P1-SPECIFICITY OF AQUALYSIN I (A SUBTILISIN-TYPE SERINE-PROTEASE) FROM THERMUS-AQUATICUS YT-1, USING P1-SUBSTITUTED DERIVATIVES OF STREPTOMYCES SUBTILISIN INHIBITOR

Authors
TANAKA T MATSUZAWA H KOJIMA S KUMAGAI I MIURA K OHTA T
Citation
T. Tanaka et al., P1-SPECIFICITY OF AQUALYSIN I (A SUBTILISIN-TYPE SERINE-PROTEASE) FROM THERMUS-AQUATICUS YT-1, USING P1-SUBSTITUTED DERIVATIVES OF STREPTOMYCES SUBTILISIN INHIBITOR, Bioscience, biotechnology, and biochemistry, 62(10), 1998, pp. 2035-2038
Citations number
17
Categorie Soggetti
Biology,Agriculture,"Biothechnology & Applied Migrobiology","Food Science & Tenology
Journal title
Bioscience, biotechnology, and biochemistry → ACNP
ISSN journal
09168451
Volume
62
Issue
10
Year of publication
1998
Pages
2035 - 2038
Database
ISI
SICI code
0916-8451(1998)62:10<2035:POAI(S>2.0.ZU;2-Y
Abstract
Aqualysin I is an alkaline serine protease isolated from Thermus aquat icus YT-1, an extreme thermophile. We have measured the P1-specificity of aqualysin I, using wildtype and five P1-substituted derivatives of Streptomyces subtilisin inhibitor (SSI). SSIs efficiently inhibited t he activity of aqualysin I, with low substrate specificity. Charge and hydrophobicity of side chain of the P1 amino acid residue showed no s ignificant effect to the P1-specificity of this enzyme.