A CBM20 low-affinity starch-binding domain from glucan, water dikinase

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A CBM20 low-affinity starch-binding domain from glucan, water dikinase. / Christiansen, Camilla; Abou Hachem, Maher; Glaring, Mikkel Andreas; Viksø-Nielsen, Anders; Sigurskjold, Bent Walther; Svensson, Birte; Blennow, Per Gunnar Andreas.

In: FEBS Letters, Vol. 583, No. 7, 2009, p. 1159-1163.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Christiansen, C, Abou Hachem, M, Glaring, MA, Viksø-Nielsen, A, Sigurskjold, BW, Svensson, B & Blennow, PGA 2009, 'A CBM20 low-affinity starch-binding domain from glucan, water dikinase', FEBS Letters, vol. 583, no. 7, pp. 1159-1163. https://doi.org/10.1016/j.febslet.2009.02.045

APA

Christiansen, C., Abou Hachem, M., Glaring, M. A., Viksø-Nielsen, A., Sigurskjold, B. W., Svensson, B., & Blennow, P. G. A. (2009). A CBM20 low-affinity starch-binding domain from glucan, water dikinase. FEBS Letters, 583(7), 1159-1163. https://doi.org/10.1016/j.febslet.2009.02.045

Vancouver

Christiansen C, Abou Hachem M, Glaring MA, Viksø-Nielsen A, Sigurskjold BW, Svensson B et al. A CBM20 low-affinity starch-binding domain from glucan, water dikinase. FEBS Letters. 2009;583(7):1159-1163. https://doi.org/10.1016/j.febslet.2009.02.045

Author

Christiansen, Camilla ; Abou Hachem, Maher ; Glaring, Mikkel Andreas ; Viksø-Nielsen, Anders ; Sigurskjold, Bent Walther ; Svensson, Birte ; Blennow, Per Gunnar Andreas. / A CBM20 low-affinity starch-binding domain from glucan, water dikinase. In: FEBS Letters. 2009 ; Vol. 583, No. 7. pp. 1159-1163.

Bibtex

@article{980cf590332b11de87b8000ea68e967b,
title = "A CBM20 low-affinity starch-binding domain from glucan, water dikinase",
abstract = "The family 20 carbohydrate-binding module (CBM20) of the Arabidopsis starch phosphorylator glucan, water dikinase 3 (GWD3) was heterologously produced and its properties were compared to the CBM20 from a fungal glucoamylase (GA). The GWD3 CBM20 has 50-fold lower affinity for cyclodextrins than that from GA. Homology modelling identified possible structural elements responsible for this weak binding of the intracellular CBM20. Differential binding of fluorescein-labelled GWD3 and GA modules to starch granules in vitro was demonstrated by confocal laser scanning microscopy and yellow fluorescent protein-tagged GWD3 CBM20 expressed in tobacco confirmed binding to starch granules in planta.",
author = "Camilla Christiansen and {Abou Hachem}, Maher and Glaring, {Mikkel Andreas} and Anders Viks{\o}-Nielsen and Sigurskjold, {Bent Walther} and Birte Svensson and Blennow, {Per Gunnar Andreas}",
note = "Keywords: Bioimaging; Carbohydrate-binding module 20; Glucan, water dikinase; Starch-binding domain; Surface plasmon resonance",
year = "2009",
doi = "10.1016/j.febslet.2009.02.045",
language = "English",
volume = "583",
pages = "1159--1163",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd",
number = "7",

}

RIS

TY - JOUR

T1 - A CBM20 low-affinity starch-binding domain from glucan, water dikinase

AU - Christiansen, Camilla

AU - Abou Hachem, Maher

AU - Glaring, Mikkel Andreas

AU - Viksø-Nielsen, Anders

AU - Sigurskjold, Bent Walther

AU - Svensson, Birte

AU - Blennow, Per Gunnar Andreas

N1 - Keywords: Bioimaging; Carbohydrate-binding module 20; Glucan, water dikinase; Starch-binding domain; Surface plasmon resonance

PY - 2009

Y1 - 2009

N2 - The family 20 carbohydrate-binding module (CBM20) of the Arabidopsis starch phosphorylator glucan, water dikinase 3 (GWD3) was heterologously produced and its properties were compared to the CBM20 from a fungal glucoamylase (GA). The GWD3 CBM20 has 50-fold lower affinity for cyclodextrins than that from GA. Homology modelling identified possible structural elements responsible for this weak binding of the intracellular CBM20. Differential binding of fluorescein-labelled GWD3 and GA modules to starch granules in vitro was demonstrated by confocal laser scanning microscopy and yellow fluorescent protein-tagged GWD3 CBM20 expressed in tobacco confirmed binding to starch granules in planta.

AB - The family 20 carbohydrate-binding module (CBM20) of the Arabidopsis starch phosphorylator glucan, water dikinase 3 (GWD3) was heterologously produced and its properties were compared to the CBM20 from a fungal glucoamylase (GA). The GWD3 CBM20 has 50-fold lower affinity for cyclodextrins than that from GA. Homology modelling identified possible structural elements responsible for this weak binding of the intracellular CBM20. Differential binding of fluorescein-labelled GWD3 and GA modules to starch granules in vitro was demonstrated by confocal laser scanning microscopy and yellow fluorescent protein-tagged GWD3 CBM20 expressed in tobacco confirmed binding to starch granules in planta.

U2 - 10.1016/j.febslet.2009.02.045

DO - 10.1016/j.febslet.2009.02.045

M3 - Journal article

C2 - 19275898

VL - 583

SP - 1159

EP - 1163

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 7

ER -

ID: 12051736