phytosterols and 3-3-dimethylallyl-pyrophosphate

phytosterols has been researched along with 3-3-dimethylallyl-pyrophosphate* in 1 studies

Other Studies

1 other study(ies) available for phytosterols and 3-3-dimethylallyl-pyrophosphate

Article	Year
Identification of a lysine residue important for the catalytic activity of yeast farnesyl diphosphate synthase. The protein journal, 2011, Volume: 30, Issue:5 The Saccharomyces cerevisiae ERG20 gene (encoding farnesyl diphosphate synthase) has been subjected to a set of mutations at the catalytic site, at position K254 to determine the in vivo impact. The mutated strains have been shown to exhibit various growth rates, sterol profiles and monoterpenol producing capacities. The results obtained suggest that K at position 254 helps to stabilize one of the three Mg(2+) forming a bridge between the enzyme and DMAPP, and demonstrate that destabilizing two of the three Mg(2+) ions, by introducing a double mutation at positions K197 and K254, results in a loss of FPPS activity and a lethal phenotype. Topics: Amino Acid Sequence; Catalytic Domain; Cell Growth Processes; Cell Survival; Enzyme Stability; Geranyltranstransferase; Green Fluorescent Proteins; Hemiterpenes; Lysine; Models, Molecular; Molecular Sequence Data; Monoterpenes; Mutagenesis, Site-Directed; Organophosphorus Compounds; Phytosterols; Recombinant Fusion Proteins; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Sequence Alignment	2011

Article

Year

Identification of a lysine residue important for the catalytic activity of yeast farnesyl diphosphate synthase.

The protein journal, 2011, Volume: 30, Issue:5

The Saccharomyces cerevisiae ERG20 gene (encoding farnesyl diphosphate synthase) has been subjected to a set of mutations at the catalytic site, at position K254 to determine the in vivo impact. The mutated strains have been shown to exhibit various growth rates, sterol profiles and monoterpenol producing capacities. The results obtained suggest that K at position 254 helps to stabilize one of the three Mg(2+) forming a bridge between the enzyme and DMAPP, and demonstrate that destabilizing two of the three Mg(2+) ions, by introducing a double mutation at positions K197 and K254, results in a loss of FPPS activity and a lethal phenotype.

Topics: Amino Acid Sequence; Catalytic Domain; Cell Growth Processes; Cell Survival; Enzyme Stability; Geranyltranstransferase; Green Fluorescent Proteins; Hemiterpenes; Lysine; Models, Molecular; Molecular Sequence Data; Monoterpenes; Mutagenesis, Site-Directed; Organophosphorus Compounds; Phytosterols; Recombinant Fusion Proteins; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Sequence Alignment

2011