Enzymes
UniProtKB help_outline | 12 proteins |
Reaction participants Show >> << Hide
- Name help_outline a 2,3-bis-O-phytanyl-sn-glycerol 1-phospholipid Identifier CHEBI:138139 Charge -1 Formula C43H87O6PR SMILEShelp_outline P(=O)(O*)(OC[C@@H](OCC[C@@H](CCC[C@@H](CCC[C@@H](CCCC(C)C)C)C)C)COCC[C@@H](CCC[C@@H](CCC[C@@H](CCCC(C)C)C)C)C)[O-] 2D coordinates Mol file for the small molecule Search links Involved in 7 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
oxidized 2[4Fe-4S]-[ferredoxin]
Identifier
RHEA-COMP:10004
Reactive part
help_outline
- Name help_outline [4Fe-4S]2+ cluster Identifier CHEBI:33722 Charge 2 Formula Fe4S4 InChIKeyhelp_outline YEAYMLBNRJYVPB-UHFFFAOYSA-N Positionhelp_outline 1 SMILEShelp_outline [S]12[Fe]3[S]4[Fe]1[S]1[Fe+]2[S]3[Fe+]41 2D coordinates Mol file for the small molecule Search links Involved in 25 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline [4Fe-4S]2+ cluster Identifier CHEBI:33722 Charge 2 Formula Fe4S4 InChIKeyhelp_outline YEAYMLBNRJYVPB-UHFFFAOYSA-N Positionhelp_outline 2 SMILEShelp_outline [S]12[Fe]3[S]4[Fe]1[S]1[Fe+]2[S]3[Fe+]41 2D coordinates Mol file for the small molecule Search links Involved in 25 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phospholipid Identifier CHEBI:138140 Charge -1 Formula C43H71O6PR SMILEShelp_outline P(OC[C@@H](OC\C=C(\CC/C=C(\C)/CC\C=C(\CCC=C(C)C)/C)/C)COC\C=C(\CC/C=C(\C)/CC\C=C(\CCC=C(C)C)/C)/C)(=O)(O*)[O-] 2D coordinates Mol file for the small molecule Search links Involved in 10 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
reduced 2[4Fe-4S]-[ferredoxin]
Identifier
RHEA-COMP:10002
Reactive part
help_outline
- Name help_outline [4Fe-4S]1+ cluster Identifier CHEBI:33723 Charge 1 Formula Fe4S4 InChIKeyhelp_outline ISVAEKDKOPJTJN-UHFFFAOYSA-N Positionhelp_outline 1 SMILEShelp_outline [S]12[Fe]3[S]4[Fe]1[S]1[Fe]2[S]3[Fe+]41 2D coordinates Mol file for the small molecule Search links Involved in 25 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline [4Fe-4S]1+ cluster Identifier CHEBI:33723 Charge 1 Formula Fe4S4 InChIKeyhelp_outline ISVAEKDKOPJTJN-UHFFFAOYSA-N Positionhelp_outline 2 SMILEShelp_outline [S]12[Fe]3[S]4[Fe]1[S]1[Fe]2[S]3[Fe+]41 2D coordinates Mol file for the small molecule Search links Involved in 25 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:54324 | RHEA:54325 | RHEA:54326 | RHEA:54327 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
UniProtKB help_outline |
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EC numbers help_outline | ||||
MetaCyc help_outline |
Related reactions help_outline
Specific form(s) of this reaction
More general form(s) of this reaction
Publications
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Geranylgeranyl reductase involved in the biosynthesis of archaeal membrane lipids in the hyperthermophilic archaeon Archaeoglobus fulgidus.
Murakami M., Shibuya K., Nakayama T., Nishino T., Yoshimura T., Hemmi H.
Complete saturation of the geranylgeranyl groups of biosynthetic intermediates of archaeal membrane lipids is an important reaction that confers chemical stability on the lipids of archaea, which generally inhabit extreme conditions. An enzyme encoded by the AF0464 gene of a hyperthermophilic arch ... >> More
Complete saturation of the geranylgeranyl groups of biosynthetic intermediates of archaeal membrane lipids is an important reaction that confers chemical stability on the lipids of archaea, which generally inhabit extreme conditions. An enzyme encoded by the AF0464 gene of a hyperthermophilic archaeon, Archaeoglobus fulgidus, which is a distant homologue of plant geranylgeranyl reductases and an A. fulgidus menaquinone-specific prenyl reductase [Hemmi H, Yoshihiro T, Shibuya K, Nakayama T, & Nishino T (2005) J Bacteriol187, 1937-1944], was recombinantly expressed and purified, and its geranylgeranyl reductase activity was examined. The radio HPLC analysis indicated that the flavoenzyme, which binds FAD noncovalently, showed activity towards lipid-biosynthetic intermediates containing one or two geranylgeranyl groups under anaerobic conditions. It showed a preference for 2,3-di-O-geranylgeranylglyceryl phosphate over 3-O-geranylgeranylglyceryl phosphate and geranylgeranyl diphosphate in vitro, and did not reduce the prenyl group of respiratory quinones in Escherichia coli cells. The substrate specificity strongly suggests that the enzyme is involved in the biosynthesis of archaeal membrane lipids. GC-MS analysis of the reaction product from 2,3-di-O-geranylgeranylglyceryl phosphate proved that the substrate was converted to archaetidic acid (2,3-di-O-phytanylglyceryl phosphate). The archaeal enzyme required sodium dithionite as the electron donor for activity in vitro, similarly to the menaquinone-specific prenyl reductase from the same anaerobic archaeon. On the other hand, in the presence of NADPH (the preferred electron donor for plant homologues), the enzyme reaction did not proceed. << Less
FEBS J. 274:805-814(2007) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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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.
Sato S., Murakami M., Yoshimura T., Hemmi H.
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 ... >> More
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. << Less
J. Bacteriol. 190:3923-3929(2008) [PubMed] [EuropePMC]
This publication is cited by 4 other entries.
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Geranylgeranyl reductase and ferredoxin from Methanosarcina acetivorans are required for the synthesis of fully reduced archaeal membrane lipid in Escherichia coli cells.
Isobe K., Ogawa T., Hirose K., Yokoi T., Yoshimura T., Hemmi H.
Archaea produce membrane lipids that typically possess fully saturated isoprenoid hydrocarbon chains attached to the glycerol moiety via ether bonds. They are functionally similar to, but structurally and biosynthetically distinct from, the fatty acid-based membrane lipids of bacteria and eukaryot ... >> More
Archaea produce membrane lipids that typically possess fully saturated isoprenoid hydrocarbon chains attached to the glycerol moiety via ether bonds. They are functionally similar to, but structurally and biosynthetically distinct from, the fatty acid-based membrane lipids of bacteria and eukaryotes. It is believed that the characteristic lipid structure helps archaea survive under severe conditions such as extremely low or high pH, high salt concentrations, and/or high temperatures. We detail here the first successful production of an intact archaeal membrane lipid, which has fully saturated isoprenoid chains, in bacterial cells. The introduction of six phospholipid biosynthetic genes from a methanogenic archaeon, Methanosarcina acetivorans, in Escherichia coli enabled the host bacterium to synthesize the archaeal lipid, i.e., diphytanylglyceryl phosphoglycerol, while a glycerol modification of the phosphate group was probably catalyzed by endogenous E. coli enzymes. Reduction of the isoprenoid chains occurred only when archaeal ferredoxin was expressed with geranylgeranyl reductase, suggesting the role of ferredoxin as a specific electron donor for the reductase. This report is the first identification of a physiological reducer for archaeal geranylgeranyl reductase. On the other hand, geranylgeranyl reductase from the thermoacidophilic archaeon Sulfolobus acidocaldarius could, by itself, replace both its orthologue and ferredoxin from M. acetivorans, which indicated that an endogenous redox system of E. coli reduced the enzyme. << Less
J. Bacteriol. 196:417-423(2014) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.