Isolation and characterization of the genes encoding two metalloproteases (MprI and MprII) from a marine bacterium, Alteromonas sp. strain O-7.
An extracellular alkaline metalloprotease (MprI) from Alteromonas sp. strain O-7 was purified and characterized. The molecular mass of the purified enzyme was estimated to be 56 kDa by SDS-PAGE. The optimum pH and temperature were pH 10.0 and 60 degrees C, respectively. The gene (mprI) encoding MprI was cloned and its nucleotide sequence was analyzed. The deduced amino acid sequence of MprI showed significant similarity to metalloproteases classified into the thermolysin family. Furthermore, sequence analysis showed that another metalloprotease (MprII)-encoding gene was located downstream from mprI. The deduced amino acid sequence of MprII showed high similarity to metalloproteases of the aminopeptidase family. Similar repeated C-terminal extensions were found in both MprI and MprII.
Miyamoto
Katsushiro
K
Osaka University of Pharmaceutical Sciences, Takatsuki, Japan.
Tsujibo
Hiroshi
H
Nukui
Eiji
E
Itoh
Hiroyuki
H
Kaidzu
Yoshihiko
Y
Inamori
Yoshihiko
Y
D020591:Alteromonas / Q000235:genetics*; D000595:Amino Acid Sequence; D001483:Base Sequence; D004591:Electrophoresis, Polyacrylamide Gel; D005798:Genes, Bacterial; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000737:chemistry / Q000235:genetics*; D008386:Marine Biology; D008666:Metalloendopeptidases / Q000737:chemistry / Q000235:genetics*; D008969:Molecular Sequence Data; D013696:Temperature
D007527:Isoenzymes; D008666:Metalloendopeptidases