Any feedback?
Please rate this page

BRENDA support

Literature summary for extracted from

  • 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 (2010), J. Mol. Biol., 404, 403-417.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Thermoplasma acidophilum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
x * 43400, calculated Thermoplasma acidophilum


Organism UniProt Comment Textmining
Thermoplasma acidophilum Q9HKS9

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2,3-di-O-geranylgeranylglyceryl phosphate + 16 reduced ferredoxin [iron-sulfur] cluster + 16 H+
Thermoplasma acidophilum 2,3-di-O-phytanylglyceryl phosphate + 16 oxidized ferredoxin [iron-sulfur] cluster


Subunits Comment Organism
? x * 43400, calculated Thermoplasma acidophilum


Synonyms Comment Organism
Thermoplasma acidophilum


Cofactor Comment Organism Structure
Thermoplasma acidophilum

pI Value

Organism Comment pI Value Maximum pI Value
Thermoplasma acidophilum calculated