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

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

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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.
Original languageEnglish
JournalF E B S Letters
Publication date2012
Volume586
Issue16
Pages2479-2482
ISSN0014-5793
DOIs
StatePublished
CitationsWeb of Science® Times Cited: 2

Keywords

  • Thioredoxin h, Starch mobilisation, Seed germination, Glutathione, Electrospray ionisation mass spectrometry
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