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Starch‐binding domains in the CBM45 family – low‐affinity domains from glucan, water dikinase and α‐amylase involved in plastidial starch metabolism. / Glaring, Mikkel Andreas; Baumann, Martin; Abou Hachem, Maher; Nakai, Hiroyuki; Nakai, Natsuko; Santelia, Diana; Sigurskjold, Bent W.; Zeeman, Samuel C.; Blennow, Andreas; Svensson, Birte.

In: F E B S Journal, Vol. 278, No. 7, 2011, p. 1175-1185.

Publication: Research - peer-reviewJournal article – Annual report year: 2011

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Author

Glaring, Mikkel Andreas; Baumann, Martin; Abou Hachem, Maher; Nakai, Hiroyuki; Nakai, Natsuko; Santelia, Diana; Sigurskjold, Bent W.; Zeeman, Samuel C.; Blennow, Andreas; Svensson, Birte / Starch‐binding domains in the CBM45 family – low‐affinity domains from glucan, water dikinase and α‐amylase involved in plastidial starch metabolism.

In: F E B S Journal, Vol. 278, No. 7, 2011, p. 1175-1185.

Publication: Research - peer-reviewJournal article – Annual report year: 2011

Bibtex

@article{7eeab5b1c935441293960436bfa30684,
title = "Starch‐binding domains in the CBM45 family – low‐affinity domains from glucan, water dikinase and α‐amylase involved in plastidial starch metabolism",
keywords = "a-glucan, a-amylase, Starch-binding domain, Starch metabolism, Carbohydrate-binding module, Water dikinase",
publisher = "Wiley-Blackwell Publishing Ltd.",
author = "Glaring, {Mikkel Andreas} and Martin Baumann and {Abou Hachem}, Maher and Hiroyuki Nakai and Natsuko Nakai and Diana Santelia and Sigurskjold, {Bent W.} and Zeeman, {Samuel C.} and Andreas Blennow and Birte Svensson",
year = "2011",
doi = "10.1111/j.1742-4658.2011.08043.x",
volume = "278",
number = "7",
pages = "1175--1185",
journal = "F E B S Journal",
issn = "1742-464X",

}

RIS

TY - JOUR

T1 - Starch‐binding domains in the CBM45 family – low‐affinity domains from glucan, water dikinase and α‐amylase involved in plastidial starch metabolism

A1 - Glaring,Mikkel Andreas

A1 - Baumann,Martin

A1 - Abou Hachem,Maher

A1 - Nakai,Hiroyuki

A1 - Nakai,Natsuko

A1 - Santelia,Diana

A1 - Sigurskjold,Bent W.

A1 - Zeeman,Samuel C.

A1 - Blennow,Andreas

A1 - Svensson,Birte

AU - Glaring,Mikkel Andreas

AU - Baumann,Martin

AU - Abou Hachem,Maher

AU - Nakai,Hiroyuki

AU - Nakai,Natsuko

AU - Santelia,Diana

AU - Sigurskjold,Bent W.

AU - Zeeman,Samuel C.

AU - Blennow,Andreas

AU - Svensson,Birte

PB - Wiley-Blackwell Publishing Ltd.

PY - 2011

Y1 - 2011

N2 - Starch‐binding domains are noncatalytic carbohydrate‐binding modules that mediate binding to granular starch. The starch‐binding domains from the carbohydrate‐binding module family 45 (CBM45, ) are found as N‐terminal tandem repeats in a small number of enzymes, primarily from photosynthesizing organisms. Isolated domains from representatives of each of the two classes of enzyme carrying CBM45‐type domains, the Solanum tuberosumα‐glucan, water dikinase and the Arabidopsis thaliana plastidial α‐amylase 3, were expressed as recombinant proteins and characterized. Differential scanning calorimetry was used to verify the conformational integrity of an isolated CBM45 domain, revealing a surprisingly high thermal stability (Tm of 84.8 °C). The functionality of CBM45 was demonstrated in planta by yellow/green fluorescent protein fusions and transient expression in tobacco leaves. Affinities for starch and soluble cyclodextrin starch mimics were measured by adsorption assays, surface plasmon resonance and isothermal titration calorimetry analyses. The data indicate that CBM45 binds with an affinity of about two orders of magnitude lower than the classical starch‐binding domains from extracellular microbial amylolytic enzymes. This suggests that low‐affinity starch‐binding domains are a recurring feature in plastidial starch metabolism, and supports the hypothesis that reversible binding, effectuated through low‐affinity interaction with starch granules, facilitates dynamic regulation of enzyme activities and, hence, of starch metabolism.

AB - Starch‐binding domains are noncatalytic carbohydrate‐binding modules that mediate binding to granular starch. The starch‐binding domains from the carbohydrate‐binding module family 45 (CBM45, ) are found as N‐terminal tandem repeats in a small number of enzymes, primarily from photosynthesizing organisms. Isolated domains from representatives of each of the two classes of enzyme carrying CBM45‐type domains, the Solanum tuberosumα‐glucan, water dikinase and the Arabidopsis thaliana plastidial α‐amylase 3, were expressed as recombinant proteins and characterized. Differential scanning calorimetry was used to verify the conformational integrity of an isolated CBM45 domain, revealing a surprisingly high thermal stability (Tm of 84.8 °C). The functionality of CBM45 was demonstrated in planta by yellow/green fluorescent protein fusions and transient expression in tobacco leaves. Affinities for starch and soluble cyclodextrin starch mimics were measured by adsorption assays, surface plasmon resonance and isothermal titration calorimetry analyses. The data indicate that CBM45 binds with an affinity of about two orders of magnitude lower than the classical starch‐binding domains from extracellular microbial amylolytic enzymes. This suggests that low‐affinity starch‐binding domains are a recurring feature in plastidial starch metabolism, and supports the hypothesis that reversible binding, effectuated through low‐affinity interaction with starch granules, facilitates dynamic regulation of enzyme activities and, hence, of starch metabolism.

KW - a-glucan

KW - a-amylase

KW - Starch-binding domain

KW - Starch metabolism

KW - Carbohydrate-binding module

KW - Water dikinase

U2 - 10.1111/j.1742-4658.2011.08043.x

DO - 10.1111/j.1742-4658.2011.08043.x

JO - F E B S Journal

JF - F E B S Journal

SN - 1742-464X

IS - 7

VL - 278

SP - 1175

EP - 1185

ER -