Extracellular metalloendopeptidase of Streptomyces rimosus.
Metalloendopeptidase was isolated from Streptomyces rimosus culture filtrates in a homogeneous form. It was determined to be a 15 kDa basic protein, most active around pH 7.5, and susceptible to inhibition by chelating agents, N-bromosuccinimide, thiorphan, and 10(-4) M zinc. The enzyme was highly specific for phenylalanine at the N-side of endopeptide bonds. Determination of amino acid sequence of the enzyme's NH(2)-part allowed the recognition of its structure homology with isolated and predicted metallopeptidases from several Streptomyces species. The data contribute to the definition of M7 family of metalloendopeptidases in streptomycetes.
Vitale
Ljubinka
L
Department of Organic Chemistry and Biochemistry, Ruder Bosković Institute, Bijenicka c.54, 10002 Zagreb, Croatia. vitale@rudjer.irb.hr
Vukelić
Bojana
B
Krizaj
Igor
I
D000595:Amino Acid Sequence; D003470:Culture Media; D006863:Hydrogen-Ion Concentration; D008666:Metalloendopeptidases / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D008969:Molecular Sequence Data; D010649:Phenylalanine / Q000378:metabolism; D013302:Streptomyces / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development; D013379:Substrate Specificity
D003470:Culture Media; D010649:Phenylalanine; D008666:Metalloendopeptidases