Cloning, sequencing, and expression in Escherichia coli of the Clostridium tetanomorphum gene encoding .beta.-methylaspartase and characterization of the recombinant protein

Biochemistry ◽  
1992 ◽  
Vol 31 (44) ◽  
pp. 10747-10756 ◽  
Author(s):  
Sayed K. Goda ◽  
Nigel P. Minton ◽  
Nigel P. Botting ◽  
David Gani
Keyword(s):  
Escherichia Coli ◽  
Recombinant Protein ◽  
Gene Encoding ◽  
Expression In Escherichia Coli ◽  
Clostridium Tetanomorphum ◽  
Sequencing And Expression

Expression in Escherichia coli of a gene encoding type II l-asparaginase from Bacillus subtilis, and characterization of its unique properties

2010 ◽  
Vol 61 (3) ◽  
pp. 517-524 ◽  
Author(s):  
Yohei Onishi ◽  
Shigekazu Yano ◽  
Jaruwan Thongsanit ◽  
Kazuyoshi Takagi ◽  
Kazuaki Yoshimune ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Bacillus Subtilis ◽  
Type Ii ◽  
Gene Encoding ◽  
Expression In Escherichia Coli

The gene encoding dipeptidyl aminopeptidase BI from Pseudomonas sp. WO24: cloning, sequencing and expression in Escherichia coli

Gene ◽  
1998 ◽  
Vol 206 (2) ◽  
pp. 229-236 ◽  
Author(s):  
Wataru Ogasawara ◽  
Go Kobayashi ◽  
Seiji Ishimaru ◽  
Hirofumi Okada ◽  
Yasushi Morikawa
Keyword(s):  
Escherichia Coli ◽  
Pseudomonas Sp ◽  
Gene Encoding ◽  
Expression In Escherichia Coli ◽  
Sequencing And Expression ◽  
Dipeptidyl Aminopeptidase

scholarly journals Characterization of the First Bacterial and Thermostable GDP-Mannose 3,5-Epimerase

2019 ◽  
Vol 20 (14) ◽  
pp. 3530 ◽  
Author(s):  
Ophelia Gevaert ◽  
Stevie Van Overtveldt ◽  
Koen Beerens ◽  
Tom Desmet
Keyword(s):  
Escherichia Coli ◽  
Recombinant Protein ◽  
Chemical Reactions ◽  
Active Site ◽  
Expression In Escherichia Coli ◽  
Thermophilic Organism ◽  
Sequence Databases

GDP-mannose 3,5-epimerase (GM35E) catalyzes the conversion of GDP-mannose towards GDP-l-galactose and GDP-l-gulose. Although this reaction represents one of the few enzymatic routes towards the production of l-sugars and derivatives, it has not yet been exploited for that purpose. One of the reasons is that so far only GM35Es from plants have been characterized, yielding biocatalysts that are relatively unstable and difficult to express heterologously. Through the mining of sequence databases, we succeeded in identifying a promising bacterial homologue. The gene from the thermophilic organism Methylacidiphilum fumariolicum was codon optimized for expression in Escherichia coli, resulting in the production of 40 mg/L of recombinant protein. The enzyme was found to act as a self-sufficient GM35E, performing three chemical reactions in the same active site. Furthermore, the biocatalyst was highly stable at temperatures up to 55 °C, making it well suited for the synthesis of new carbohydrate products with application in the pharma industry.

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