Inactivation of barley limit dextrinase inhibitor by thioredoxin-catalysed disulfide reduction

Publication: Research - peer-reviewJournal article – Annual report year: 2012

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Inactivation of barley limit dextrinase inhibitor by thioredoxin-catalysed disulfide reduction. / Jensen, Johanne Mørch; Hägglund, Per; Christensen, Hans Erik Mølager; Svensson, Birte.

In: F E B S Letters, Vol. 586, No. 16, 2012, p. 2479-2482.

Publication: Research - peer-reviewJournal article – Annual report year: 2012

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Jensen, Johanne Mørch; Hägglund, Per; Christensen, Hans Erik Mølager; Svensson, Birte / Inactivation of barley limit dextrinase inhibitor by thioredoxin-catalysed disulfide reduction.

In: F E B S Letters, Vol. 586, No. 16, 2012, p. 2479-2482.

Publication: Research - peer-reviewJournal article – Annual report year: 2012

Bibtex

@article{1c5a24566ddf4064ae4227b8e8ddd512,
title = "Inactivation of barley limit dextrinase inhibitor by thioredoxin-catalysed disulfide reduction",
keywords = "Thioredoxin h, Starch mobilisation, Seed germination, Glutathione, Electrospray ionisation mass spectrometry",
publisher = "Elsevier BV",
author = "Jensen, {Johanne Mørch} and Per Hägglund and Christensen, {Hans Erik Mølager} and Birte Svensson",
year = "2012",
doi = "10.1016/j.febslet.2012.06.009",
volume = "586",
number = "16",
pages = "2479--2482",
journal = "F E B S Letters",
issn = "0014-5793",

}

RIS

TY - JOUR

T1 - Inactivation of barley limit dextrinase inhibitor by thioredoxin-catalysed disulfide reduction

A1 - Jensen,Johanne Mørch

A1 - Hägglund,Per

A1 - Christensen,Hans Erik Mølager

A1 - Svensson,Birte

AU - Jensen,Johanne Mørch

AU - Hägglund,Per

AU - Christensen,Hans Erik Mølager

AU - Svensson,Birte

PB - Elsevier BV

PY - 2012

Y1 - 2012

N2 - Barley limit dextrinase (LD) that catalyses hydrolysis of α-1,6 glucosidic linkages in starch-derived dextrins is inhibited by limit dextrinase inhibitor (LDI) found in mature seeds. LDI belongs to the chloroform/methanol soluble protein family (CM-protein family) and has four disulfide bridges and one glutathionylated cysteine. Here, thioredoxin is shown to progressively reduce disulfide bonds in LDI accompanied by loss of activity. A preferential reduction of the glutathionylated cysteine, as indicated by thiol quantification and molecular mass analysis using electrospray ionisation mass spectrometry, was not related to LDI inactivation. LDI reduction is proposed to cause conformational destabilisation leading to loss of function.

AB - Barley limit dextrinase (LD) that catalyses hydrolysis of α-1,6 glucosidic linkages in starch-derived dextrins is inhibited by limit dextrinase inhibitor (LDI) found in mature seeds. LDI belongs to the chloroform/methanol soluble protein family (CM-protein family) and has four disulfide bridges and one glutathionylated cysteine. Here, thioredoxin is shown to progressively reduce disulfide bonds in LDI accompanied by loss of activity. A preferential reduction of the glutathionylated cysteine, as indicated by thiol quantification and molecular mass analysis using electrospray ionisation mass spectrometry, was not related to LDI inactivation. LDI reduction is proposed to cause conformational destabilisation leading to loss of function.

KW - Thioredoxin h

KW - Starch mobilisation

KW - Seed germination

KW - Glutathione

KW - Electrospray ionisation mass spectrometry

U2 - 10.1016/j.febslet.2012.06.009

DO - 10.1016/j.febslet.2012.06.009

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 16

VL - 586

SP - 2479

EP - 2482

ER -