geranylgeranyl-pyrophosphate has been researched along with phytyl-diphosphate* in 2 studies
2 other study(ies) available for geranylgeranyl-pyrophosphate and phytyl-diphosphate
| Article | Year |
|---|---|
An uncultivated crenarchaeota contains functional bacteriochlorophyll a synthase.
A fosmid clone 37F10 containing an archaeal 16S rRNA gene was screened out from a metagenomic library of Pearl River sediment, southern China. Sequence analysis of the 35 kb inserted fragment of 37F10 found that it contains a single 16S rRNA gene belonging to Miscellaneous Crenarchaeotal Group (MCG) and 36 open reading frames (ORFs). One ORF (orf11) encodes putative bacteriochlorophyll a synthase (bchG) gene. Bacteriochlorophyll a synthase gene has never been reported in a member of the domain Archaea, in accordance with the fact that no (bacterio)-chlorophyll has ever been detected in any cultivated archaea. The putative archaeal bchG (named as ar-bchG) was cloned and heterologously expressed in Escherichia coli. The protein was found to be capable of synthesizing bacteriochlorophyll a by esterification of bacteriochlorophyllide a with phytyl diphosphate or geranylgeranyl diphosphate. Furthermore, phylogenetic analysis clearly indicates that the ar-bchG diverges before the bacterial bchGs. Our results for the first time demonstrate that a key and functional enzyme for bacteriochlorophyll a biosynthesis does exist in Archaea. Topics: Carbon-Oxygen Ligases; China; Chlorophyllides; Cloning, Molecular; Cluster Analysis; Crenarchaeota; Diphosphates; DNA, Archaeal; Escherichia coli; Gene Expression; Molecular Sequence Data; Open Reading Frames; Phylogeny; Polyisoprenyl Phosphates; Rivers; Sequence Analysis, DNA; Sequence Homology | 2009 |
Specific partial reduction of geranylgeranyl diphosphate by an enzyme from the thermoacidophilic archaeon Sulfolobus acidocaldarius yields a reactive prenyl donor, not a dead-end product.
Geranylgeranyl reductase from Sulfolobus acidocaldarius was shown to catalyze the reduction of geranylgeranyl groups in the precursors of archaeal membrane lipids, generally reducing all four double bonds. However, when geranylgeranyl diphosphate was subjected to the reductase reaction, only three of the four double bonds were reduced. Mass spectrometry and acid hydrolysis indicated that the allylic double bond was preserved in the partially reduced product derived from geranylgeranyl diphosphate. Thus, the reaction product was shown to be phytyl diphosphate, which is a substrate for archaeal prenyltransferases, unlike the completely reduced compound phytanyl diphosphate. Topics: Diphosphates; Diterpenes; Neoprene; Oxidoreductases; Polyisoprenyl Phosphates; Substrate Specificity; Sulfolobus acidocaldarius | 2008 |