engleski

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^-^4M 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 several Streptomyces species. The data contribute to the definition of M7 family of metalloendopeptidases in streptomycetes.

Metalloendopeptidase ; Specificity ; Amino acid sequence ; Streptomyces rimosus

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