopreventive Bowman-Birk inhibitor in ternary complex with bovine trypsin at 2.3 A resolution

652815

crystal structure of the enzyme-benzylamine complex, enzyme-phenylethylamine complex and the enzyme-phenylbutylamine complex

653809

crystallization of the mutant enzyme E97N/Y99L/S190A in presence of the inhibitors benzamidine, [4-(6-chloro-naphthalene-2-sulfonyl)-piperazin-1-yl]-(3,4,5-6-tetrahydro-[2H-1,4']bipyridinyl-4yl)-methanone or 2,7-bis(4-amidinobenzylidene)cycloheptan-1-one

650468

hanging drop vapour diffusion method, trypsin complexed with p-amidinosalicylidene-L-alaninato(aqua)copper(II), m-amidinosalicylidene-L-alaninato(aqua)copper(II), bis(p-amidinosalicylidene-L-alaninato)iron(III) or bis(m-amidinosalicylidene-L-alaninato)iron(III). X-ray crystallographic analyses of complexes between bovine beta-trypsin and Schiff base copper(II) or iron(III) chelates

hanging-drop method

in complex with Sagittaria sagittifolia arrowhead protease inhibitor API-A, sitting drop vapour diffusion method, using 0.1 M sodium cacodylate pH 6.5, 0.2 M ammonium sulfate, and 20% PEG 8000

695341

Kunitz domain 1, KD1, of tissue factor pathway inhibitor-2 in complex with trypsin

669362

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

717850

X-ray crystal structure of beta-trypsin and alpha-trypsin

a series of crystal structures of trypsin, containing either an autoproteolytic cleaved peptide fragment or a covalently bound inhibitor. Cocrystallization with PMSF or DFP

P35049

652472

analysis of structures at three different pH-values and two different temperatures, comparison with more trypsin structures

667047

in complex with Locusta migratoria protease inhibitor 3, hanging drop vapour diffusion method, using 0.1 M sodium citrate pH 4.9 and 24% PEG 4000

695318

sitting-drop vapour-diffusion method, X-ray studies of trypsin with its own autolysis products and in presence of the added amino acids arginine, lysine and glutamate

P35049

649167

vapour diffusion method, crystal structure of the enzyme in complex with 1b, 1cMe, 1d and 1dAc

Saccharopolyspora erythraea

652872

structure of the enzyme-benzamidine complex determined at 1.8 A resolution

crystals of variant X99rT containing the 99-loop (Glu97, Tyr99) of factor Xa, and variant X(99/175/190)rT containing the 99-loop the 175-loop (Ser172, Ser173, Phe174, Ile175) and Ala190 of factor Xa obtained in presence of benzamidine

Rattus norvegicus

652902

X-ray crystal structure of trypsin R96H at pH 8.0 in the presence of CuCl2

Rattus norvegicus

95450

95439

structure of unmodified, unliganded trypsin crystallized at physiological pH, to 0.81 A resolution. Comparisons of the catalytic triad confirm the conserved position of the catalytic residues in an unoccupied active site, and demonstrate great mobility of the catalytic serine. The two conformations of the catalytic serine show some conformational fluidity in the active site of unliganded trypsin. The hydrogen-bonding network between the residues of the catalytic triad and neighbouring bonding partners is seen in the majority of serine protease structures determined to date, implying that much of this network is maintained in the unliganded state

Saccharopolyspora erythraea

P24664

731072

crystal structure of the enzyme-benzylamine complex, enzyme-phenylethylamine complex and the enzyme-phenylpropylamine complex

salmon

653809

hanging-drop method

salmon

649162

Streptomyces griseus

95433

FX99 mutant of trypsin, hanging drop vapour diffusion method, using 1.6 M ammonium sulfate

Streptomyces griseus

699531

hanging drop vapour diffusion method, recombinant wild-type enzyme and mutant enzyme T190P at 1.5 and 1.9 A resolution

crystal structure of epsilon-trypsin

95448

enzyme in complex with Tamarindus indica trypsin inhibitor, sitting drop vapour diffusion method, at 20°C, mixing of 0.002 ml of 5 mg/ml protein solution with 0.002 ml of precipitant solution containing 4 M ammonium acetate and 0.1 M sodium acetate trihydrate, pH 4.6, X-ray diffraction structure determination and analysis at 2.0 A resolution, presence of one unit of inhibitor-trypsin complex per asymmetric unit

706963

in complex with heterochiral peptide t-butyloxycarbonyl-L-Pro-D-Asp-alpha-methyl-alanyl-L-Leu-L-Ala-NHMe. Peptide does not bind at active site but is located in the interstitial region, and interacts with the calcium-binding loop

669538

molecular dynamic simulation to study trypsin with and without a six-aminoacid peptide bound in the solvents water, acetonitrile and hexane. The enzyme is more compact and less native-like in hexane than in the other two polar solvents. The substrate can stabilize the native protein structure in the two polar media, but not in the nonpolar hexane. There are no significant differences in the conformation of the S1 pocket upon the substrate binding in water and acetonitrile media while a reverse behavior is observed in hexane media, implying a possible induced fit binding mechanism in the non-polar media. The substrate binding enhances the stability of catalytic H-bond network. The enzyme and the substrate appear to be more appropriate to the reactive conformation in the organic solvents compared with aqueous solution. There is much greater substrate binding strength in hexane media than the water and acetonitrile ones

P00761

732354

sitting drop vapor diffusion method. Crystals of porcine trypsin are prepared with either a vacant S1-subsite or with the S1-subsite occupied by one of three alcohols, slected for their properties as substrate analogues: guanidine-3-propanol, 4-aminobutanol and p-hydroxymethylbenzamidine

P00761

650242

sitting-drop vapour diffusion method, crystals of beta-trypsin-bdellastasin complex. Deamination, isomerization and racemization of Asn115 is the key step in crystallization

649124

vapour-diffusion hanging-drop technique, crystal structures of trypsin in presence of varying concentrations of polydocanol. Polydocanol binds to the protein with its hydrophilic head. There are at least 11 binding sites for polydocanol in trypsin. The hydrophilic binding of polydocanol results in cross-linked pairs of trypsin molecules