Properties of cold-adapted subtilisine-like proteinase of endemic yeast Leucosporidium antarcticum

An extracellular serine proteinase from psychrophilic marine Antarctic yeast L. antarcticum has been purified to homogeneity and characterized. The enzyme specificity, which resembles both chymotrypsin and subtilisin, as well as kinetic (topt of 25 degrees C, activity up to -20 degrees C, pHoptBzTyr...

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Bibliographic Details
Published in:	Mededelingen (Rijksuniversiteit te Gent. Fakulteit van de Landbouwkundige en Toegepaste Biologische Wetenschappen) Vol. 66; no. 3a; p. 329
Main Authors:	Turkiewicz, M, Pazgier, M, Kalinowska, H, Bielecki, S
Format:	Journal Article
Language:	English
Published:	Belgium 2001
Subjects:	Acclimatization Amino Acid Sequence Basidiomycota - enzymology Cold Temperature Enzyme Stability Molecular Sequence Data Peptide Fragments - chemistry Protein Conformation Seawater - microbiology Serine Endopeptidases - chemistry Serine Endopeptidases - metabolism Subtilisins - metabolism Thermodynamics
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Summary:	An extracellular serine proteinase from psychrophilic marine Antarctic yeast L. antarcticum has been purified to homogeneity and characterized. The enzyme specificity, which resembles both chymotrypsin and subtilisin, as well as kinetic (topt of 25 degrees C, activity up to -20 degrees C, pHoptBzTyrOEt of 8.0-8.5), and thermodynamic properties conferring cold-adaptation of the proteinase, were determined The comparison of N-terminal sequence of 35 amino acid residues with known sequences of serine proteinases indicates that the enzyme can be preliminarly classified as a subtilisin-like proteinase, belonging to the proteinase K subfamily (clan SB, family S8, subfamily C).
ISSN:	1373-7503