P1-Specificity of Aqualysin I (a Subtilisin-type Serine Protease) from Thermus aquaticus YT-1, using P1-Substituted Derivatives of Streptomyces Subtilisin Inhibitor

Terumichi TANAKADepartment of Biotechnology, The University of Tokyo

Hiroshi MATSUZAWADepartment of Biotechnology, The University of Tokyo

Shuichi KOJIMADepartment of Industrial Chemistry, Faculty of Engineering, The University of Tokyo

Izumi KUMAGAIDepartment of Industrial Chemistry, Faculty of Engineering, The University of Tokyo

Kin-ichiro MIURADepartment of Industrial Chemistry, Faculty of Engineering, The University of Tokyo

Takahisa OHTADepartment of Biotechnology, The University of Tokyo

Abstract

Aqualysin I is an alkaline serine protease isolated from Thermus aquaticus YT-1, an extreme thermophile. We have measured the P1-specificity of aqualysin I, using wild-type and five P1-substituted derivatives of Streptomyces subtilisin inhibitor (SSI). SSIs efficiently inhibited the activity of aqualysin I, with low substrate specificity. Charge and hydrophobicity of side chain of the P1 amino acid residue showed no significant effect to the P1-specificity of this enzyme.

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P1-Specificity of Aqualysin I (a Subtilisin-type Serine Protease) from Thermus aquaticus YT-1, using P1-Substituted Derivatives of Streptomyces Subtilisin Inhibitor

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P1-Specificity of Aqualysin I (a Subtilisin-type Serine Protease) from Thermus aquaticus YT-1, using P1-Substituted Derivatives of Streptomyces Subtilisin Inhibitor

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