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.
Ehrenfreund
P
P
Molecular Biology Institute, Austrian Academy of Sciences, Salzburg.
Mollay
C
C
Kreil
G
G
D000626:Aminopeptidases / Q000302:isolation & purification* / Q000378:metabolism*; D002614:Chelating Agents / Q000494:pharmacology; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004151:Dipeptides / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006596:Hexosaminidases / Q000235:genetics / Q000378:metabolism; D007700:Kinetics; D011499:Protein Processing, Post-Translational; D013302:Streptomyces / Q000201:enzymology*; D013379:Substrate Specificity
D002614:Chelating Agents; D004151:Dipeptides; D006596:Hexosaminidases; D000626:Aminopeptidases; C022450:prolyl aminopeptidase