An off-lattice dynamic Monte Carlo (MC) method is used to investigate the conformational dynamics of chymotrypsin inhibitor 2 (CI2) and subtilisin in both free and complex forms over two time windows, referring to short and long time scales. The conformational dynamics of backbone bonds analysed ...
The potential individual substrate-binding pockets of Ssp, were identified by overlaying the structure of subtilisin BPN’ in complex with the inhibitor CI2 (PDB: 1LW6)44with the subtilase domain of Ssp. The bound reactive site loop of CI2 provided a guide to the subsite positions in Ssp (Fig...
Hydrogen Bonding to Active-Site Histidine in Peptidyl Boronic Acid Inhibitor Complexes of Chymotrypsin and Subtilisin: Proton Magnetic Resonance Assignment... 1H NMR chemical shift assignments were established for Nδ1H (16.9 ppm) and Nε2H (16.1 ppm) of the active-center His57 for the complex ...
The P1 site was was identified as methionine, which was in good agreement with the substrate specificity of alpha-chymotrypsin. SSI, which also possesses a methionine residue at the P1 site, inhibits alpha-chymotrypsin poorly (inhibitor constant, 4.0 microM). Such a difference in the inhibitory ...
An ultraviolet absorption difference spectrum that is typical of a change in ionization state (pKa 9.7→>11.5) of a tyrosyl residue has been observed on the binding between Streptomyces subtilisin inhibitor (SSI) and subtilisin BPN' [EC 3.4.21.14] at alkaline pH, ionic strength 0.1 M, at 25...
Tedeschi F, Di Maro A, Facchiano A, Costantini S, Chambery A, Bruni N, et al. Wheat subtilisin/chymotrypsin inhibitor (WSCI) as a scaffold for novel serine protease inhibitors with a given specificity. Molec Biosystems. 2012;8:3335-43....
Primary structure and inhibitory properties of a subtilisin-chymotrypsin inhibitor from Streptomyces virginiae - Terabe, Kojima, et al. - 1994 () Citation Context ...tributed among Streptomyces spp. (16–18) and that a strong correlation exists between the structure around the reactive region of...
Primary Structure and Reactive Site of a Novel Wheat Proteinase Inhibitor of Subtilisin and Chymotrypsin : Biological Chemistry
Primary structure and reactive site of a novel wheat proteinase inhibitor of subtilisin and chymotrypsin. Biol. Chem. 384: 295-304.E. Poerio, S. Di Gennaro, A. Di Maro, F. Farisei, P. Ferranti, A. Parente, Primary structure and reactive site of a novel wheat proteinase inhibitor of ...