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Information on EC 1.3.7.11 - 2,3-bis-O-geranylgeranyl-sn-glycero-phospholipid reductase
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1.3.7.11 2,3-bis-O-geranylgeranyl-sn-glycero-phospholipid reductaseIUBMB Comments
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 .
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The expected taxonomic range for this enzyme is: Archaea, Bacteria
Reaction Schemes
+
16
=
+
16
+
16
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
Synonyms
ma1492, saggr, af0464, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CrtI homologue
digeranylgeranylglycerophospholipid reductase
EC 1.3.99.34
-
-
formerly
-
geranylgeranyl reductase
GGR
MA1484
MA1492
MA_1484
MA_1492
phytoene dehydrogenase family protein
SaGGR
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REACTION
REACTION DIAGRAM
COMMENTARY
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+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
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
-
-
-
?
3-O-geranylgeranyl-sn-glycerol 1-phosphate + reduced acceptor
3-O-phytyl-sn-glycerol 1-phosphate + acceptor
activity is comparable to the activity with 2,3-di-O-geranylgeranyl-sn-glycerol 1-phosphate as substrate
-
-
?
3-O-geranylgeranyl-sn-glycerol 1-phosphate + reduced acceptor
?
the enzyme shows a preference for 2,3-di-O-geranylgeranylglyceryl phosphate over 3-O-geranylgeranylglyceryl phosphate and geranylgeranyl diphosphate in vitro
-
-
?
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
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
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+
geranylgeraniol + reduced ferredoxin
14,15-dihydrogeranylgeraniol + oxidized ferredoxin
MA1492 selectively reduces the x-double bond of a geranylgeranyl group
-
-
?
geranylgeranyl diphosphate + reduced acceptor
?
the enzyme shows a preference for 2,3-di-O-geranylgeranylglyceryl phosphate over 3-O-geranylgeranylglyceryl phosphate and geranylgeranyl diphosphate in vitro
-
-
?
geranylgeranyl diphosphate + reduced acceptor
phytyl diphosphate + acceptor
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
-
-
?
geranylgeranyl diphosphate + reduced dithionite
hexahydro-geranylgeranyl diphoshate + oxidized dithionite
2,3-bis-O-geranylgeranyl-sn-glycerol 1-phosphate + reduced acceptor
2,3-bis-O-phytanyl-sn-glycerol 1-phosphate + acceptor
the enzyme is involved in the biosynthesis of archaeal membrane lipids
-
-
?
2,3-bis-O-geranylgeranyl-sn-glycerol 1-phosphate + reduced acceptor
2,3-bis-O-phytanyl-sn-glycerol 1-phosphate + acceptor
the enzyme shows a preference for 2,3-di-O-geranylgeranylglyceryl phosphate over 3-O-geranylgeranylglyceryl phosphate and geranylgeranyl diphosphate in vitro
-
-
?
2,3-bis-O-geranylgeranyl-sn-glycerol 1-phosphate + reduced acceptor
2,3-bis-O-phytanyl-sn-glycerol 1-phosphate + acceptor
the enzyme is involved in the biosynthesis of archaeal membrane lipids
-
-
?
2,3-bis-O-geranylgeranyl-sn-glycerol 1-phosphate + reduced acceptor
2,3-bis-O-phytanyl-sn-glycerol 1-phosphate + acceptor
most preferred substrate. Since the physiological reducing agents for the enzyme remains unknown, sodium dithionite is used as acceptor
-
-
?
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
i.e. DGGGP-glycerol
-
-
?
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
i.e. DGGGP-glycerol
-
-
?
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
-
-
-
?
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
Methanobrevibacter ruminantium DSM 1039
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
i.e. DGGGP-glycerol
-
-
?
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
i.e. DGGGP-glycerol
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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+
-
-
-
?
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+
-
-
-
?
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+
-
-
-
?
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+
-
-
-
?
geranylgeranyl diphosphate + reduced dithionite
hexahydro-geranylgeranyl diphoshate + oxidized dithionite
non-native substrate
-
-
?
geranylgeranyl diphosphate + reduced dithionite
hexahydro-geranylgeranyl diphoshate + oxidized dithionite
non-native substrate
-
-
?
additional information
?
-
enzyme MA1492 reacts with membrane lipid biosynthetic intermediates, i.e. geranylgeranyl diphosphate (GGPP) and geranylgeranylglyceryl phosphate (GGGP), suggesting that the enzyme also reduces the intermediates
-
-
?
additional information
?
-
-
enzyme MA1492 reacts with membrane lipid biosynthetic intermediates, i.e. geranylgeranyl diphosphate (GGPP) and geranylgeranylglyceryl phosphate (GGGP), suggesting that the enzyme also reduces the intermediates
-
-
?
additional information
?
-
substrate specificity and regiospecificity of recombinant MA1492, overview. The enzyme is definitely specific to compounds containing C20 geranylgeranyl groups and reduces only one of four double bonds in a geranylgeranyl chain. GC-MS analysis of the product from geranylgeraniol confirms that the reduction selectively occurs on the omega-terminal double bond
-
-
?
additional information
?
-
-
substrate specificity and regiospecificity of recombinant MA1492, overview. The enzyme is definitely specific to compounds containing C20 geranylgeranyl groups and reduces only one of four double bonds in a geranylgeranyl chain. GC-MS analysis of the product from geranylgeraniol confirms that the reduction selectively occurs on the omega-terminal double bond
-
-
?
additional information
?
-
enzyme MA1492 reacts with membrane lipid biosynthetic intermediates, i.e. geranylgeranyl diphosphate (GGPP) and geranylgeranylglyceryl phosphate (GGGP), suggesting that the enzyme also reduces the intermediates
-
-
?
additional information
?
-
substrate specificity and regiospecificity of recombinant MA1492, overview. The enzyme is definitely specific to compounds containing C20 geranylgeranyl groups and reduces only one of four double bonds in a geranylgeranyl chain. GC-MS analysis of the product from geranylgeraniol confirms that the reduction selectively occurs on the omega-terminal double bond
-
-
?
additional information
?
-
the wild-type enzyme reduces the non-native substrate geranylgeranyl diphoshate with reductant sodium dithionite and produces H6GGPP. Geranylgeranyl diphosphate is bound by three binding sites for GGPP, mechansim of the enzyme orientating double bonds to be reduced by the bound FAD cofactor, overview. Catalytic reaction mechansim and substrate binding structure, overview
-
-
?
additional information
?
-
the wild-type enzyme reduces the non-native substrate geranylgeranyl diphoshate with reductant sodium dithionite and produces H6GGPP. Geranylgeranyl diphosphate is bound by three binding sites for GGPP, mechansim of the enzyme orientating double bonds to be reduced by the bound FAD cofactor, overview. Catalytic reaction mechansim and substrate binding structure, overview
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
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
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+
2,3-bis-O-geranylgeranyl-sn-glycerol 1-phosphate + reduced acceptor
2,3-bis-O-phytanyl-sn-glycerol 1-phosphate + acceptor
the enzyme is involved in the biosynthesis of archaeal membrane lipids
-
-
?
2,3-bis-O-geranylgeranyl-sn-glycerol 1-phosphate + reduced acceptor
2,3-bis-O-phytanyl-sn-glycerol 1-phosphate + acceptor
the enzyme is involved in the biosynthesis of archaeal membrane lipids
-
-
?
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
-
-
-
?
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
Methanobrevibacter ruminantium DSM 1039
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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+
-
-
-
?
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+
-
-
-
?
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+
-
-
-
?
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+
-
-
-
?
additional information
?
-
enzyme MA1492 reacts with membrane lipid biosynthetic intermediates, i.e. geranylgeranyl diphosphate (GGPP) and geranylgeranylglyceryl phosphate (GGGP), suggesting that the enzyme also reduces the intermediates
-
-
?
additional information
?
-
-
enzyme MA1492 reacts with membrane lipid biosynthetic intermediates, i.e. geranylgeranyl diphosphate (GGPP) and geranylgeranylglyceryl phosphate (GGGP), suggesting that the enzyme also reduces the intermediates
-
-
?
additional information
?
-
enzyme MA1492 reacts with membrane lipid biosynthetic intermediates, i.e. geranylgeranyl diphosphate (GGPP) and geranylgeranylglyceryl phosphate (GGGP), suggesting that the enzyme also reduces the intermediates
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
flavoprotein, the catalytic domain has a large cavity surrounded by a characteristic YxWxFPx7-8GxG motif and by the isoalloxazine ring of an FAD molecule
FAD
the GGPP DELTA14 double bond is directly adjacent to the N5 position of the FAD cofactor, binding structure, overview
Ferredoxin
dependent on, encoded by gene MA_1485, role of ferredoxin as a specific electron donor for the reductase
-
additional information
the enzyme requires sodium dithionite as the electron donor for activity in vitro. In the presence of NADPH (the preferred electron donor for plant homologues), the enzyme reaction does not proceed
-
additional information
-
the enzyme requires sodium dithionite as the electron donor for activity in vitro. In the presence of NADPH (the preferred electron donor for plant homologues), the enzyme reaction does not proceed
-
additional information
no activity with NAD(P)H, the bound flavin is reduced with dithionite but not with NAD(P)H
-
additional information
-
no activity with NAD(P)H, the bound flavin is reduced with dithionite but not with NAD(P)H
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0067
geranylgeranyl diphosphate
wild-type enzyme, pH 5.5, 50°C
0.0088
geranylgeranyl diphosphate
mutant I206F, pH 5.5, 50°C
0.0156
geranylgeranyl diphosphate
mutant L377H, pH 5.5, 50°C
0.0158
geranylgeranyl diphosphate
mutant I206F/L377H, pH 5.5, 50°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
evolution
MA1492 is a distinct type of archaeal geranylgeranyl reductase that is not homologous to known geranylgeranyl reductases, but is homologous to phytoene desaturase CrtI, which is the carotenogenic enzyme that catalyzes oxidation/isomerization of phytoene to lycopene, CrtI, EC 1.3.5.6
evolution
-
MA1492 is a distinct type of archaeal geranylgeranyl reductase that is not homologous to known geranylgeranyl reductases, but is homologous to phytoene desaturase CrtI, which is the carotenogenic enzyme that catalyzes oxidation/isomerization of phytoene to lycopene, CrtI, EC 1.3.5.6
-
physiological function
the enzyme is involved in the biosynthesis of archaeal membrane lipids
physiological function
MA1492 might play a physiological role in the membrane lipid biosynthesis
physiological function
the enzyme is essential in phospholipid biosynthesis. Reduction of the isoprenoid chains occurs only when archaeal ferredoxin is expressed with geranylgeranyl reductase, suggesting the role of ferredoxin as a specific electron donor for the reductase
physiological function
-
MA1492 might play a physiological role in the membrane lipid biosynthesis
-
physiological function
-
the enzyme is essential in phospholipid biosynthesis. Reduction of the isoprenoid chains occurs only when archaeal ferredoxin is expressed with geranylgeranyl reductase, suggesting the role of ferredoxin as a specific electron donor for the reductase
-
Show AA Sequence and Transmembrane Helices (594 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
divided into the FADbinding, catalytic and C-terminal domains
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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
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
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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F219L
site-directed mutagenesis, the mutant enzymes ceases GGPP reduction at H4GGPP without significant conversion to H6GGPP
G91H
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
site-directed mutagenesis, the mutant does not accumulate appreciable levels of H2GGPP at any point during the reaction, the mutant enzyme shows increased H6GGPP production compared to the wild-type enzyme
I206F/L377H
site-directed mutagenesis, the mutant does not accumulate appreciable levels of H2GGPP at any point during the reaction, the mutant enzyme shows increased H6GGPP production compared to the wild-type enzyme
L377H
site-directed mutagenesis, the mutant does not accumulate appreciable levels of H2GGPP at any point during the reaction, the mutant enzyme shows increased H6GGPP production compared to the wild-type enzyme
F219L
-
site-directed mutagenesis, the mutant enzymes ceases GGPP reduction at H4GGPP without significant conversion to H6GGPP
-
G91H
-
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
-
site-directed mutagenesis, the mutant does not accumulate appreciable levels of H2GGPP at any point during the reaction, the mutant enzyme shows increased H6GGPP production compared to the wild-type enzyme
-
L377H
-
site-directed mutagenesis, the mutant does not accumulate appreciable levels of H2GGPP at any point during the reaction, the mutant enzyme shows increased H6GGPP production compared to the wild-type enzyme
-
additional information
additional information
successful production of an intact archaeal membrane lipid, which has fully saturated isoprenoid chains, in bacterial cells, by heterologous expression of the enzyme from Methanosarcina acetivorans, overview. Introduction of six phospholipid biosynthetic genes from a methanogenic archaeon, Methanosarcina acetivorans, in Escherichia coli enables the host bacterium to synthesize the archaeal lipid, i.e. diphytanylglyceryl phosphoglycerol, while a glycerol modification of the phosphate group that is probably catalyzed by endogenous Escherichia coli enzymes. Reduction of the isoprenoid chains occurs only when archaeal ferredoxin is expressed with geranylgeranyl reductase, suggesting the role of ferredoxin as a specific electron donor for the reductase. Geranylgeranyl reductase from the thermoacidophilic archaeon Sulfolobus acidocaldarius can, by itself, replace both its orthologue and ferredoxin from Methanosarcina acetivorans, which indicates that an endogenous redox system of Escherichia coli reduces the enzyme
additional information
-
successful production of an intact archaeal membrane lipid, which has fully saturated isoprenoid chains, in bacterial cells, by heterologous expression of the enzyme from Methanosarcina acetivorans, overview. Introduction of six phospholipid biosynthetic genes from a methanogenic archaeon, Methanosarcina acetivorans, in Escherichia coli enables the host bacterium to synthesize the archaeal lipid, i.e. diphytanylglyceryl phosphoglycerol, while a glycerol modification of the phosphate group that is probably catalyzed by endogenous Escherichia coli enzymes. Reduction of the isoprenoid chains occurs only when archaeal ferredoxin is expressed with geranylgeranyl reductase, suggesting the role of ferredoxin as a specific electron donor for the reductase. Geranylgeranyl reductase from the thermoacidophilic archaeon Sulfolobus acidocaldarius can, by itself, replace both its orthologue and ferredoxin from Methanosarcina acetivorans, which indicates that an endogenous redox system of Escherichia coli reduces the enzyme
-
additional information
structure-guided design of the enzyme yields SaGGR variants that enhance the rate of H6GGPP product formation. Additional mutants are observed to arrest the degree of GGPP reduction at H2GGPP and H4GGPP. Crystal structures of these variants reveal the structural bases for their altered activities, in addition to providing insight into the SaGGR mechanism. Three mutants (I206F, L377H, and I206F/L377H) exhibit faster production of H6GGPP than the wild-type, increasing the overall rate of product formation by up to 2.4fold
additional information
-
structure-guided design of the enzyme yields SaGGR variants that enhance the rate of H6GGPP product formation. Additional mutants are observed to arrest the degree of GGPP reduction at H2GGPP and H4GGPP. Crystal structures of these variants reveal the structural bases for their altered activities, in addition to providing insight into the SaGGR mechanism. Three mutants (I206F, L377H, and I206F/L377H) exhibit faster production of H6GGPP than the wild-type, increasing the overall rate of product formation by up to 2.4fold
-
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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
recombinant N-terminally poly-His-tagged enzyme MA1492 from Escherichia coli strain KRX by cobalt affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Xu, Q.; Eguchi, T.; Mathews, I.I.; Rife, C.L.; Chiu, H.J.; Farr, C.L.; Feuerhelm, J.; Jaroszewski, L.; Klock, H.E.; Knuth, M.W.; Miller, M.D.; Weekes, D.; Elsliger, M.A.; Deacon, A.M.; Godzik, A.; Lesley, S.A.; Wilson, I.A.
Insights into substrate specificity of geranylgeranyl reductases revealed by the structure of digeranylgeranylglycerophospholipid reductase, an essential enzyme in the biosynthesis of archaeal membrane lipids
J. Mol. Biol.
404
403-417
2010
Thermoplasma acidophilum (Q9HKS9)
brenda
Murakami, M.; Shibuya, K.; Nakayama, T.; Nishino, T.; Yoshimura, T.; Hemmi, H.
Geranylgeranyl reductase involved in the biosynthesis of archaeal membrane lipids in the hyperthermophilic archaeon Archaeoglobus fulgidus
FEBS J.
274
805-814
2007
Archaeoglobus fulgidus (O29786), Archaeoglobus fulgidus
brenda
Sato, S.; Murakami, M.; Yoshimura, T.; Hemmi, H.
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
J. Bacteriol.
190
3923-3929
2008
Sulfolobus acidocaldarius (Q4JA33)
brenda
Sasaki, D.; Fujihashi, M.; Iwata, Y.; Murakami, M.; Yoshimura, T.; Hemmi, H.; Miki, K.
Structure and mutation analysis of archaeal geranylgeranyl reductase
J. Mol. Biol.
409
543-557
2011
Sulfolobus acidocaldarius (Q4JA33)
brenda
Ogawa, T.; Isobe, K.; Mori, T.; Asakawa, S.; Yoshimura, T.; Hemmi, H.
A novel geranylgeranyl reductase from the methanogenic archaeon Methanosarcinaacetivorans displays unique regiospecificity
FEBS J.
281
3165-3176
2014
Methanosarcina acetivorans (Q8TQP8), Methanosarcina acetivorans, Methanosarcina acetivorans DSM 2834 (Q8TQP8)
brenda
Isobe, K.; Ogawa, T.; Hirose, K.; Yokoi, T.; Yoshimura, T.; Hemmi, H.
Geranylgeranyl reductase and ferredoxin from Methanosarcina acetivorans are required for the synthesis of fully reduced archaeal membrane lipid in Escherichia coli cells
J. Bacteriol.
196
417-423
2014
Methanosarcina acetivorans (Q8TQQ6), Methanosarcina acetivorans DSM 2834 (Q8TQQ6)
brenda
Kung, Y.; McAndrew, R.P.; Xie, X.; Liu, C.C.; Pereira, J.H.; Adams, P.D.; Keasling, J.D.
Constructing tailored isoprenoid products by structure-guided modification of geranylgeranyl reductase
Structure
22
1028-1036
2014
Sulfolobus acidocaldarius (Q4JA33), Sulfolobus acidocaldarius DSM 639 (Q4JA33)
brenda
Meadows, C.; Mingardon, F.; Garabedian, B.; Baidoo, E.; Benites, V.; Rodrigues, A.; Abourjeily, R.; Chanal, A.; Lee, T.
Discovery of novel geranylgeranyl reductases and characterization of their substrate promiscuity
Biotechnol. Biofuels
11
340
2018
Methanobrevibacter ruminantium (D3E3T0), Methanocaldococcus infernus (D5VQY0), Methanococcoides burtonii (Q12WF0), Methanosarcina acetivorans (Q8TQQ6), Thermoplasma acidophilum (Q9HKS9), Thermococcus nautili (W8NRH6), Methanobrevibacter ruminantium DSM 1039 (D3E3T0), Methanosarcina acetivorans DSM 2834 (Q8TQQ6), Methanocaldococcus infernus DSM 11812 (D5VQY0), Methanococcoides burtonii DSM 6242 (Q12WF0)
brenda
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Release 2023.1 (January 2023)
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