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Electrospray Mass Spectrometry Characterization of Post-Translational Modifications of Barley α-Amylase 1 Produced in Yeast

Bio/Technology volume 11, pages 1162–1165 (1993)Cite this article

Abstract

We have used electrospray mass spectrometry (ESMS) in combination with protein chemistry and genetics to delineate post-translational modifications in yeast of barley α-amylase 1 (AMY1), a 45 kD enzyme crucial for production of malt, an important starting material in the manufacture of beer and whisky. In addition to signal peptide processing these modifications are: (1) removal of C-terminal Arg-Ser by Kex1p, (2) glutathionylation of Cys95, (3) O-glycosylation, and (4) additional degradation of the C-terminus.

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Author notes

  1. Morten Søgaard

    Present address: Program in Cellular Biochemistry & Biophysics, Rockefeller Research Laboratories, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, New York, N.Y., 10021

  2. Peter Roepstorff and Birte Svensson: Corresponding authors.

Authors and Affiliations

  1. Department of Chemistry, Carlsberg Laboratory, Gamle Carlsberg Vej 10, DK-2500, Copenhagen Valby, Denmark

    Birte Svensson

  2. Institute of Molecular Biology, Odense University, Campusvej 55, DK-5230, Odense M, Denmark

    Jens S. Andersen & Peter Roepstorff

Authors
  1. Morten Søgaard
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  2. Jens S. Andersen
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  3. Peter Roepstorff
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  4. Birte Svensson
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Søgaard, M., Andersen, J., Roepstorff, P. et al. Electrospray Mass Spectrometry Characterization of Post-Translational Modifications of Barley α-Amylase 1 Produced in Yeast. Nat Biotechnol 11, 1162–1165 (1993). https://doi.org/10.1038/nbt1093-1162

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