1.3.7.11: 2,3-bis-O-geranylgeranyl-sn-glycero-phospholipid reductase
This is an abbreviated version!
For detailed information about 2,3-bis-O-geranylgeranyl-sn-glycero-phospholipid reductase, go to the full flat file.
Reaction
+ 16 oxidized ferredoxin [iron-sulfur] cluster = + 16 reduced ferredoxin [iron-sulfur] cluster + 16 H+
Synonyms
AF0464, CrtI homologue, digeranylgeranylglycerophospholipid reductase, EC 1.3.99.34, geranylgeranyl reductase, GGR, MA1484, MA1492, MA_1484, MA_1492, phytoene dehydrogenase family protein, Sa-GGR, SaGGR, Ta0516
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General Information
General Information on EC 1.3.7.11 - 2,3-bis-O-geranylgeranyl-sn-glycero-phospholipid reductase
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evolution
physiological function
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
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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
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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
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MA1492 might play a physiological role in the membrane lipid biosynthesis
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physiological function
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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
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