title: [The novel Adams-like microbial metalloendopeptidase].
abstract: Heterologous gene expression of extracellular minor metalloendopeptidase of Bacillus pumilus 3-19 in protease-deficient B. subtilis strain has been studied. The fraction of enzyme in total pool of B. pumilus 3-19 secreted proteases composes less than 8%. The enzyme was isolated from culture liquid of recombinant strain, its primary structure was determined, physicochemical properties were investigated. It was concluded that secreted metallo endopeptidase of B. pumilus 3-19 represents the first prokaryotic homolog of eukaryotic adamalysin/reprolysin protein family.
authors.forename: N P
authors.initials: NP
authors.lastname: Balaban
authors.forename: N L
authors.initials: NL
authors.lastname: Rudakova
authors.forename: A R
authors.initials: AR
authors.lastname: Sabirova
authors.forename: L R
authors.initials: LR
authors.lastname: Valeeva
authors.forename: M R
authors.initials: MR
authors.lastname: Sharipova
mesh_terms: D000595:Amino Acid Sequence; D001407:Bacillus / Q000201:enzymology*; D004795:Enzyme Stability; D007700:Kinetics; D008666:Metalloendopeptidases / Q000737:chemistry* / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D011387:Prokaryotic Cells; D017434:Protein Structure, Tertiary
chemical_list: D008666:Metalloendopeptidases; C028220:Crotalus adamanteus proteinase II