Thermitase - kinetic differentiation to the subtilisins.
In the last 12 years more than 80 peptidyl substrates and substrate analogous inhibitors were synthesized in our group and used to characterize thermitase, a serine proteinase of the subtilisin family produced by Thermoactinomyces vulgaris. The kinetic parameters of hydrolysis and inhibition reactions, respectively, with thermitase were determined and compared with those found with related enzymes. Conclusions with respect to the extent of the active site of thermitase and to the specificity of the different subsites could be drawn.
Peters
K
K
Institute of Physiological Chemistry, Medical Faculty of the Martin Luther University Halle, Germany.
Brömme
D
D
Jahreis
G
G
Fittkau
S
S
D001665:Binding Sites; D006868:Hydrolysis; D007700:Kinetics; D012697:Serine Endopeptidases / Q000378:metabolism*; D015842:Serine Proteinase Inhibitors / Q000378:metabolism*; D013381:Subtilisins / Q000378:metabolism*
D015842:Serine Proteinase Inhibitors; D012697:Serine Endopeptidases; D013381:Subtilisins; C022728:thermitase