EC Number   |
Protein Variants |
Reference |
|---|
   1.3.7.11 | F219L |
site-directed mutagenesis, the mutant enzymes ceases GGPP reduction at H4GGPP without significant conversion to H6GGPP |
-, 746511 |
| 1.3.7.11 | G91H |
site-directed mutagenesis, the mutant stops the reduction of GGPP at H2GGPP, only a very small quantity of H2GGPP is reduced further to H4GGPP or to H6GGPP |
-, 746511 |
| 1.3.7.11 | I206F |
site-directed mutagenesis, the mutant does not accumulate appreciable levels of H2GGPP at any point during the reaction, the mutant enzyme shows increased H6GGPP production compared to the wild-type enzyme |
-, 746511 |
| 1.3.7.11 | I206F/L377H |
site-directed mutagenesis, the mutant does not accumulate appreciable levels of H2GGPP at any point during the reaction, the mutant enzyme shows increased H6GGPP production compared to the wild-type enzyme |
746511 |
| 1.3.7.11 | L377H |
site-directed mutagenesis, the mutant does not accumulate appreciable levels of H2GGPP at any point during the reaction, the mutant enzyme shows increased H6GGPP production compared to the wild-type enzyme |
-, 746511 |
| 1.3.7.11 | more |
structure-guided design of the enzyme yields SaGGR variants that enhance the rate of H6GGPP product formation. Additional mutants are observed to arrest the degree of GGPP reduction at H2GGPP and H4GGPP. Crystal structures of these variants reveal the structural bases for their altered activities, in addition to providing insight into the SaGGR mechanism. Three mutants (I206F, L377H, and I206F/L377H) exhibit faster production of H6GGPP than the wild-type, increasing the overall rate of product formation by up to 2.4fold |
-, 746511 |
| 1.3.7.11 | more |
successful production of an intact archaeal membrane lipid, which has fully saturated isoprenoid chains, in bacterial cells, by heterologous expression of the enzyme from Methanosarcina acetivorans, overview. Introduction of six phospholipid biosynthetic genes from a methanogenic archaeon, Methanosarcina acetivorans, in Escherichia coli enables the host bacterium to synthesize the archaeal lipid, i.e. diphytanylglyceryl phosphoglycerol, while a glycerol modification of the phosphate group that is probably catalyzed by endogenous Escherichia coli enzymes. Reduction of the isoprenoid chains occurs only when archaeal ferredoxin is expressed with geranylgeranyl reductase, suggesting the role of ferredoxin as a specific electron donor for the reductase. Geranylgeranyl reductase from the thermoacidophilic archaeon Sulfolobus acidocaldarius can, by itself, replace both its orthologue and ferredoxin from Methanosarcina acetivorans, which indicates that an endogenous redox system of Escherichia coli reduces the enzyme |
-, 745218 |
