This cytosolic enzyme catalyses the first pathway-specific step in the biosynthesis of the core membrane diether lipids in archaebacteria . Requires Mg2+ for maximal activity . It catalyses the alkylation of the primary hydroxy group in sn-glycerol 1-phosphate by geranylgeranyl diphosphate (GGPP) in a prenyltransfer reaction where a hydroxy group is the nucleophile in the acceptor substrate . The other enzymes involved in the biosynthesis of polar lipids in Archaea are EC 1.1.1.261 (sn-glycerol-1-phosphate dehydrogenase), EC 2.5.1.42 (geranylgeranylglycerol-phosphate geranylgeranyltransferase) and EC 2.7.7.67 (CDP-archaeol synthase), which lead to the formation of CDP-unsaturated archaeol. The final step in the pathway involves the addition of L-serine, with concomitant removal of CMP, leading to the production of unsaturated archaetidylserine .
This cytosolic enzyme catalyses the first pathway-specific step in the biosynthesis of the core membrane diether lipids in archaebacteria [2]. Requires Mg2+ for maximal activity [2]. It catalyses the alkylation of the primary hydroxy group in sn-glycerol 1-phosphate by geranylgeranyl diphosphate (GGPP) in a prenyltransfer reaction where a hydroxy group is the nucleophile in the acceptor substrate [2]. The other enzymes involved in the biosynthesis of polar lipids in Archaea are EC 1.1.1.261 (sn-glycerol-1-phosphate dehydrogenase), EC 2.5.1.42 (geranylgeranylglycerol-phosphate geranylgeranyltransferase) and EC 2.7.7.67 (CDP-archaeol synthase), which lead to the formation of CDP-unsaturated archaeol. The final step in the pathway involves the addition of L-serine, with concomitant removal of CMP, leading to the production of unsaturated archaetidylserine [5].
first committed step in the biosynthetic pathway of glycerol dibiphytanyl glycerol tetraethers, the membrane lipids of the thermophilic and acidophilic euryarchaeota
first committed step in the biosynthetic pathway of glycerol dibiphytanyl glycerol tetraethers, the membrane lipids of the thermophilic and acidophilic euryarchaeota
first committed step in the biosynthetic pathway of glycerol dibiphytanyl glycerol tetraethers, the membrane lipids of the thermophilic and acidophilic euryarchaeota
first committed step in the biosynthetic pathway of glycerol dibiphytanyl glycerol tetraethers, the membrane lipids of the thermophilic and acidophilic euryarchaeota
diversity of thaumarchaeotal GGGP synthases in the marine water column, phylogenetic analysis and tree and correlation to the classification of shallow and deep water clusters, overview. Differences in isoprenoid glycerol dialkyl glycerol tetraethers distributions from subsurface to deep waters that may be explained by differences in the GGGP synthase, suggesting a genetic control on isoprenoid glycerol dialkyl glycerol tetraethers distribution. Diversity of archaeal GGGP synthases, overview
the key enzyme catalyses the formation of an ether bond between isoprenyl diphosphate and glycerol-1-phosphate to form 3-(O-geranylgeranyl)-sn-glycerol 1-phosphate, and is the first committed step towards ether membrane lipid synthesis
first committed step in the biosynthetic pathway of glycerol dibiphytanyl glycerol tetraethers, the membrane lipids of the thermophilic and acidophilic euryarchaeota
first committed step in the biosynthetic pathway of glycerol dibiphytanyl glycerol tetraethers, the membrane lipids of the thermophilic and acidophilic euryarchaeota
the oligomerization interfaces are studied by introducing disturbing mutations and subsequently the stability and activity of generated dimeric and monomeric variants are compared with the wild-type enzyme. Oligomerization might positively affect the thermostability-flexibility trade-off in the enzyme by allowing a higher intrinsic flexibility of the individual protomers
the oligomerization interfaces are studied by introducing disturbing mutations and subsequently the stability and activity of generated dimeric and monomeric variants are compared with the wild-type enzyme. Oligomerization might positively affect the thermostability-flexibility trade-off in the enzyme by allowing a higher intrinsic flexibility of the individual protomers
sitting-drop vapor-diffusion method at 20°C, crystal structure of the enzyme in complex with substrate sn-glycerol-1-phosphate is determined at 2.35 A resolution
diversity of thaumarchaeotal GGGP synthases in the marine water column, phylogenetic analysis and tree and correlation to the classification of shallow and deep water clusters, overview
(S)-geranylgeranylglyceryl phosphate synthase. Purification and characterization of the first pathway-specific enzyme in archaebacterial membrane lipid biosynthesis
Nemoto, N.; Miyazono, K.I.; Tanokura, M.; Yamagishi, A.
Crystal structure of (S)-3-O-geranylgeranylglyceryl phosphate synthase from Thermoplasma acidophilum in complex with the substrate sn-glycerol 1-phosphate