Degradation of streptomyces metalloprotease inhibitor (SMPI) by neutral protease from Bacillus subtilis var. amylosacchariticus.
The zinc-containing neutral endopeptidase (neutral protease: BANP) from Bacillus subtilis var. amylosacchariticus was inhibited by the proteinaceous metalloprotease inhibitor isolated from Streptomyces nigrescens (SMPI). The degree of inhibition was, however, significantly less than that for thermolysin (TLN). During incubation of BANP with SMPI, the inhibitor was proteolytically degraded and inactivated. Analysis of the digestion products suggested that a minor diversity in their substrate specificities between TLN and BANP affects the sensitivity to the proteinaceous metalloprotease inhibitor, SMPI.
Tsuru
D
D
School of Pharmaceutical Sciences, Nagasaki University, Japan.
Fujita
Y
Y
Morikawa
S
S
Ito
K
K
Yoshimoto
T
T
D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000201:enzymology*; D001426:Bacterial Proteins / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D008666:Metalloendopeptidases / Q000037:antagonists & inhibitors*; D008969:Molecular Sequence Data; D013302:Streptomyces / Q000201:enzymology*; D013379:Substrate Specificity; D013820:Thermolysin / Q000037:antagonists & inhibitors*
D001426:Bacterial Proteins; C056999:metalloproteinase inhibitor, Streptomyces; D008666:Metalloendopeptidases; D013820:Thermolysin; C071298:bacillolysin