Irreversible Sortase A-Mediated Ligation Driven by Diketopiperazine Formation

2014 ◽  
Vol 79 (2) ◽  
pp. 487-492 ◽  
Author(s):  
Fa Liu ◽  
Ethan Y. Luo ◽  
David B. Flora ◽  
Adam R. Mezo
Keyword(s):  
Sortase A ◽  
Diketopiperazine Formation

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

Influence of Solvents upon Diketopiperazine Formation of FPG8K

2021 ◽  
Author(s):  
Zhi-chao Zhang ◽  
Shannon A. Raab ◽  
David A. Hales ◽  
David E. Clemmer
Keyword(s):  
Diketopiperazine Formation ◽  
Influence Of Solvents

scholarly journals Sorting out the Superbugs: Potential of Sortase A Inhibitors among Other Antimicrobial Strategies to Tackle the Problem of Antibiotic Resistance

Antibiotics ◽  
2021 ◽  
Vol 10 (2) ◽  
pp. 164 ◽  
Author(s):  
Nikita Zrelovs ◽  
Viktorija Kurbatska ◽  
Zhanna Rudevica ◽  
Ainars Leonchiks ◽  
Davids Fridmanis
Keyword(s):  
Cell Wall ◽  
Antibiotic Resistance ◽  
Pathogenic Bacteria ◽  
Resistance Mechanisms ◽  
Surface Proteins ◽  
Sortase A ◽  
Inhibitory Compounds ◽  
Alternative Means ◽  
Alternative Approaches ◽  
Conventional Antibiotics

Rapid spread of antibiotic resistance throughout the kingdom bacteria is inevitably bringing humanity towards the “post-antibiotic” era. The emergence of so-called “superbugs”—pathogen strains that develop resistance to multiple conventional antibiotics—is urging researchers around the globe to work on the development or perfecting of alternative means of tackling the pathogenic bacteria infections. Although various conceptually different approaches are being considered, each comes with its advantages and drawbacks. While drug-resistant pathogens are undoubtedly represented by both Gram(+) and Gram(−) bacteria, possible target spectrum across the proposed alternative approaches of tackling them is variable. Numerous anti-virulence strategies aimed at reducing the pathogenicity of target bacteria rather than eliminating them are being considered among such alternative approaches. Sortase A (SrtA) is a membrane-associated cysteine protease that catalyzes a cell wall sorting reaction by which surface proteins, including virulence factors, are anchored to the bacterial cell wall of Gram(+) bacteria. Although SrtA inhibition seems perspective among the Gram-positive pathogen-targeted antivirulence strategies, it still remains less popular than other alternatives. A decrease in virulence due to inactivation of SrtA activity has been extensively studied in Staphylococcus aureus, but it has also been demonstrated in other Gram(+) species. In this manuscript, results of past studies on the discovery of novel SrtA inhibitory compounds and evaluation of their potency were summarized and commented on. Here, we discussed the rationale behind the inhibition of SrtA, raised some concerns on the comparability of the results from different studies, and touched upon the possible resistance mechanisms as a response to implementation of such therapy in practice. The goal of this article is to encourage further studies of SrtA inhibitory compounds.

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

scholarly journals Streptavidin-hydrogel prepared by sortase A-assisted click chemistry for enzyme immobilization on an electrode

2018 ◽  
Vol 99 ◽  
pp. 56-61 ◽  
Author(s):  
Takuya Matsumoto ◽  
Yuki Isogawa ◽  
Tsutomu Tanaka ◽  
Akihiko Kondo
Keyword(s):  
Click Chemistry ◽  
Enzyme Immobilization ◽  
Sortase A

scholarly journals In situ regeneration of bioactive coatings enabled by an evolved Staphylococcus aureus sortase A

2016 ◽  
Vol 7 (1) ◽  
Author(s):  
Hyun Ok Ham ◽  
Zheng Qu ◽  
Carolyn A. Haller ◽  
Brent M. Dorr ◽  
Erbin Dai ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Sortase A ◽  
Bioactive Coatings ◽  
In Situ Regeneration
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