Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

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

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+

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

ECTree

     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.7 With an iron-sulfur protein as acceptor
                1.3.7.11 2,3-bis-O-geranylgeranyl-sn-glycero-phospholipid reductase

Cloned

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

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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)