Proteomics

Dataset Information

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AtLEGbeta / gamma protease specificity and putative substrate characterization by HUNTER


ABSTRACT: Arabidopsis thaliana Legumain (aka VPE) beta / gamma were characterized for their cleavage specificity and putative substrates were identified by the N-termini enrichment method HUNTER.

INSTRUMENT(S): impact II

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Leaf

SUBMITTER: Fatih Demir  

LAB HEAD: Pitter Florian Huesgen

PROVIDER: PXD019276 | Pride | 2020-07-29

REPOSITORIES: Pride

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Publications

Structural and functional studies of <i>Arabidopsis thaliana</i> legumain beta reveal isoform specific mechanisms of activation and substrate recognition.

Dall Elfriede E   Zauner Florian B FB   Soh Wai Tuck WT   Demir Fatih F   Dahms Sven O SO   Cabrele Chiara C   Huesgen Pitter F PF   Brandstetter Hans H  

The Journal of biological chemistry 20200721 37


The vacuolar cysteine protease legumain plays important functions in seed maturation and plant programmed cell death. Because of their dual protease and ligase activity, plant legumains have become of particular biotechnological interest, <i>e.g.</i> for the synthesis of cyclic peptides for drug design or for protein engineering. However, the molecular mechanisms behind their dual protease and ligase activities are still poorly understood, limiting their applications. Here, we present the crysta  ...[more]

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