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Characterization of legumain degradation of intact proteins

ABSTRACT: Legumain or asparagine endopeptidase is a unique cysteine endopeptidase with a distinctive specificity for the hydrolysis of peptide bonds after asparagine and to a lesser extent after aspartate. In order to improve our understanding of legumain substrate recognition we have performed proteomic profiling of legumain specificity on native proteins using two different N-terminal labelling methodologies (FPPS and ISIL). Our data revealed a strict P1 specificity of legumain with clear cleavage preference for unstructured secondary regions in the substrate proteins. No extended cleavage specificity on native proteins was observed. Moreover, a limited number of identified cleavages on individual substrates suggest its primary role in precision proteolysis and regulatory proteolytic events.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Marko Fonovic

LAB HEAD: Marko Fonovic

PROVIDER: PXD010466 | Pride | 2018-11-29

REPOSITORIES: Pride

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			Action	DRS
	FPPS_Ctrl_01.raw	Raw
	FPPS_Ctrl_02.raw	Raw
	FPPS_Ctrl_03.raw	Raw
	FPPS_Ctrl_04.raw	Raw
	FPPS_Ctrl_05.raw	Raw

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