scholarly journals Turning an Asparaginyl Endopeptidase into a Peptide Ligase

ACS Catalysis ◽  
2020 ◽  
Vol 10 (15) ◽  
pp. 8825-8834 ◽  
Author(s):  
Xinya Hemu ◽  
Abbas El Sahili ◽  
Side Hu ◽  
Xiaohong Zhang ◽  
Aida Serra ◽  
...  
Keyword(s):  
Asparaginyl Endopeptidase

Asparaginyl endopeptidase during maturation and germination of durum wheat

1996 ◽  
Vol 97 (3) ◽  
pp. 475-480 ◽  
Author(s):  
Andrea Bottari ◽  
Antonella Capocchi ◽  
Luciano Galleschi ◽  
Andrea Jopova ◽  
Franco Saviozzi
Keyword(s):  
Durum Wheat ◽  
Asparaginyl Endopeptidase

scholarly journals Use of an Asparaginyl Endopeptidase for Chemo-enzymatic Peptide and Protein Labeling

2020 ◽  
Author(s):  
Simon Tang ◽  
Davide Cardella ◽  
Alexander J. Lander ◽  
Xuefei Li ◽  
Yu-Hsuan Tsai ◽  
...  
Keyword(s):  
Phenylboronic Acid ◽  
Product Formation ◽  
Protein Labeling ◽  
Recognition Sequence ◽  
Reaction Conditions ◽  
Site Specific ◽  
Asparaginyl Endopeptidase ◽  
Coupling System ◽  
Labeling System ◽  
Specific Peptide

Transpeptidases are ideal biocatalysts for site-specific peptide and protein labeling, whereas reactions that target N-terminus cysteine with commercially available reagents have become common practice. However, a versatile approach that allows bioconjugation at the terminus of choice (N or C), while avoiding the use of backbone-modified substrates (<i>e.g.</i> depsipeptide) or large excess of reagent, is highly desirable. Aiming to meet these benchmarks, we have combined the advantages of asparaginyl endopeptidase (AEP) catalysis with a N-terminal cysteine trapping reaction and created a chemo-enzymatic labeling system. In this approach, polypeptide with a Asn-Cys-Leu recognition sequence are ligated with a counterpart possessing an N-terminal Gly-Leu by AEP; the byproduct Cys-Leu is subsequently trapped by a stable and inexpensive scavenger, 2-formyl phenylboronic acid (FPBA), to yield an inert thiazolidine derivative, thereby driving the reaction forward to product formation. By carefully screening the reaction conditions for optimal compatibility and minimal hydrolysis, conversion to the ligated product in the model reaction resulted in excellent yields. The versatility of this AEP ligation/FPBA coupling system was further demonstrated by site-specific labeling the N- or C-termini of various proteins.

scholarly journals Legumain/asparaginyl endopeptidase controls extracellular matrix remodeling through the degradation of fibronectin in mouse renal proximal tubular cells

FEBS Letters ◽  
2007 ◽  
Vol 581 (7) ◽  
pp. 1417-1424 ◽  
Author(s):  
Yoshikata Morita ◽  
Hisazumi Araki ◽  
Toshiro Sugimoto ◽  
Keisuke Takeuchi ◽  
Takuya Yamane ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Extracellular Matrix Remodeling ◽  
Matrix Remodeling ◽  
Proximal Tubular Cells ◽  
Tubular Cells ◽  
Asparaginyl Endopeptidase ◽  
Proximal Tubular ◽  
Renal Proximal Tubular Cells ◽  
Renal Proximal Tubular

Two novel asparaginyl endopeptidase-like cysteine proteinases from the protist Trichomonas vaginalis: their evolutionary relationship within the clan CD cysteine proteinases

Gene ◽  
2004 ◽  
Vol 335 ◽  
pp. 25-35 ◽  
Author(s):  
Josefina León-Félix ◽  
Jaime Ortega-López ◽  
Ricardo Orozco-Solı́s ◽  
Rossana Arroyo
Keyword(s):  
Trichomonas Vaginalis ◽  
Evolutionary Relationship ◽  
Cysteine Proteinases ◽  
Asparaginyl Endopeptidase

scholarly journals Recent advances in the development of legumain-selective chemical probes and peptide prodrugs

2019 ◽  
Vol 400 (12) ◽  
pp. 1529-1550 ◽  
Author(s):  
Marcin Poreba
Keyword(s):  
Small Molecule ◽  
Molecular Target ◽  
Biological Processes ◽  
Chemical Probes ◽  
Moth Bean ◽  
Historical Perspectives ◽  
Asparaginyl Endopeptidase ◽  
Cellular Events ◽  
Leguminous Seeds ◽  
Extracellular Activity

Abstract Legumain, which is also known as vacuolar processing enzyme (VPE) or asparaginyl endopeptidase (AEP), is a cysteine protease that was first discovered and characterized in the leguminous seeds of the moth bean in the early 1990s. Later, this enzyme was also detected in higher organisms, including eukaryotes. This pH-dependent protease displays the highest activity in acidic endolysosomal compartments; however, legumain also displays nuclear, cytosolic and extracellular activity when stabilized by other proteins or intramolecular complexes. Based on the results from over 25 years of research, this protease is involved in multiple cellular events, including protein degradation and antigen presentation. Moreover, when dysregulated, this protease contributes to the progression of several diseases, with cancer being the well-studied example. Research on legumain biology was undoubtedly facilitated by the use of small molecule chemical tools. Therefore, in this review, I present the historical perspectives and most current strategies for the development of small molecule substrates, inhibitors and activity-based probes for legumain. These tools are of paramount importance in elucidating the roles of legumain in multiple biological processes. Finally, as this enzyme appears to be a promising molecular target for anticancer therapies, the development of legumain-activated prodrugs is also described.

scholarly journals Asparaginyl endopeptidase from the carcinogenic liver fluke, Opisthorchis viverrini, and its potential for serodiagnosis

2008 ◽  
Vol 12 (6) ◽  
pp. e49-e59 ◽  
Author(s):  
Thewarach Laha ◽  
Jittiyawadee Sripa ◽  
Banchob Sripa ◽  
Mark Pearson ◽  
Leon Tribolet ◽  
...  
Keyword(s):  
Liver Fluke ◽  
Opisthorchis Viverrini ◽  
Asparaginyl Endopeptidase

Characterization of asparaginyl endopeptidase activity in endosperm of developing and germinating castor oil seeds

1994 ◽  
Vol 91 (4) ◽  
pp. 599-604 ◽  
Author(s):  
Fiona A. Cornel ◽  
William C. Plaxton
Keyword(s):  
Castor Oil ◽  
Oil Seeds ◽  
Asparaginyl Endopeptidase ◽  
Endopeptidase Activity

scholarly journals Synthesis and evaluation of aza-peptidyl inhibitors of the lysosomal asparaginyl endopeptidase, legumain

2012 ◽  
Vol 22 (3) ◽  
pp. 1340-1343 ◽  
Author(s):  
Jiyoun Lee ◽  
Matthew Bogyo
Keyword(s):  
Asparaginyl Endopeptidase ◽  
Peptidyl Inhibitors

scholarly journals Functional Role of Asparaginyl Endopeptidase Ubiquitination by TRAF6 in Tumor Invasion and Metastasis

2014 ◽  
Vol 106 (4) ◽  
Author(s):  
Yingying Lin ◽  
Yongming Qiu ◽  
Cheng Xu ◽  
Qiaoling Liu ◽  
Baowei Peng ◽  
...  
Keyword(s):  
Tumor Invasion ◽  
Functional Role ◽  
Invasion And Metastasis ◽  
Asparaginyl Endopeptidase

In vitro splicing of concanavalin A is catalyzed by asparaginyl endopeptidase

1994 ◽  
Vol 1 (8) ◽  
pp. 502-504 ◽  
Author(s):  
Wang Min ◽  
D. Hugh Jones
Keyword(s):  
Concanavalin A ◽  
Asparaginyl Endopeptidase ◽  
In Vitro Splicing
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