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Maturation pathway of metalloprotease produced by Aeromonas sobria
Author(s) -
Takahashi Eizo,
Fujii Yoshio,
Kobayashi Hidetomo,
Yamanaka Hiroyasu,
Nair Gopinath Balakrish,
Takeda Yoshifumi,
Arimoto Sakae,
Negishi Tomoe,
Okamoto Keinosuke
Publication year - 2010
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.2010.00258.x
Subject(s) - metalloproteinase , biology , protease , biochemistry , peptide sequence , serine protease , amino acid , serine , microbiology and biotechnology , gene , enzyme
Previously, we cloned the metalloprotease gene of Aeromonas sobria ( amp ) and determined its nucleotide sequence (GenBank accession number DQ784565). The protease is composed of 591 amino acid residues. In this study, we purified the mature metalloprotease from the culture supernatant of A. sobria and determined the amino terminal sequence and molecular size of AMP. In addition, we examined the production of AMP diachronically and found that AMP emerges outside of the cell as an intermediate composed of mature and propeptide regions. Subsequently, we determined that the N‐terminal amino acid sequence of the intermediate and found that the sequence is identical to that of the mature metalloprotease. This means that the intermediate is composed of a mature AMP region and a C‐terminal propeptide. The cross culture experiment of mutants of metalloprotease and serine protease of A. sobria on skim milk agar medium indicates that the intermediate released outside of the cell is inactive and that serine protease produced by A. sobria accelerates the conversion of the intermediate from the inactive to the active form.