Design of a Specific Peptide Tag that Affords Covalent and Site-Specific Enzyme Immobilization Catalyzed by Microbial Transglutaminase

2005 ◽  
Vol 6 (4) ◽  
pp. 2299-2304 ◽  
Author(s):  
Jo Tominaga ◽  
Noriho Kamiya ◽  
Satoshi Doi ◽  
Hirofumi Ichinose ◽  
Tatsuo Maruyama ◽  
...  
ChemBioChem ◽  
2018 ◽  
Vol 19 (4) ◽  
pp. 369-378 ◽  
Author(s):  
Oscar Romero ◽  
Blanca de las Rivas ◽  
David Lopez-Tejedor ◽  
Jose M. Palomo

2015 ◽  
Vol 112 (10) ◽  
pp. 2016-2024 ◽  
Author(s):  
Zsofia Botyanszki ◽  
Pei Kun R. Tay ◽  
Peter Q. Nguyen ◽  
Martin G. Nussbaumer ◽  
Neel S. Joshi

ChemBioChem ◽  
2017 ◽  
Vol 18 (19) ◽  
pp. 1923-1927 ◽  
Author(s):  
Philipp R. Spycher ◽  
Christian A. Amann ◽  
Jöri E. Wehrmüller ◽  
David R. Hurwitz ◽  
Olivier Kreis ◽  
...  

2021 ◽  
Author(s):  
Penny J. Le ◽  
Shane Miersch ◽  
Matthew W. Forbes ◽  
Nick Jarvik ◽  
Anthony Ku ◽  
...  

2020 ◽  
Author(s):  
Simon Tang ◽  
Davide Cardella ◽  
Alexander J. Lander ◽  
Xuefei Li ◽  
Yu-Hsuan Tsai ◽  
...  

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.


2016 ◽  
Vol 18 (2) ◽  
pp. 422-430 ◽  
Author(s):  
Rie Wakabayashi ◽  
Kensuke Yahiro ◽  
Kounosuke Hayashi ◽  
Masahiro Goto ◽  
Noriho Kamiya

2004 ◽  
Vol 35 (6-7) ◽  
pp. 613-618 ◽  
Author(s):  
Jo Tominaga ◽  
Noriho Kamiya ◽  
Satoshi Doi ◽  
Hirofumi Ichinose ◽  
Masahiro Goto

2004 ◽  
pp. 191-204 ◽  
Author(s):  
Mahesh Uttamchandani ◽  
Grace Y. J. Chen ◽  
Marie-Laure Lesaicherre ◽  
Shao Q. Yao

2001 ◽  
Vol 12 (5) ◽  
pp. 701-710 ◽  
Author(s):  
Haruya Sato ◽  
Eiko Hayashi ◽  
Naoyuki Yamada ◽  
Masanobu Yatagai ◽  
Yoshiyuki Takahara

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