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beta-Glucosylarginine: a new glucose-protein bond in a self-glucosylating protein from sweet corn.
Singh, D G; Lomako, J; Lomako, W M; Whelan, W J; Meyer, H E; Serwe, M; Metzger, J W.
Affiliation
  • Singh DG; Department of Biochemistry and Molecular Biology, University of Miami School of Medicine, (M823), FL 33101, USA.
FEBS Lett ; 376(1-2): 61-4, 1995 Nov 27.
Article in En | MEDLINE | ID: mdl-8521968
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 beta-glucose residue joined to an arginine residue.
Subject(s)
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Collection: 01-internacional Database: MEDLINE Main subject: Arginine / Zea mays / Glucose / Glucosides Language: En Journal: FEBS Lett Year: 1995 Document type: Article Affiliation country:
Search on Google
Collection: 01-internacional Database: MEDLINE Main subject: Arginine / Zea mays / Glucose / Glucosides Language: En Journal: FEBS Lett Year: 1995 Document type: Article Affiliation country:
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