Identification of splicing legumain from Momordica cochinchinesis
Ontology highlight
ABSTRACT:
INSTRUMENT(S): LTQ Orbitrap Elite
ORGANISM(S): Momordica Cochinchinensis
TISSUE(S): Seed
SUBMITTER: 
Xinya Hemu
LAB HEAD: James P. Tam
PROVIDER: PXD028327 | Pride | 2022-02-15
REPOSITORIES: Pride
Publications
The legumain McPAL1 from Momordica cochinchinensis is a highly stable Asx-specific splicing enzyme.
Liew Heng Tai HT To Janet J Zhang Xiaohong X Hemu Xinya X Chan Ning-Yu NY Serra Aida A Sze Siu Kwan SK Liu Chuan-Fa CF Tam James P JP
The Journal of biological chemistry 20211026 6
Legumains, also known as asparaginyl endopeptidases (AEPs), cleave peptide bonds after Asn/Asp (Asx) residues. In plants, certain legumains also have ligase activity that catalyzes biosynthesis of Asx-containing cyclic peptides. An example is the biosynthesis of MCoTI-I/II, a squash family-derived cyclic trypsin inhibitor, which involves splicing to remove the N-terminal prodomain and then N-to-C-terminal cyclization of the mature domain. To identify plant legumains responsible for the maturatio ...[more]
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