Literature summary for 1.3.1.101 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.

Cloned(Commentary)

Cloned (Comment)	Organism
-	Thermoplasma acidophilum

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

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
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	UniProt	Comment	Textmining
Thermoplasma acidophilum	Q9HKS9	-	-

Purification (Comment)	Organism
-	Thermoplasma acidophilum

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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)+	-	?

Synonyms	Comment	Organism
2,3-digeranylgeranylglycerophospholipid reductase	-	Thermoplasma acidophilum
digeranylgeranylglycerophospholipid reductase	-	Thermoplasma acidophilum

Cofactor	Comment	Organism	Structure
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

General Information	Comment	Organism
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