Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/164031
Title: Substrate-binding glycine residues are major determinants for hydrolase and ligase activity of plant legumains
Authors: Hemu, Xinya
Chan, Ning-Yu
Liew, Heng Tai
Hu, Side
Zhang, Xiaohong
Serra, Aida
Lescar, Julien
Liu, Chuan-Fa
Tam, James P.
Keywords: Science::Biological sciences
Issue Date: 2023
Source: Hemu, X., Chan, N., Liew, H. T., Hu, S., Zhang, X., Serra, A., Lescar, J., Liu, C. & Tam, J. P. (2023). Substrate-binding glycine residues are major determinants for hydrolase and ligase activity of plant legumains. New Phytologist. https://dx.doi.org/10.1111/nph.18841
Project: MOE2016-T3-1-003 
Journal: New Phytologist 
Abstract: Peptide asparaginyl ligases (PALs) are Asn/Asp(Asx)-specific ligases that are useful for precision modifications of proteins and live-cell surfaces. PALs share high sequence and structural similarity to legumains, asparaginyl endopeptidases (AEPs) that primarily hydrolyze peptide bonds after Asx, thus making it challenging to identify PALs from AEPs. Previously, we showed that the substrate binding sequences flanking the catalytic site can strongly influence the enzymatic direction of a legumain and which we named as ligase activity determinants (LADs). Here, we show that two conserved substrate-binding Gly residues of LADs are critical, but negative determinants for ligase activity, based on a combined bioinformatics analysis of 1,500 plant legumains, mutagenesis, and functional study of 16 novel legumains, plus identification of seven new PALs. We also show that PALs are rare and AEPs are more common, accounting for about 1% and 88%, respectively. Our results suggest that specific glycine residues are molecular determinants to identify PALs and AEPs as two different legumain subfamilies.
URI: https://hdl.handle.net/10356/164031
ISSN: 0028-646X
DOI: 10.1111/nph.18841
Schools: School of Biological Sciences 
Research Centres: NTU Institute of Structural Biology 
Rights: © 2023 New Phytologist Foundation. This is an open access article under the terms of the Creative Commons Attribution-NonCommercial License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes.
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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