Streptomyces rimosus extracellular proteases 3. Isolation and characterization of leucine aminopeptidase |
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Authors: | Lj Vitale M Renko B Lenarčič V Turk M Pokorny |
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Institution: | (1) Ruđer Boškovic Institute, 41001 Zagreb, Yugoslavia;(2) Jožef Stefan Institute, 61000 Ljubljana, Yugoslavia;(3) Research and Development Institute, Krka Pharmaceutical and Chemical Works, 68 000 Novo mesto, Yugoslavia |
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Abstract: | Summary A leucine aminopeptidase was purified to homogeneity fromStreptomyces rimosus culture filtrates, which are waste broth of oxytetracycline bioproduction process. Purification procedure includes ultrafiltration
and chromatography on CM-Sephadex, AH-Sepharose and FPLC Mono S column.
The enzyme is a monomer with molecular weight of 27,500 Daltons and pI of 7.3, stable in broad pH range and up to 70°C. It
is a metallo enzyme dependent on Ca2+ ions for its full activity. By its specificity it is a true aminopeptidase active on amino acid amide, arylamide, peptide
and ester bonds. The hydrolysing activity shows preference for leucine at the N-terminal position of substrates, also acts
on aromatic acids and methionine, but does not release glycine, proline, acidic amino acids orD-amino acid residues. |
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