CHEBI:73131 - 2,3-bis-O-phytanyl-sn-glycerol 1-phosphate

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ChEBI Name 2,3-bis-O-phytanyl-sn-glycerol 1-phosphate ChEBI ID CHEBI:73131 ChEBI ASCII Name 2,3-bis-O-phytanyl-sn-glycerol 1-phosphate Definition A glycerophospholipid that is sn-glycerol 1-phosphate carrying two O-phytanyl groups at positions 2 and 3. Stars This entity has been manually annotated by the ChEBI Team. Supplier Information ZINC000058638721 Download Molfile XML SDF Find compounds which contain this structure Find compounds which resemble this structure Take structure to the Advanced Search Formula C43H89O6P Net Charge 0 Average Mass 733.13690 Monoisotopic Mass 732.63968 InChI InChI=1S/C43H89O6P/c1-35(2)17-11-19-37(5)21-13-23-39(7)25-15-27-41(9)29-31-47-33-43(34-49-50(44,45)46)48-32-30-42(10)28-16-26-40(8)24-14-22-38(6)20-12-18-36(3)4/h35-43H,11-34H2,1-10H3,(H2,44,45,46)/t37-,38-,39-,40-,41-,42-,43+/m1/s1 InChIKey UKQGAMWGTOTQPC-ALOLAALWSA-N SMILES CC(C)CCC[C@@H](C)CCC[C@@H](C)CCC[C@@H](C)CCOC[C@@H](COP(O)(O)=O)OCC[C@H](C)CCC[C@H](C)CCC[C@H](C)CCCC(C)C ChEBI Ontology Outgoing 2,3-bis-O-phytanyl-sn-glycerol 1-phosphate (CHEBI:73131) has functional parent 2,3-di-O-phytanyl-sn-glycerol (CHEBI:34227) 2,3-bis-O-phytanyl-sn-glycerol 1-phosphate (CHEBI:73131) is a glycerophospholipid (CHEBI:37739) 2,3-bis-O-phytanyl-sn-glycerol 1-phosphate (CHEBI:73131) is conjugate acid of 2,3-bis-O-phytanyl-sn-glycerol 1-phosphate(2−) (CHEBI:73125) Incoming 2,3-bis-O-phytanyl-sn-glycerol 1-phosphate(2−) (CHEBI:73125) is conjugate base of 2,3-bis-O-phytanyl-sn-glycerol 1-phosphate (CHEBI:73131) IUPAC Name (2S)-2,3-bis{[(3R,7R,11R)-3,7,11,15-tetramethylhexadecyl]oxy}propyl dihydrogen phosphate Registry Number Type Source 2713872 Reaxys Registry Number Reaxys Citations Xu Q, Eguchi T, Mathews II, Rife CL, Chiu HJ, Farr CL, Feuerhelm J, Jaroszewski L, Klock HE, Knuth MW, Miller MD, Weekes D, Elsliger MA, Deacon AM, Godzik A, Lesley SA, Wilson IA (2010) Insights into substrate specificity of geranylgeranyl reductases revealed by the structure of digeranylgeranylglycerophospholipid reductase, an essential enzyme in the biosynthesis of archaeal membrane lipids. Journal of molecular biology 404, 403-417 [PubMed:20869368] [show Abstract] Archaeal membrane lipids consist of branched, saturated hydrocarbons distinct from those found in bacteria and eukaryotes. Digeranylgeranylglycerophospholipid reductase (DGGR) catalyzes the hydrogenation process that converts unsaturated 2,3-di-O-geranylgeranylglyceryl phosphate to saturated 2,3-di-O-phytanylglyceryl phosphate as a critical step in the biosynthesis of archaeal membrane lipids. The saturation of hydrocarbon chains confers the ability to resist hydrolysis and oxidation and helps archaea withstand extreme conditions. DGGR is a member of the geranylgeranyl reductase family that is also widely distributed in bacteria and plants, where the family members are involved in the biosynthesis of photosynthetic pigments. We have determined the crystal structure of DGGR from the thermophilic heterotrophic archaea Thermoplasma acidophilum at 1.6 Å resolution, in complex with flavin adenine dinucleotide (FAD) and a bacterial lipid. The DGGR structure can be assigned to the well-studied, p-hydroxybenzoate hydroxylase (PHBH) SCOP superfamily of flavoproteins that include many aromatic hydroxylases and other enzymes with diverse functions. In the DGGR complex, FAD adopts the IN conformation (closed) previously observed in other PHBH flavoproteins. DGGR contains a large substrate-binding site that extends across the entire ligand-binding domain. Electron density corresponding to a bacterial lipid was found within this cavity. The cavity consists of a large opening that tapers down to two, narrow, curved tunnels that closely mimic the shape of the preferred substrate. We identified a sequence motif, PxxYxWxFP, that defines a specificity pocket in the enzyme and precisely aligns the double bond of the geranyl group with respect to the FAD cofactor, thus providing a structural basis for the substrate specificity of geranylgeranyl reductases. DGGR is likely to share a common mechanism with other PHBH enzymes in which FAD switches between two conformations that correspond to the reductive and oxidative half cycles. The structure provides evidence that substrate binding likely involves conformational changes, which are coupled to the two conformational states of the FAD. Nishimura Y, Eguchi T (2007) Stereochemistry of reduction in digeranylgeranylglycerophospholipid reductase involved in the biosynthesis of archaeal membrane lipids from Thermoplasma acidophilum. Bioorganic chemistry 35, 276-283 [PubMed:17275067] [show Abstract] The basic core structure of archaeal membrane lipids is 2,3-di-O-phytanylglyceryl phosphate, which is formed by reduction of 2,3-di-O-geranylgeranylglyceryl phosphate. This reaction is the final committed step in the biosynthesis of archaeal membrane lipids and is catalyzed by digeranylgeranylglycerophospholipid reductase (DGGGPL reductase). The putative DGGGPL reductase gene (Ta0516m) of Thermoplasma acidophilum was cloned and expressed. The purified recombinant enzyme appeared to catalyze the formation of 2,3-di-O-phytanylglyceryl phosphate from 2,3-di-O-geranylgeranylglyceryl phosphate, which confirmed that the Ta0516m gene of T. acidophilum encodes DGGGPL reductase. The stereospecificity in reduction of 2,3-di-O-phytylglyceryl phosphate by the recombinant reductase appeared to take place through addition of hydrogen in a syn manner by analyzing the enzyme reaction product by NMR spectroscopy. Last Modified 04 September 2014