Peptide asparaginyl ligases—renegade peptide bond makers

Making peptide bonds is tightly controlled by genetic code and machinery which includes cofactors, ATP, and RNAs. In this regard, the stand-alone and genetic-code-independent peptide ligases constitute a new family of renegade peptide-bond makers. A prime example is butelase-1, an Asn/Asp(Asx)-speci...

Full description

Saved in:
Bibliographic Details
Main Authors: Tam, James P., Chan, Ning-Yu, Liew, Heng Tai, Tan, Shaun J., Chen, Yu
Other Authors: School of Biological Sciences
Format: Article
Language:English
Published: 2021
Subjects:
Online Access:https://hdl.handle.net/10356/148282
Tags: Add Tag
No Tags, Be the first to tag this record!
Institution: Nanyang Technological University
Language: English
id sg-ntu-dr.10356-148282
record_format dspace
spelling sg-ntu-dr.10356-1482822023-02-28T16:59:06Z Peptide asparaginyl ligases—renegade peptide bond makers Tam, James P. Chan, Ning-Yu Liew, Heng Tai Tan, Shaun J. Chen, Yu School of Biological Sciences NTU Institute of Structural Biology Science Asparaginyl Endopeptidase Asn-specific Ligation Making peptide bonds is tightly controlled by genetic code and machinery which includes cofactors, ATP, and RNAs. In this regard, the stand-alone and genetic-code-independent peptide ligases constitute a new family of renegade peptide-bond makers. A prime example is butelase-1, an Asn/Asp(Asx)-specific ligase that structurally belongs to the asparaginyl endopeptidase family. Butelase-1 specifically recognizes a C-terminal Asx-containing tripeptide motif, Asn/Asp-Xaa-Yaa (Xaa and Yaa are any amino acids), to form a site-specific Asn-Xaa peptide bond either intramolecularly as cyclic proteins or intermolecularly as modified proteins. Our work in the past five years has validated that butelase-1 is a potent and versatile ligase. Here we review the advances in ligases, with a focus on butelase-1, and their applications in engineering bioactive peptides and precision protein modifications, antibody-drug conjugates, and live-cell labeling. Ministry of Education (MOE) Accepted version This work was supported by Academic Research Grant Tier 3 (MOE2016-T3-1-003) from the Singapore Ministry of Education 2021-04-22T09:20:56Z 2021-04-22T09:20:56Z 2020 Journal Article Tam, J. P., Chan, N., Liew, H. T., Tan, S. J. & Chen, Y. (2020). Peptide asparaginyl ligases—renegade peptide bond makers. Science China Chemistry, 63(3), 296-307. https://dx.doi.org/10.1007/s11426-019-9648-3 1869-1870 https://hdl.handle.net/10356/148282 10.1007/s11426-019-9648-3 3 63 296 307 en Science China Chemistry © 2020 Science in China Press and Springer-Verlag GmbH Germany, part of Springer Nature. All rights reserved. This paper was published in Science China Chemistryand is made available with permission of Science in China Press. The original publication is available at www.scichina.com and www.springerlink.com. application/pdf
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic Science
Asparaginyl Endopeptidase
Asn-specific Ligation
spellingShingle Science
Asparaginyl Endopeptidase
Asn-specific Ligation
Tam, James P.
Chan, Ning-Yu
Liew, Heng Tai
Tan, Shaun J.
Chen, Yu
Peptide asparaginyl ligases—renegade peptide bond makers
description Making peptide bonds is tightly controlled by genetic code and machinery which includes cofactors, ATP, and RNAs. In this regard, the stand-alone and genetic-code-independent peptide ligases constitute a new family of renegade peptide-bond makers. A prime example is butelase-1, an Asn/Asp(Asx)-specific ligase that structurally belongs to the asparaginyl endopeptidase family. Butelase-1 specifically recognizes a C-terminal Asx-containing tripeptide motif, Asn/Asp-Xaa-Yaa (Xaa and Yaa are any amino acids), to form a site-specific Asn-Xaa peptide bond either intramolecularly as cyclic proteins or intermolecularly as modified proteins. Our work in the past five years has validated that butelase-1 is a potent and versatile ligase. Here we review the advances in ligases, with a focus on butelase-1, and their applications in engineering bioactive peptides and precision protein modifications, antibody-drug conjugates, and live-cell labeling.
author2 School of Biological Sciences
author_facet School of Biological Sciences
Tam, James P.
Chan, Ning-Yu
Liew, Heng Tai
Tan, Shaun J.
Chen, Yu
format Article
author Tam, James P.
Chan, Ning-Yu
Liew, Heng Tai
Tan, Shaun J.
Chen, Yu
author_sort Tam, James P.
title Peptide asparaginyl ligases—renegade peptide bond makers
title_short Peptide asparaginyl ligases—renegade peptide bond makers
title_full Peptide asparaginyl ligases—renegade peptide bond makers
title_fullStr Peptide asparaginyl ligases—renegade peptide bond makers
title_full_unstemmed Peptide asparaginyl ligases—renegade peptide bond makers
title_sort peptide asparaginyl ligases—renegade peptide bond makers
publishDate 2021
url https://hdl.handle.net/10356/148282
_version_ 1759857765905334272