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Thermostable farnesyl diphosphate synthase of Bacillus stearothermophilus: molecular cloning, sequence determination, overproduction, and purification.
TLDR
The structural gene for thermostable farnesyl diphosphate synthase from Bacillus stearothermophilus was cloned, sequenced, and overexpressed in Escherichia coli cells and the deduced amino acid sequence shows a 42% similarity with that of E. coli FPP synthase.
Conversion from Farnesyl Diphosphate Synthase to Geranylgeranyl Diphosphate Synthase by Random Chemical Mutagenesis (*)
TLDR
Comparisons of kinetic parameters of the mutated and wild type enzymes revealed several phenomena that may relate with the change of the ultimate chain length, which might suggest that the aromatic ring of tyrosine 81 blocks the chain elongation longer than FPP.
Polyprenyl diphosphate synthases.
It is noteworthy that in spite of the similarity of the reactions catalyzed by these prenyltransferases, the modes of expression of catalytic function are surprisingly different, varying according to
Purification and properties of geranylgeranyl-diphosphate synthase from bovine brain.
TLDR
Results indicate that geranylgeranyl dphosphate, a lipid precursor for the biosynthesis of a majority of prenylated proteins, is synthesized from dimethylallyl diphosphate and isopentenyl diph phosphate by the action of farnesyl-diphosphates synthase.
Evidence for Covalent Attachment of Diphytanylglyceryl Phosphate to the Cell-surface Glycoprotein of Halobacterium halobium *
TLDR
Results indicate that the cell-surface glycoprotein of this halobacterium is modified with diphytanylglyceryl phosphate.
Thermostable farnesyl diphosphate synthase of Bacillus stearothermophilus: crystallization and site-directed mutagenesis.
TLDR
The gene for thermostable farnesyl diphosphate synthase from Bacillus stearothermophilus was cloned, sequenced, and overexpressed in Escherichia coli and crystallized, finding the enzyme carried only two cysteine residues in contrast to its counterparts from other sources.
Molecular Cloning, Expression, and Purification of Undecaprenyl Diphosphate Synthase
TLDR
Cloning of the gene for undecaprenyl diphosphate synthase was successful, providing the first primary structure for any prenyltransferase that catalyzes Z-prenyl chain elongation, which has characteristic conserved regions, including aspartate-rich motifs.
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