Streptomyces griseus protease

James, M.N.G., et al. Structures of product and inhibitor complexes of Streptomyces griseus protease A at 1.8 A resolution. A model for serine protease catalysis. 

Streptomyces griseus protease A (Brayer et al., 1978), see Trypsin Streptomyces griseus protease B (Delbaere et al., 1975), see Trypsin Subtilisin (Wright et al., 1969)... 

Enzymatic Hydrolysis. One-half of the S35-labeled proteinaceous residue was suspended in 95 ml. of distilled water and the pH was adjusted to about 7.5 with 2N ammonium hydroxide. Five milliliters of ethanol and 10 mg. of Streptomyces griseus protease (Pronase,1 6 PU... 

P. Dauber-Osguthorpe, D. J. Osguthorpe, P. S. Stem and J. Moult, Low frequency motion in proteins comparison of normal mode and molecular dynamics of streptomyces griseus protease A, J. Comput. Phys., 151(1), 169-189 (1999). 

R8. Robinson, J. C., and Pierce, J. E., Prevention of background staining of starch gels. Preliminary treatment of the starch with streptomyces griseus protease. Am. J. Clin. Pathol. 40, 588-590 (1963). 

Figure 10. A stereodiagram showing a comparison of the active site geometry of Streptomyces griseus protease A (SGPA) with that of bovine -trypsin. SGPA is presented by solid bonds, trypsin by open bonds. The root mean square deviation after minimisation by application of an appropriate rotation translation matrix is 0.39 A for some 62 common atom positions. From [97].

L. Jurasek, R. W. Olafson, P. Johnson, and L. B. Smillie, Miiwn Winter Symp., 11,93 (1976). Relationships between the Structures and Activities of Some Microbial Serine Proteases, I. Purification, Enzymic Properties and Primary Sequences of Streptomyces griseus Proteases A, B, and Trypsin. 

Achromobacter protease a-Chymotrypsin, subtilisins Carboxypeptidase Y Elastase Trypsin, Streptomyces griseus protease Staphylococcus aureus V8 protease Serine protease Serine protease Serine protease Serine protease Serine protease Serine protease -Lys-X -Trp(Tyr,Phe,Leu,Met)-X nonspecific -Ala(Ser,Met,Phe)-X -Arg(Lys)-X -Glu(Asp)-X... 

The enzyme s three-dimensional structure was determined by standard techniques. The structure of complexes between the enzyme and two tetrapeptide derivatives, Ac-Pro-Ala-Pro-PheOH and Ac-Pro-Ala-Pro-TyrOH, was also elucidated. Details of the interaction between these peptides and Streptomyces griseus protease A (SGPA) were carefully investigated, and the authors discussed the conformational changes occurring in the enzyme as a result of interactions with the substrate as well as possible catalytic mechanisms of this serine protease. 

The common proteases used in protease mapping are chymotrypsin. Staphylococcus aureus protease, papain, subtilisin, Streptomyces griseus protease, flcln, and elastase. Of these, papain requires 2-mercaptoethanol which inhibits acrylamide polymerization. This protease therefore cannot be used for proteolysis during electrophoresis. Cofactors needed by proteases can be incorporated into the gels. 

T trypsin, CT a-chymotrypsin, P papain, Bs Bacillus subtilis proteases, AP AspergUlus spp. proteases, SG Streptomyces griseus proteases, PP Penidllium spp. proteases, + inhibited, — not inhibited, inhibited by some inhibitors of the particular source. 

Streptomyces griseus Protease Black Angus steer hide Gehring et al. (2002)... 

Elliott, R. J., Bennet, A. J., Braun, C. A., MacLeod, A. M., Borgford, T. J. (2000). Active-site variants of Streptomyces griseus protease B with peptide-ligation activity. Chem. Biol, 7, 163-171. 

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