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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.1.101
-
 Thermoplasma acidophilum

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.3.1.101 vapor-diffusion method, crystal structure at 1.6 A resolution, in complex with flavin adenine dinucleotide (FAD) and a bacterial lipid Thermoplasma acidophilum
1.3.7.11 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.3.7.11 43400
-
 x * 43400, calculated Thermoplasma acidophilum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.1.101 2,3-bis-O-geranylgeranyl-sn-glyceryl 1-phosphate + 8 NAD(P)H + 8 H+ Thermoplasma acidophilum the enzyme catalyzes a critical step in the biosynthesis of archaeal membrane lipids. The saturation of hydrocarbon chains confers the ability to resist hydrolysis and oxidation and helps archaea withstand extreme conditions 2,3-bis-O-phytanyl-sn-glycerol 1-phosphate + 8 NAD(P)+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.101 Thermoplasma acidophilum Q9HKS9
-
-
1.3.7.11 Thermoplasma acidophilum Q9HKS9
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.1.101
-
 Thermoplasma acidophilum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.1.101 2,3-bis-O-geranylgeranyl-sn-glyceryl 1-phosphate + 8 NAD(P)H + 8 H+ the enzyme catalyzes a critical step in the biosynthesis of archaeal membrane lipids. The saturation of hydrocarbon chains confers the ability to resist hydrolysis and oxidation and helps archaea withstand extreme conditions Thermoplasma acidophilum 2,3-bis-O-phytanyl-sn-glycerol 1-phosphate + 8 NAD(P)+
-
 ?
1.3.7.11 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

EC Number Subunits Comment Organism
1.3.7.11 ? x * 43400, calculated Thermoplasma acidophilum

Synonyms

EC Number Synonyms Comment Organism
1.3.1.101 2,3-digeranylgeranylglycerophospholipid reductase
-
 Thermoplasma acidophilum
1.3.1.101 digeranylgeranylglycerophospholipid reductase
-
 Thermoplasma acidophilum
1.3.7.11 Ta0516
-
 Thermoplasma acidophilum

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.1.101 FAD the sequence PxxYxWxFP defines a specificity pocket in the enzyme and precisely aligns the double bond of the geranyl group with respect to the FAD cofactor, thus providing a structural basis for the substrate specificity of geranylgeranyl reductases. FAD switches between two conformations that correspond to the reductive and oxidative half cycles. The structure provides evidence that substrate binding likely involves conformational changes, which are coupled to the two conformational states of the FAD Thermoplasma acidophilum
1.3.7.11 FAD
-
 Thermoplasma acidophilum

pI Value

EC Number Organism Comment pI Value Maximum pI Value
1.3.7.11 Thermoplasma acidophilum calculated
-
 7

General Information

EC Number General Information Comment Organism
1.3.1.83 evolution highly conserved regions of characterized geranylgeranyl reductases, GGRs, from archaea, plants, and bacteria, overview Thermoplasma acidophilum
1.3.1.83 additional information structural basis for recognition of a geranyl group by geranylgeranyl reductases, GGRs, overview Thermoplasma acidophilum
1.3.1.83 physiological function DGGR catalyzes a critical step in the biosynthesis of archaeal membrane lipids. The saturation of hydrocarbon chains confers the ability to resist hydrolysis and oxidation and helps archaea withstand extreme conditions Thermoplasma acidophilum
1.3.1.101 physiological function the enzyme catalyzes a critical step in the biosynthesis of archaeal membrane lipids. The saturation of hydrocarbon chains confers the ability to resist hydrolysis and oxidation and helps archaea withstand extreme conditions Thermoplasma acidophilum