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

M. Søgaard; J. S. Andersen; P. Roepsdorff; Birte Svensson

doi:10.1038/nbt1093-1162

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

M. Søgaard
, J. S. Andersen
, P. Roepsdorff
, Birte Svensson

Carlsberg Research Center

Research output: Contribution to journal › Journal article › Research › peer-review

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.

Original language	English
Journal	Bio/Technology
Volume	11
Issue number	10
Pages (from-to)	1162-1165
ISSN	0733-222X
DOIs	https://doi.org/10.1038/nbt1093-1162
Publication status	Published - 1993
Externally published	Yes

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

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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AU - Søgaard, M.

AU - Andersen, J. S.

AU - Roepsdorff, P.

AU - Svensson, Birte

PY - 1993

Y1 - 1993

N2 - 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.

AB - 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.

U2 - 10.1038/nbt1093-1162

DO - 10.1038/nbt1093-1162

M3 - Journal article

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JF - Bio/Technology

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ER -

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

Abstract

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