A bacterial glucanotransferase can replace the complex maltose metabolism required for starch to sucrose conversion in leaves at night

Christian Ruzanski, Julia Smirnova, Martin Rejzek, Darrell Cockburn, Henriette L. Pedersen, Marilyn Pike, William G.T. Willats, Birte Svensson, Martin Steup, Oliver Ebenhöh, Alison M. Smith, Robert A. Field

Research output: Contribution to journalArticle

20 Scopus citations

Abstract

Background:Maltose metabolism during leaf starch degradation requires a multidomain glucanotransferase and a complex polysaccharide. Results: A conventional bacterial glucanotransferase rescues an Arabidopsis mutant lacking the multidomain glucanotransferase. Conclusion:Both the plant glucanotransferase-polysaccharide couple and the bacterial enzyme provide a glucosyl buffer in the starch degradation pathway. Significance:New light is shed on the regulation and evolution of maltose metabolism.

Original languageEnglish (US)
Pages (from-to)28581-28598
Number of pages18
JournalJournal of Biological Chemistry
Volume288
Issue number40
DOIs
StatePublished - Oct 4 2013

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Ruzanski, C., Smirnova, J., Rejzek, M., Cockburn, D., Pedersen, H. L., Pike, M., Willats, W. G. T., Svensson, B., Steup, M., Ebenhöh, O., Smith, A. M., & Field, R. A. (2013). A bacterial glucanotransferase can replace the complex maltose metabolism required for starch to sucrose conversion in leaves at night. Journal of Biological Chemistry, 288(40), 28581-28598. https://doi.org/10.1074/jbc.M113.497867