Information on EC 1.3.7.11 - 2,3-bis-O-geranylgeranyl-sn-glycero-phospholipid reductase

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The expected taxonomic range for this enzyme is: Archaea, Eukaryota

EC NUMBER
COMMENTARY hide
1.3.7.11
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RECOMMENDED NAME
GeneOntology No.
2,3-bis-O-geranylgeranyl-sn-glycero-phospholipid reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a 2,3-bis-(O-phytanyl)-sn-glycero-phospholipid + 16 oxidized ferredoxin [iron-sulfur] cluster = a 2,3-bis-(O-geranylgeranyl)-sn-glycero-phospholipid + 16 reduced ferredoxin [iron-sulfur] cluster + 16 H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
CDP-archaeol biosynthesis
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lipid metabolism
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Glycerophospholipid metabolism
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SYSTEMATIC NAME
IUBMB Comments
2,3-bis-(O-phytanyl)-sn-glycero-phospholipid:ferredoxin oxidoreductase
A flavoprotein (FAD). The enzyme is involved in the biosynthesis of archaeal membrane lipids. It catalyses the reduction of all 8 double bonds in 2,3-bis-O-geranylgeranyl-sn-glycero-phospholipids and all 4 double bonds in 3-O-geranylgeranyl-sn-glycerol phospholipids with comparable activity. Unlike EC 1.3.1.101, 2,3-bis-O-geranylgeranyl-sn-glycerol 1-phosphate reductase [NAD(P)H], this enzyme shows no activity with NADPH, and requires a dedicated ferredoxin [4].
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,3-bis-O-geranylgeranyl-sn-glycerol 1-phosphate + reduced acceptor
2,3-bis-O-phytanyl-sn-glycerol 1-phosphate + acceptor
show the reaction diagram
2,3-di-O-geranylgeranylglyceryl phosphate + 16 reduced ferredoxin [iron-sulfur] cluster + 16 H+
2,3-di-O-phytanylglyceryl phosphate + 16 oxidized ferredoxin [iron-sulfur] cluster
show the reaction diagram
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?
3-O-geranylgeranyl-sn-glycerol 1-phosphate + reduced acceptor
3-O-phytyl-sn-glycerol 1-phosphate + acceptor
show the reaction diagram
activity is comparable to the activity with 2,3-di-O-geranylgeranyl-sn-glycerol 1-phosphate as substrate
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?
3-O-geranylgeranyl-sn-glycerol 1-phosphate + reduced acceptor
?
show the reaction diagram
the enzyme shows a preference for 2,3-di-O-geranylgeranylglyceryl phosphate over 3-O-geranylgeranylglyceryl phosphate and geranylgeranyl diphosphate in vitro
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?
a 2,3-bis-(O-geranylgeranyl)-sn-glycero-phospholipid + 16 dithionite + 16 H+
a 2,3-bis-(O-phytanyl)-sn-glycero-phospholipid + 16 oxidized dithionite
show the reaction diagram
a 2,3-bis-(O-geranylgeranyl)-sn-glycero-phospholipid + 16 reduced ferredoxin [iron-sulfur] cluster + 16 H+
a 2,3-bis-(O-phytanyl)-sn-glycero-phospholipid + 16 oxidized ferredoxin [iron-sulfur] cluster
show the reaction diagram
a 2,3-bis-(O-phytanyl)-sn-glycero-phospholipid + 16 oxidized ferredoxin [iron-sulfur] cluster
a 2,3-bis-(O-geranylgeranyl)-sn-glycero-phospholipid + 16 reduced ferredoxin [iron-sulfur] cluster + 16 H+
show the reaction diagram
geranylgeraniol + reduced ferredoxin
14,15-dihydrogeranylgeraniol + oxidized ferredoxin
show the reaction diagram
MA1492 selectively reduces the x-double bond of a geranylgeranyl group
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geranylgeranyl diphosphate + reduced acceptor
?
show the reaction diagram
the enzyme shows a preference for 2,3-di-O-geranylgeranylglyceryl phosphate over 3-O-geranylgeranylglyceryl phosphate and geranylgeranyl diphosphate in vitro
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?
geranylgeranyl diphosphate + reduced acceptor
phytyl diphosphate + acceptor
show the reaction diagram
the enzyme does not accept NADPH. Since the physiological reducing agents for the enzyme remains unknown, sodium dithionite is used as acceptor. Geranylgeranyl diphosphate is partially reduced to phytyl diphosphate with 10% of the activity compared to the complete reduction of 2,3-di-O-phytanyl-sn-glycerol 1-phosphate
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?
geranylgeranyl diphosphate + reduced dithionite
hexahydro-geranylgeranyl diphoshate + oxidized dithionite
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2,3-bis-O-geranylgeranyl-sn-glycerol 1-phosphate + reduced acceptor
2,3-bis-O-phytanyl-sn-glycerol 1-phosphate + acceptor
show the reaction diagram
a 2,3-bis-(O-phytanyl)-sn-glycero-phospholipid + 16 oxidized ferredoxin [iron-sulfur] cluster
a 2,3-bis-(O-geranylgeranyl)-sn-glycero-phospholipid + 16 reduced ferredoxin [iron-sulfur] cluster + 16 H+
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ferredoxin
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flavin
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the enzyme contains a flavin coenzyme
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0067 - 0.0158
geranylgeranyl diphosphate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43400
x * 43400, calculated
46000
x * 46000, SDS-PAGE
46978
x * 46978, calculated from sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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divided into the FADbinding, catalytic and C-terminal domains
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystals are obtained using 3.5-4.5 M sodium formate with 0.1 M sodium acetate buffer, pH 4.6, as the precipitant solution and 1.0 mM geranylgeranyl diphosphate is added for co-crystallization, 1.8 A resolution
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wild-type and mutant enzymes, in apoform or complexed with geranygeranyl diphosphate, sitting drop vapor diffusion, mixing of 10 mg/ml protein in 25 mM HEPES, pH 7.4, with well solution containing 0.1M Tris, pH 7.5, 10% PEG 3350, and 0.2 M L-proline, in a 1:1 ratio, sparse matrix-screening crystallization method for method screening, addition of 5 mM GGPP for ligand-bound crystals, 2 days, X-ray diffractin structure determination and analysis, modeling
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in complex with flavin adenine dinucleotide, to 1.6 A resolution. Substrate binding likely involves conformational changes, which are coupled to the two conformational states of the FAD cofactor
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strains BLR(DE3) or Rosetta2(DE3) by nickel affinity chromatography, cleavage of the His-tag by TEV protease, followed by another step of nickel affinity chromatography to remove the tag, followed by desalting gel filtration
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recombinant N-terminally poly-His-tagged enzyme MA1492 from Escherichia coli strain KRX by cobalt affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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expression in Escherichia coli with a polyhistidine-tag at its N-terminus
gene MA_1484, cloned as MA1485-MA1484 tandem genes encoding a ferredoxin-like protein and a GGR homologue, respectively, MA1485 just upstream from MA1484. Recombinant expression in Escherichia coli strain TOP10 in inclusion bodies, co-expression with ferredoin is required for activity, or coexpression with geranylgeranyl reductase from the thermoacidophilic archaeon Sulfolobus acidocaldarius, which can, by itself, replace both its orthologue and ferredoxin from Methanosarcina acetivorans for phospholipid biosynthetic activity in Escherichia coli. Phentyype of transgenic Escherichia coli cells
gene MA_1492, sequence comparisons, recombinant expression of N-terminally poly-His-tagged enzyme MA1492 in Escherichia coli KRX cells, which are genetically modified to produce unsaturated archaeal-type lipids, leads to production of partially saturated lipid derivatives
recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strains BLR(DE3) or Rosetta2(DE3)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F219L
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site-directed mutagenesis, the mutant enzymes ceases GGPP reduction at H4GGPP without significant conversion to H6GGPP
G91H
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site-directed mutagenesis, the mutant stops the reduction of GGPP at H2GGPP, only a very small quantity of H2GGPP is reduced further to H4GGPP or to H6GGPP
I206F
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site-directed mutagenesis, the mutant does not accumulate appreciable levels of H2GGPP at any point during the reaction, the mutant enzyme shows increased H6GGPP prduction compared to the wild-type enzyme
I206F/L377H
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site-directed mutagenesis, the mutant does not accumulate appreciable levels of H2GGPP at any point during the reaction, the mutant enzyme shows increased H6GGPP prduction compared to the wild-type enzyme
L377H
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site-directed mutagenesis, the mutant does not accumulate appreciable levels of H2GGPP at any point during the reaction, the mutant enzyme shows increased H6GGPP prduction compared to the wild-type enzyme
F219L
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site-directed mutagenesis, the mutant enzymes ceases GGPP reduction at H4GGPP without significant conversion to H6GGPP
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G91H
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site-directed mutagenesis, the mutant stops the reduction of GGPP at H2GGPP, only a very small quantity of H2GGPP is reduced further to H4GGPP or to H6GGPP
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I206F
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site-directed mutagenesis, the mutant does not accumulate appreciable levels of H2GGPP at any point during the reaction, the mutant enzyme shows increased H6GGPP prduction compared to the wild-type enzyme
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L377H
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site-directed mutagenesis, the mutant does not accumulate appreciable levels of H2GGPP at any point during the reaction, the mutant enzyme shows increased H6GGPP prduction compared to the wild-type enzyme
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additional information
Show AA Sequence (438 entries)
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