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. 1993 Oct;11(10):1162-5.
doi: 10.1038/nbt1093-1162.

Electrospray mass spectrometry characterization of post-translational modifications of barley alpha-amylase 1 produced in yeast

M Søgaard  1 , J S Andersen, P Roepstorff, B Svensson
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Electrospray mass spectrometry characterization of post-translational modifications of barley alpha-amylase 1 produced in yeast

M Søgaard et al. Biotechnology (N Y). 1993 Oct.

Abstract

We have used electrospray mass spectrometry (ESMS) in combination with protein chemistry and genetics to delineate post-translational modifications in yeast of barley alpha-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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