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

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The enzyme appears in viruses and cellular organisms

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].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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the enzyme is involved in the biosynthesis of archaeal membrane lipids
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
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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
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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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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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
flavin
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the enzyme contains a flavin coenzyme
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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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
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli with a polyhistidine-tag at its N-terminus
Show AA Sequence (228 entries)
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