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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 

Purification and properties of an iminopeptidase from culture media of Streptomyces plicatus.

The degradation of the prosequence of the secreted enzyme endo-beta-N-acetylglucosaminidase H from Streptomyces plicatus is not elucidated. Both the primary structure of this segment and the finding that the secreted species contain ragged aminoterminal ends of specific structure suggested that a dipeptidylaminopeptidase might mature this enzyme. Therefore, we tested the culture medium of Streptomyces plicatus for prolin-specific peptidases. Proline iminopeptidase was purified about 800-fold to homogeneity from the culture medium. Dipeptidylaminopeptidase, the enzyme that seemed most likely to process the prosequence of endo-beta-N-acetylglucosaminidase H, could not be detected.[1]

References

  1. Purification and properties of an iminopeptidase from culture media of Streptomyces plicatus. Ehrenfreund, P., Mollay, C., Kreil, G. Biochem. Biophys. Res. Commun. (1992) [Pubmed]
 
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