P1 specificity of aqualysin I (a subtilisin-type serine protease) from Thermus aquaticus YT-1, using P1-substituted derivatives of Streptomyces subtilisin inhibitor.
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.
Tanaka
T
T
Department of Biotechnology, The University of Tokyo, Japan. tanakat@eco.tut.ac.jp
Matsuzawa
H
H
Kojima
S
S
Kumagai
I
I
Miura
K
K
Ohta
T
T
D001426:Bacterial Proteins / Q000494:pharmacology; D001665:Binding Sites; D007700:Kinetics; D009842:Oligopeptides / Q000378:metabolism; D012697:Serine Endopeptidases / Q000378:metabolism*; D015842:Serine Proteinase Inhibitors / Q000494:pharmacology; D013379:Substrate Specificity; D013824:Thermus / Q000201:enzymology*
D001426:Bacterial Proteins; D009842:Oligopeptides; D015842:Serine Proteinase Inhibitors; C018150:subtilisin inhibitor protein, Streptomyces; D012697:Serine Endopeptidases; C055102:aqualysin I