Ca2+-independent sortase-A exhibits high selective protein ligation activity in the cytoplasm ofEscherichia coli

2015 ◽  
Vol 10 (9) ◽  
pp. 1487-1492 ◽  
Author(s):  
Hidehiko Hirakawa ◽  
Suguru Ishikawa ◽  
Teruyuki Nagamune
Keyword(s):  
Ofescherichia Coli ◽  
Sortase A ◽  
Protein Ligation

Enhancement of sortase A-mediated protein ligation by inducing a β-hairpin structure around the ligation site

2011 ◽  
Vol 47 (16) ◽  
pp. 4742 ◽  
Author(s):  
Yuichi Yamamura ◽  
Hidehiko Hirakawa ◽  
Satoshi Yamaguchi ◽  
Teruyuki Nagamune
Keyword(s):  
Hairpin Structure ◽  
Sortase A ◽  
Protein Ligation ◽  
Ligation Site

Engineering of an anti-epidermal growth factor receptor antibody to single chain format and labeling by sortase A-mediated protein ligation

2011 ◽  
Vol 109 (6) ◽  
pp. 1461-1470 ◽  
Author(s):  
Mariusz P. Madej ◽  
Gregory Coia ◽  
Charlotte C. Williams ◽  
Joanne M. Caine ◽  
Lesley A. Pearce ◽  
...  
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Growth Factor Receptor ◽  
Sortase A ◽  
Single Chain ◽  
Protein Ligation ◽  
Receptor Antibody ◽  
Epidermal Growth

Enzymatic activity of circular sortase A under denaturing conditions: An advanced tool for protein ligation

2014 ◽  
Vol 82 ◽  
pp. 200-209 ◽  
Author(s):  
D. Zhulenkovs ◽  
K. Jaudzems ◽  
A. Zajakina ◽  
A. Leonchiks
Keyword(s):  
Enzymatic Activity ◽  
Sortase A ◽  
Protein Ligation ◽  
Advanced Tool

Insights into the biochemical and functional characterization of sortase E transpeptidase of Corynebacterium glutamicum

2019 ◽  
Vol 476 (24) ◽  
pp. 3835-3847 ◽  
Author(s):  
Aliyath Susmitha ◽  
Kesavan Madhavan Nampoothiri ◽  
Harsha Bajaj
Keyword(s):  
Protein Engineering ◽  
Cell Attachment ◽  
Functional Characterization ◽  
Protein Structures ◽  
Structural Similarity ◽  
Surface Proteins ◽  
Sortase A ◽  
Peptide Cleavage ◽  
New Findings

Most Gram-positive bacteria contain a membrane-bound transpeptidase known as sortase which covalently incorporates the surface proteins on to the cell wall. The sortase-displayed protein structures are involved in cell attachment, nutrient uptake and aerial hyphae formation. Among the six classes of sortase (A–F), sortase A of S. aureus is the well-characterized housekeeping enzyme considered as an ideal drug target and a valuable biochemical reagent for protein engineering. Similar to SrtA, class E sortase in GC rich bacteria plays a housekeeping role which is not studied extensively. However, C. glutamicum ATCC 13032, an industrially important organism known for amino acid production, carries a single putative sortase (NCgl2838) gene but neither in vitro peptide cleavage activity nor biochemical characterizations have been investigated. Here, we identified that the gene is having a sortase activity and analyzed its structural similarity with Cd-SrtF. The purified enzyme showed a greater affinity toward LAXTG substrate with a calculated KM of 12 ± 1 µM, one of the highest affinities reported for this class of enzyme. Moreover, site-directed mutation studies were carried to ascertain the structure functional relationship of Cg-SrtE and all these are new findings which will enable us to perceive exciting protein engineering applications with this class of enzyme from a non-pathogenic microbe.

Sortase A Mediated Protein Modifications and Peptide Conjugations

2016 ◽  
Vol 12 (4) ◽  
pp. 205-213 ◽  
Author(s):  
Natalya Voloshchuk ◽  
Danni Liang ◽  
Jun Liang
Keyword(s):  
Sortase A ◽  
Protein Modifications

Morphology and growth pattern of a rod-negativeenv B mutant ofEscherichia coli K12

1974 ◽  
Vol 14 (6) ◽  
pp. 465-477 ◽  
Author(s):  
G. D. Bloom ◽  
J. Gumpert ◽  
S. Normark ◽  
E. Schuhmann ◽  
U. Taubeneck ◽  
...  
Keyword(s):  
Growth Pattern ◽  
Ofescherichia Coli
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