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

doi:10.1074/jbc.M113.497867

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 journal › Article › peer-review

30 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 language	English (US)
Pages (from-to)	28581-28598
Number of pages	18
Journal	Journal of Biological Chemistry
Volume	288
Issue number	40
DOIs	https://doi.org/10.1074/jbc.M113.497867
State	Published - 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

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

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.",

author = "Christian Ruzanski and Julia Smirnova and Martin Rejzek and Darrell Cockburn and Pedersen, {Henriette L.} and Marilyn Pike and Willats, {William G.T.} and Birte Svensson and Martin Steup and Oliver Ebenh{\"o}h and Smith, {Alison M.} and Field, {Robert A.}",

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doi = "10.1074/jbc.M113.497867",

language = "English (US)",

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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

TY - JOUR

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.

PY - 2013/10/4

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.

AB - 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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DO - 10.1074/jbc.M113.497867

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AN - SCOPUS:84885158803

SN - 0021-9258

VL - 288

SP - 28581

EP - 28598

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 40

ER -

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

Abstract

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