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β‐Glucosylarginine: a new glucose‐protein bond in a self‐glucosylating protein from sweet corn

β‐Glucosylarginine: a new glucose‐protein bond in a self‐glucosylating protein from sweet corn In the search for a protein primer for starch synthesis, an autocatalytic self‐glucosylating protein has been isolated from sweet corn. Several tryptic peptides were obtained from the [14C]glucosylated protein and were sequenced, corresponding to over 40% of the estimated total sequence (molecular mass 42 kDa). There is no homology with the amino acid sequence of the autocatalytic glycogen primer, glycogenin, nor in respect of the nature of the union between the autocatalytically added glucose and the protein, which, in the case of the corn protein, now named amylogenin, is a novel glucose‐protein bond, a single β‐glucose residue joined to an arginine residue. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Febs Letters Wiley

β‐Glucosylarginine: a new glucose‐protein bond in a self‐glucosylating protein from sweet corn

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References (13)

Publisher
Wiley
Copyright
© 2015 Federation of European Biochemical Societies
eISSN
1873-3468
DOI
10.1016/0014-5793(95)01247-6
Publisher site
See Article on Publisher Site

Abstract

In the search for a protein primer for starch synthesis, an autocatalytic self‐glucosylating protein has been isolated from sweet corn. Several tryptic peptides were obtained from the [14C]glucosylated protein and were sequenced, corresponding to over 40% of the estimated total sequence (molecular mass 42 kDa). There is no homology with the amino acid sequence of the autocatalytic glycogen primer, glycogenin, nor in respect of the nature of the union between the autocatalytically added glucose and the protein, which, in the case of the corn protein, now named amylogenin, is a novel glucose‐protein bond, a single β‐glucose residue joined to an arginine residue.

Journal

Febs Letters – Wiley

Published: Nov 27, 1995

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