Journal article
Inactivation of barley limit dextrinase inhibitor by thioredoxin-catalysed disulfide reduction
Department of Systems Biology, Technical University of Denmark1
Enzyme and Protein Chemistry, Department of Systems Biology, Technical University of Denmark2
Department of Chemistry, Technical University of Denmark3
Metalloprotein Chemistry and Engineering, Department of Chemistry, Technical University of Denmark4
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.
Language: | English |
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Publisher: | Wiley |
Year: | 2012 |
Pages: | 2479-2482 |
ISSN: | 18733468 and 00145793 |
Types: | Journal article |
DOI: | 10.1016/j.febslet.2012.06.009 |
ORCIDs: | 0000-0002-6627-7518 , Christensen, Hans Erik Mølager and Svensson, Birte |