Thermostable Farnesyl Diphosphate Synthase of Bacillus stearothermophilus: Molecular Cloning, Sequence Determination, Overproduction, and Purification1

1993 ◽  
Vol 113 (3) ◽  
pp. 355-263 ◽  
Author(s):  
Tanetoshi Koyama ◽  
Shusei Obata ◽  
Masami Osabe ◽  
Ayumi Takeshita ◽  
Ken Yokoyama ◽  
...  
Keyword(s):  
Molecular Cloning ◽  
Bacillus Stearothermophilus ◽  
Farnesyl Diphosphate ◽  
Farnesyl Diphosphate Synthase ◽  
Sequence Determination

Site-directed mutagenesis of farnesyl diphosphate synthase; effect of substitution on the three carboxyl-terminal amino acids

1994 ◽  
Vol 72 (1) ◽  
pp. 75-79 ◽  
Author(s):  
Tanetoshi Koyama ◽  
Kazuhiro Saito ◽  
Kyozo Ogura ◽  
Shusei Obata ◽  
Ayumi Takeshita
Keyword(s):  
Amino Acids ◽  
Bacillus Stearothermophilus ◽  
Farnesyl Diphosphate ◽  
Site Directed Mutagenesis ◽  
Farnesyl Diphosphate Synthase ◽  
Wild Type ◽  
Wild Type Enzyme ◽  
Directed Mutation ◽  
Catalytic Function ◽  
Terminal Amino

Site-directed mutation was introduced into the gene for the farnesyl diphosphate synthase of Bacillus stearothermophilus. To investigate the significance of the three C-terminal amino acids, where arginine is completely conserved throughout the farnesyl diphosphate synthases of prokaryotes and eukaryotes, three kinds of mutant enzymes, R295V, D296G, and H297L, which have replacements of arginine-295 with valine, aspartate-296 with glycine, and histidine-297 with leucine, respectively, were overproduced and purified to homogeneity. All of the three mutant enzymes showed similar catalytic activities to that of the wild-type enzyme, indicating that the basic amino acids including the conserved arginine in the C-terminal region are not essential for catalytic function. They were also similar to the wild-type enzyme with respect to pH optima, thermostability, reaction product, and kinetic parameters for allylic substrates. However, their Km values for isopentenyl diphosphate are approximately twice that of the wild type.

Substrate specificity of farnesyl diphosphate synthase from Bacillus stearothermophilus

1995 ◽  
Vol 5 (15) ◽  
pp. 1605-1608 ◽  
Author(s):  
Yuji Maki ◽  
Akiko Masukawa ◽  
Hideaki Ono ◽  
Takae Endo ◽  
Tanetoshi Koyama ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Bacillus Stearothermophilus ◽  
Farnesyl Diphosphate ◽  
Farnesyl Diphosphate Synthase

ChemInform Abstract: An Artificial Substrate for the Thermostable Farnesyl Diphosphate Synthase from Bacillus stearothermophilus

ChemInform ◽  
2010 ◽  
Vol 28 (45) ◽  
pp. no-no
Author(s):  
M. NAGAKI ◽  
T. KOYAMA ◽  
T. NISHINO ◽  
K. SHIMIZU ◽  
Y. MAKI ◽  
...  
Keyword(s):  
Bacillus Stearothermophilus ◽  
Farnesyl Diphosphate ◽  
Artificial Substrate ◽  
Farnesyl Diphosphate Synthase

Molecular Cloning, Characterisation, and Heterologous Expression of Farnesyl Diphosphate Synthase from Sanghuangporus baumii

2020 ◽  
Vol 62 (2) ◽  
pp. 132-141 ◽  
Author(s):  
Xutong Wang ◽  
Tingting Sun ◽  
Jian Sun ◽  
Shixin Wang ◽  
Yisha Ma ◽  
...  
Keyword(s):  
Heterologous Expression ◽  
Molecular Cloning ◽  
Farnesyl Diphosphate ◽  
Farnesyl Diphosphate Synthase
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