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

19 Citations (Scopus)

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

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Maltose
Metabolism
Starch
Sucrose
Bacterial Polysaccharides
Degradation
Arabidopsis
Polysaccharides
Buffers
Enzymes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

Ruzanski, Christian ; Smirnova, Julia ; Rejzek, Martin ; Cockburn, Darrell ; Pedersen, Henriette L. ; Pike, Marilyn ; Willats, William G T ; Svensson, Birte ; Steup, Martin ; Ebenhöh, Oliver ; Smith, Alison M. ; Field, Robert A. / A bacterial glucanotransferase can replace the complex maltose metabolism required for starch to sucrose conversion in leaves at night. In: Journal of Biological Chemistry. 2013 ; Vol. 288, No. 40. pp. 28581-28598.
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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.",
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Ruzanski, C, Smirnova, J, Rejzek, M, Cockburn, D, Pedersen, HL, Pike, M, Willats, WGT, Svensson, B, Steup, M, Ebenhöh, O, Smith, AM & Field, RA 2013, 'A bacterial glucanotransferase can replace the complex maltose metabolism required for starch to sucrose conversion in leaves at night', Journal of Biological Chemistry, vol. 288, no. 40, pp. 28581-28598. https://doi.org/10.1074/jbc.M113.497867

A bacterial glucanotransferase can replace the complex maltose metabolism required for starch to sucrose conversion in leaves at night. / Ruzanski, Christian; Smirnova, Julia; Rejzek, Martin; Cockburn, Darrell; Pedersen, Henriette L.; Pike, Marilyn; Willats, William G T; Svensson, Birte; Steup, Martin; Ebenhöh, Oliver; Smith, Alison M.; Field, Robert A.

In: Journal of Biological Chemistry, Vol. 288, No. 40, 04.10.2013, p. 28581-28598.

Research output: Contribution to journalArticle

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T1 - A bacterial glucanotransferase can replace the complex maltose metabolism required for starch to sucrose conversion in leaves at night

AU - Ruzanski, Christian

AU - Smirnova, Julia

AU - Rejzek, Martin

AU - Cockburn, Darrell

AU - Pedersen, Henriette L.

AU - Pike, Marilyn

AU - Willats, William G T

AU - Svensson, Birte

AU - Steup, Martin

AU - Ebenhöh, Oliver

AU - Smith, Alison M.

AU - Field, Robert A.

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Y1 - 2013/10/4

N2 - 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.

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