scholarly journals Cloning and characterization of the Bacillus subtilis birA gene encoding a repressor of the biotin operon.

1995 ◽  
Vol 177 (9) ◽  
pp. 2572-2575 ◽  
Author(s):  
S Bower ◽  
J Perkins ◽  
R R Yocum ◽  
P Serror ◽  
A Sorokin ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Gene Encoding

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

Cloning and characterization of the Bacillus subtilis prkA gene encoding a novel serine protein kinase

Gene ◽  
1996 ◽  
Vol 168 (1) ◽  
pp. 55-60 ◽  
Author(s):  
Cécile Fischer ◽  
Christophe Geourjon ◽  
Claude Bourson ◽  
Josef Deutscher
Keyword(s):  
Bacillus Subtilis ◽  
Protein Kinase ◽  
Gene Encoding

Cloning and Characterization of the yjeA Gene, Encoding a Novel Deoxyribonuclease, from Bacillus subtilis

2007 ◽  
Vol 142 (5) ◽  
pp. 647-654 ◽  
Author(s):  
K.-L. Ng ◽  
C.-C. Lam ◽  
Z. Fu ◽  
Y.-F. Han ◽  
K. W.K. Tsim ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Gene Encoding

Gene cloning and characterization of glycine oxidase from newly isolated Bacillus subtilis strain R5

Biologia ◽  
2011 ◽  
Vol 66 (1) ◽  
pp. 1-7 ◽  
Author(s):  
Farrukh Jamil ◽  
Naeem Rashid ◽  
Qurra-tul-Ann Gardner ◽  
Muhammad Akhtar
Keyword(s):  
Enzyme Activity ◽  
Bacillus Subtilis ◽  
Specific Activity ◽  
Subtilis Strain ◽  
Amino Acid Residues ◽  
Expression And Purification ◽  
Gene Encoding ◽  
Glycine Oxidase ◽  
Bacillus Subtilis Strain R5

AbstractThe gene encoding the glycine oxidase from Bacillus subtilis strain R5 (goxR) was cloned and expressed in Escherichia coli. The gene consisted of 1,110 nucleotides that encoded a protein (GoxR) of 369 amino acid residues with a molecular mass of 40,761 Da. The GoxR exhibited 98.6% identity with glycine oxidase from B. subtilis strain 168. Gene expression and purification of the recombinant GoxR were performed. The recombinant GoxR existed in a homotetramer form. The recombinant protein effectively catalyzed the oxidation of glycine and d-alanine. The specific activity of the purified recombinant GoxR was 0.96 U/mg when glycine was used as a substrate and 1.0 U/mg when d-alanine was substrate. The enzyme displayed its highest activity at pH 8.0 and at a temperature of 50°C. The activation energy of the reaction catalyzed by the enzyme was calculated to be 26 kJ/mol. The enzyme activity was significantly inhibited in the presence of organic solvents. No enhancement of enzyme activity was observed in the presence of metal cations. The experimental results presented in this study demonstrate that the enzyme was a bonafide glycine oxidase.

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