Streptomyces subtilisin inhibitor

Hiromi, K Akasaka, K Mitsui, Y Tonomura, B Murao, S (eds) (1985) Protein Protease Inhibitor - The Case of Streptomyces Subtilisin Inhibitor. Elsevier Amsterdam - Oxford - New York. 

Aspartate transcarbamylase regulatory domains 1 and 2 Streptomyces subtilisin inhibitor Glutathione reductase domain 3 Thermolysin domain 1... 

Hexokinase Pyruvate kinase Adenylate kinase Phosphoglycerate kinase Phosphofructokinase Protease inhibitors Pancreatic trypsin inhibitor Soybean trypsin inhibitor Streptomyces subtilisin inhibitor Nucleases... 

Nuclear Magnetic Resonance Studies on Streptomyces Subtilisin Inhibitor and its Complexes with Proteinases... 

Fig. 2.1 Structure of SSI subunit. (Reproduced with permission from Y., Mitsui, et al Protein Protease Inhibitor-The Case of Streptomyces Subtilisin Inhibitor (SSI) (K. Hiromi et al. ed.), p. 174, Elsevier, Amsterdam (1985)).

Kainosho M, Tsuji T, Assignment of the three methionyl carbonyl carbon resonances in Streptomyces subtilisin inhibitor by a carbon-13 and nitrogen-15 double-labeling technique. A new strategy for structural studies of proteins in solution, Biochemistry, 21 6273-6279, 1982. 

Another important area of dynamic studies in biological samples is the effect of hydration upon molecular mobility in proteins and carbohydrates. The reason for these studies is primarily that protein dynamics, in particular, are crucial to their function, and so examining factors, such as the degree of hydration, that affect their dynamics is very important. However, it is obviously near-impossible to study dynamics in aqueous solution as a function of degree of hydration, and, since most proteins are not soluble in nonaqueous solvents, solid-state studies must be used. The motions at three methionine (Met) residues in Streptomyces subtilisin inhibitor (SSI) were studied with 2H NMR using a sample in which the Met residues at two crucial enzyme recognition sites (PI and P4) were specifically deuterated, along with one in the hydrophobic core.114 The motions of the Met side-chains were then examined... 

Akasaka, K. Spin diffusion and the dynamic structure of a protein Streptomyces subtilisin inhibitor. J. Magnet Res. 1983, 36, 135-140. 

The Streptomyces subtilisin inhibitor is closely related to the Kazal inhibitor family (Laskowski and Kato, 1980). The subunits of this dimeric inhibitor dissociate during thermal unfolding (Takahashi and Sturtevant, 1981), when dilute solutions (2--5 mg/ml) are heated slowly (l C/min) in a Privalov (1980) type of DSC instrument. The Td for Strepton yces subtilisin inhibitor is 17 C above that for STI at this heating rate (Table II), suggesting that it is intermediate in stability among the inhibitors tested. 

Takahashi, K., and Sturtevant, J. M. (1981). Thermal denaturation of Streptomyces subtilisin inhibitor, subtilisin BPN, and the subti11 sin—inhibitor complex. Biochemistry 20, 6185-6190. 

Ikenaka, T. (1985) Chapter 4 in Protein Protease Inhibitor - The case of Streptomyces Subtilisin inhibitor, pp, 159-163, (K. Hiromi, K. Akasaka, Y. Mitsui, B. Tonomura and S. Murao, eds.) Elsevier Science Publishers, Amsterdam... 

The inhibitor has been purified using a modification of the scheme of Millet and Gregoire [2] (Table 2) plus a final fractionation on a reverse phase HPLC column employing an n-butanol gradient (in 0.1% trifluoroacetic acid). The amino acid composition differs somewhat from inhibitors of E. coli or Streptomyces (Table 3) but they are probably all of the same general class in that they contain a low percentage of cysteine and are active on either subtilisin (E. coli and Streptomyces) or related serine proteases [8],... 

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