the enzyme shows preference for Phe and His over Leu, Ile, Val, Arg, and Lys. Peptides with positively charged amino acids Arg and Lys or aliphatic amino acids Leu, Ile, and Val are all poor substrates, 2-aminobenzoyl-KLIPSKQ-[N-(2,4-dinitrophenyl)-ethylenediamine], 2-aminobenzoyl-KLWPSKQ-[N-(2,4-dinitrophenyl)-ethylenediamine], 2-aminobenzoyl-KLVSSKQ-[N-(2,4-dinitrophenyl)-ethylenediamine], 2-aminobenzoyl-KLISSKQ-[N-(2,4-dinitrophenyl)-ethylenediamine], 2-aminobenzoyl-KLWSSKQ-[N-(2,4-dinitrophenyl)-ethylenediamine], and 2-aminobenzoyl-KLPSSKQ-[N-(2,4-dinitrophenyl)-ethylenediamine] are resistant to hydrolysis
a substantial decrease of the SGP catalytic efficiency (kcat/Km) is observed as the NaCl concentration is increases up to 1 M, while in the range up to 200 mM NaCl the effect is mainly in Km because there is no significant decrease in kcat values. A significant decrease in the kcat values is observed as the salt concentration is further increased from 200 to 800 mM NaCl
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purified enzyme complexed with angiotensin II, hanging drop method, room temperature, from 42% saturated ammonium sulfate, 0.1 M sodium acetate, pH 4.0, 10% v/v ethylene glycol, crystals are soaked in cryosolution containing 30% glvcerol, 45% saturated ammonium sulfate,and 0.1 M sodium acetate, pH 4.0, heavy atom derivatizing, X-ray diffraction structure determination and analysis at 1.9-2.5 A resolution, molecular modeling and multiple isomorphous replacement phasing
enzyme-(acetyl-FKF-(3S,4S)-phenylstatinyl)-LR-NH2 complex and enzyme-acetyl-FKF(2R,3S)-phenylisoseryl-ALR-NH2 complex. Native crystals of the enzyme are grown at room temperature by the hanging-drop vapor diffusion method from 42% saturated ammonium sulfate, 10% ethylene glycol and 0.1 M sodium acetate buffer (pH 4.0). These crystals are then soaked in solutions of varying concentrations of the transition state analogs (acetyl-FKF-(3S,4S)-phenylstatinyl)-LR-NH2 and acetyl-FKF(2R,3S)-phenylisoseryl-ALR-NH2
Studies on new acid proteases from Scytalidium lignicolum ATCC 24568. Part IX. Additional evidence for the identity of Scytalidium lignicolum acid proteinases with the carboxyl proteinase group: the interaction between angiotensin I and S-PI-insensitive acid proteinases by means of a zinc(II)-dye complex as a probe