A comprehensive practical laboratory course on protein engineering: Evolution of a glycine oxidase variant active on the herbicide glyphosate

2019 ◽  
Vol 47 (6) ◽  
pp. 689-699 ◽  
Author(s):  
Elena Rosini ◽  
Loredano Pollegioni
Keyword(s):  
Protein Engineering ◽  
Laboratory Course ◽  
Glycine Oxidase ◽  
Herbicide Glyphosate

CASCAT: The Power of The Combined Protein Engineering Approach: Evolution of A Glycine Oxidase for A Novel Mechanism of Glyphosate Tolerance☆

2010 ◽  
Vol 150 ◽  
pp. 122-123
Author(s):  
Pollegioni Loredano ◽  
Pedotti Mattia ◽  
Rosini Elena ◽  
Molla Gianluca ◽  
Moschetti Tommaso
Keyword(s):  
Protein Engineering ◽  
Glyphosate Tolerance ◽  
Engineering Approach ◽  
Glycine Oxidase

Complementary laboratory course in cariology

1996 ◽  
Vol 60 (6) ◽  
pp. 533-535
Author(s):  
D Steinberg ◽  
Z Hirschfeld
Keyword(s):  
Laboratory Course

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.

An 8-Year Replication of Key NTVS Findings by Students in a Psychology Laboratory Course

2014 ◽  
Author(s):  
Cheryl B. Stewart ◽  
Zachary Ahlstrom ◽  
Jamie L. Anderson ◽  
Samantha J. Stegura ◽  
Michael S. Ward
Keyword(s):  
Psychology Laboratory ◽  
Laboratory Course

Protein Engineering of Penicillin Acylase

Acta Naturae ◽  
2010 ◽  
Vol 2 (3) ◽  
pp. 47-61 ◽  
Author(s):  
V I Tishkov ◽  
S S Savin ◽  
A S Yasnaya
Keyword(s):  
Protein Engineering ◽  
Penicillin Acylase

Advanced Crop Management and Diagnostics: A Field Laboratory Course

1994 ◽  
Vol 23 (2) ◽  
pp. 93-97
Author(s):  
L. E. Schweitzer ◽  
T. W. Semmel
Keyword(s):  
Crop Management ◽  
Laboratory Course ◽  
Field Laboratory
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