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

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

Standard

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

In: FEBS Letters, Vol. 586, No. 16, 30.07.2012, p. 2479-2482.

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

Harvard

Jensen, JM, Hägglund, P, Christensen, HEM & Svensson, B 2012, 'Inactivation of barley limit dextrinase inhibitor by thioredoxin-catalysed disulfide reduction', FEBS Letters, vol. 586, no. 16, pp. 2479-2482. https://doi.org/10.1016/j.febslet.2012.06.009

APA

Jensen, J. M., Hägglund, P., Christensen, H. E. M., & Svensson, B. (2012). Inactivation of barley limit dextrinase inhibitor by thioredoxin-catalysed disulfide reduction. FEBS Letters, 586(16), 2479-2482. https://doi.org/10.1016/j.febslet.2012.06.009

Vancouver

Jensen JM, Hägglund P, Christensen HEM, Svensson B. Inactivation of barley limit dextrinase inhibitor by thioredoxin-catalysed disulfide reduction. FEBS Letters. 2012 Jul 30;586(16):2479-2482. https://doi.org/10.1016/j.febslet.2012.06.009

Author

Jensen, Johanne Morch ; Hägglund, Per ; Christensen, Hans Erik Molager ; Svensson, Birte. / Inactivation of barley limit dextrinase inhibitor by thioredoxin-catalysed disulfide reduction. In: FEBS Letters. 2012 ; Vol. 586, No. 16. pp. 2479-2482.

Bibtex

@article{bfb20a20b4c54a8c8dc8ceb59a08c8e9,
title = "Inactivation of barley limit dextrinase inhibitor by thioredoxin-catalysed disulfide reduction",
abstract = "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. Crown",
keywords = "Electrospray ionisation mass spectrometry, Glutathione, Seed germination, Starch mobilisation, Thioredoxin h",
author = "Jensen, {Johanne Morch} and Per H{\"a}gglund and Christensen, {Hans Erik Molager} and Birte Svensson",
year = "2012",
month = jul,
day = "30",
doi = "10.1016/j.febslet.2012.06.009",
language = "English",
volume = "586",
pages = "2479--2482",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd",
number = "16",

}

RIS

TY - JOUR

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

AU - Jensen, Johanne Morch

AU - Hägglund, Per

AU - Christensen, Hans Erik Molager

AU - Svensson, Birte

PY - 2012/7/30

Y1 - 2012/7/30

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. Crown

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. Crown

KW - Electrospray ionisation mass spectrometry

KW - Glutathione

KW - Seed germination

KW - Starch mobilisation

KW - Thioredoxin h

UR - http://www.scopus.com/inward/record.url?scp=84864283205&partnerID=8YFLogxK

U2 - 10.1016/j.febslet.2012.06.009

DO - 10.1016/j.febslet.2012.06.009

M3 - Journal article

C2 - 22728244

AN - SCOPUS:84864283205

VL - 586

SP - 2479

EP - 2482

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 16

ER -

ID: 240159896