[Isolation and characterization of the ALP1 protease from Aspergillus fumigatus and its protein inhibitor from Physarium polycephalum].
It is known that Aspergillus fumigatus secretes a serine protease ALP1 of the subtilisin family in the presence of extracellular protein substrates. We found conditions of A. fumigatus culturing that provide a high ALP1 activity inside cells without induction by extracellular proteins. The identity of the properties of the secreted and intracellular enzymes was shown. A thermostable protein inhibitor of the ALP1 protease was isolated from the plasmodium of the myxomycete Physarum polycephalum. Its molecular mass is 32-33 kDa. The inhibitor inhibits the ALP1 protease activity with IC50 of 0.14 microM. This protein was also shown to be a less efficient inhibitor of the activity of HIV-1 protease (IC50 2.5 microM). The English version of the paper: Russian Journal of Bioorganic Chemistry, 2005, vol. 31, no. 3; see also http://www.maik.ru.
Davies
D A
DA
Kalinina
N A
NA
Samokhvalova
L V
LV
Malakhova
G V
GV
Scott
G
G
Volynskaia
A M
AM
Nesmeianov
V A
VA
D000818:Animals; D001232:Aspergillus fumigatus / Q000201:enzymology*; D005656:Fungal Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000302:isolation & purification*; D016333:HIV Protease / Q000737:chemistry; D010804:Physarum / Q000737:chemistry*; D015842:Serine Proteinase Inhibitors / Q000737:chemistry* / Q000302:isolation & purification*; D013381:Subtilisins / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000302:isolation & purification*
D005656:Fungal Proteins; D015842:Serine Proteinase Inhibitors; D013381:Subtilisins; D016333:HIV Protease