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Information on EC 1.3.1.101 - 2,3-bis-O-geranylgeranyl-sn-glycerol 1-phosphate reductase [NAD(P)H] for references in articles please use BRENDA:EC1.3.1.101Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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The expected taxonomic range for this enzyme is: Thermoplasma acidophilum
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2,3-bis-O-geranylgeranyl-sn-glycerol 1-phosphate reductase [NAD(P)H]
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2,3-bis-(O-phytanyl)-sn-glycerol 1-phosphate + 8 NAD(P)+ = 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate + 8 NAD(P)H + 8 H+
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archaetidylserine and archaetidylethanolamine biosynthesis
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Glycerophospholipid metabolism
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2,3-bis-O-phytanyl-sn-glycerol 1-phosphate:NAD(P)+ oxidoreductase
A flavoprotein (FAD). The enzyme from the archaeon Thermoplasma acidophilum is involved in the biosynthesis of membrane lipids. In vivo the reaction occurs in the reverse direction with the formation of 2,3-bis-O-phytanyl-sn-glycerol 1-phosphate. cf. EC 1.3.7.11, 2,3-bis-O-geranylgeranyl-sn-glycero-phospholipid reductase.
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2,3-digeranylgeranylglycerophospholipid reductase
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digeranylgeranylglycerophospholipid reductase
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UniProt
brenda
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physiological function
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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
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2,3-bis-O-geranylgeranyl-sn-glycerol 1-phosphate + 8 NAD(P)H + 8 H+
2,3-bis-O-phytanyl-sn-glycerol 1-phosphate + 8 NAD(P)+
2,3-bis-O-geranylgeranyl-sn-glyceryl 1-phosphate + 8 NAD(P)H + 8 H+
2,3-bis-O-phytanyl-sn-glycerol 1-phosphate + 8 NAD(P)+
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
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2,3-bis-O-phytyl-sn-glycero-phosphoethanolamine + NAD(P)H + H+
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2,3-bis-O-phytyl-sn-glyceryl phosphate + NAD(P)H + H+
2,3-bis-O-phytanyl-sn-glycerol 1-phosphate + NAD(P)+
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3-O-(2,3-bis-O-phytyl-sn-glycero-phospho)-sn-glycerol + NAD(P)H + H+
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additional information
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neither 2,3-bis-O-geranylgeranylglycerol nor 2,3-bis-O-geranylgeranylglyceryl phosphate dimethyl ester is recognized as a substrate
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2,3-bis-O-geranylgeranyl-sn-glycerol 1-phosphate + 8 NAD(P)H + 8 H+
2,3-bis-O-phytanyl-sn-glycerol 1-phosphate + 8 NAD(P)+
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2,3-bis-O-geranylgeranyl-sn-glycerol 1-phosphate + 8 NAD(P)H + 8 H+
2,3-bis-O-phytanyl-sn-glycerol 1-phosphate + 8 NAD(P)+
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formation of 2,3-di-O-phytanyl-sn-glyceryl phosphate (archaetidic acid), which is the basic core structure of archaeal membrane lipids
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2,3-bis-O-geranylgeranyl-sn-glycerol 1-phosphate + 8 NAD(P)H + 8 H+
2,3-bis-O-phytanyl-sn-glycerol 1-phosphate + 8 NAD(P)+
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formation of 2,3-di-O-phytanylglyceryl phosphate, which is the basic core structure of archaeal membrane lipids
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2,3-bis-O-geranylgeranyl-sn-glycerol 1-phosphate + 8 NAD(P)H + 8 H+
2,3-bis-O-phytanyl-sn-glycerol 1-phosphate + 8 NAD(P)+
2,3-bis-O-geranylgeranyl-sn-glyceryl 1-phosphate + 8 NAD(P)H + 8 H+
2,3-bis-O-phytanyl-sn-glycerol 1-phosphate + 8 NAD(P)+
Q9HKS9
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
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2,3-bis-O-geranylgeranyl-sn-glycerol 1-phosphate + 8 NAD(P)H + 8 H+
2,3-bis-O-phytanyl-sn-glycerol 1-phosphate + 8 NAD(P)+
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formation of 2,3-di-O-phytanyl-sn-glyceryl phosphate (archaetidic acid), which is the basic core structure of archaeal membrane lipids
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2,3-bis-O-geranylgeranyl-sn-glycerol 1-phosphate + 8 NAD(P)H + 8 H+
2,3-bis-O-phytanyl-sn-glycerol 1-phosphate + 8 NAD(P)+
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formation of 2,3-di-O-phytanylglyceryl phosphate, which is the basic core structure of archaeal membrane lipids
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NAD(P)H
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required for activity
FAD
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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
FAD
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the cofactor is bound to the enzyme in the ratio 1:1
FAD
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required for activity
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additional information
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the enzyme does not require metal ions for activity
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additional information
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EDTA has little effect on activity
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0.0115
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pH 6.5, 50°C, substrate: 2,3-di-O-geranylgeranyl-sn-glycerol 1-phosphate
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membrane associated protein
brenda
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43000
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x * 43000, SDS-PAGE
45000
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x * 45000, SDS-PAGE
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x * 43000, SDS-PAGE
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vapor-diffusion method, crystal structure at 1.6 A resolution, in complex with flavin adenine dinucleotide (FAD) and a bacterial lipid
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expression in Escherichia coli Rosetta (DE3)
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GGR_PICTO
Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)
397
43748
Swiss-Prot
GGR_THEAC
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
396
43353
Swiss-Prot
GGR_THEVO
Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)
396
43203
Swiss-Prot
A0A0D8DJJ4_9EURY
397
43525
TrEMBL
A0A2K3JIM4_9EURY
396
43073
TrEMBL
A0A1Q9P433_9ARCH
455
51060
TrEMBL
A0A1Q9NPD1_9ARCH
347
39387
TrEMBL
A0A1Q9PAG0_9ARCH
409
44341
TrEMBL
A0A0A7LEX9_9EURY
396
43254
TrEMBL
R9TB51_METII
Methanomassiliicoccus intestinalis (strain Issoire-Mx1)
396
42854
TrEMBL
N6WT34_9EURY
400
43788
TrEMBL
A0A256XLH5_9EURY
399
43445
TrEMBL
A0A0Q0XL60_9EURY
397
43525
TrEMBL
S0AMA9_FERAC
396
43581
TrEMBL
A0A1W2G0P5_9EURY
397
43748
TrEMBL
A0A151EIC1_9EURY
399
43423
TrEMBL
A0A1Q9P1Q8_9ARCH
453
50690
TrEMBL
A0A1V4ZAI9_9EURY
396
42825
TrEMBL
A0A1V4YSI9_9EURY
399
43212
TrEMBL
A0A256ZBR9_9EURY
414
44357
TrEMBL
A0A0Q4BCM5_9EURY
399
43357
TrEMBL
A0A1V0N495_9EURY
396
43594
TrEMBL
A0A0Q4B2X2_9EURY
393
42309
TrEMBL
A0A1V4ZC36_9EURY
53
5938
TrEMBL
T0NJT8_9EURY
396
43573
TrEMBL
A0A151E1J3_9EURY
399
43584
TrEMBL
R9T7B0_METII
Methanomassiliicoccus intestinalis (strain Issoire-Mx1)
391
42487
TrEMBL
A0A151DZ68_9EURY
396
43229
TrEMBL
A0A151EEC4_9EURY
397
43412
TrEMBL
A0A0Q0VQ29_9EURY
397
43525
TrEMBL
A0A179EGI9_9EURY
416
46433
TrEMBL
A0A0Q4BIJ4_9EURY
397
43045
TrEMBL
A0A151EM79_9EURY
397
43433
TrEMBL
M4YNR1_THEXX
Thermoplasmatales archaeon (strain BRNA1)
398
43282
TrEMBL
A0A2K3J3Y2_9EURY
396
43073
TrEMBL
A0A2K3IX22_9EURY
403
44457
TrEMBL
M9SBC6_METAX
Methanomethylophilus alvus (strain Mx1201)
398
43194
TrEMBL
A0A1V4TBZ7_9EURY
395
42259
TrEMBL
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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
J. Mol. Biol.
404
403-417
2010
Thermoplasma acidophilum, Thermoplasma acidophilum (Q9HKS9)
brenda
Nishimura, Y.; Eguchi, T.
Stereochemistry of reduction in digeranylgeranylglycerophospholipid reductase involved in the biosynthesis of archaeal membrane lipids from Thermoplasma acidophilum
Bioorg. Chem.
35
276-283
2007
Thermoplasma acidophilum, Thermoplasma acidophilum (Q9HKS9)
brenda
Nishimura, Y.; Eguchi, T.
Biosynthesis of archaeal membrane lipids: digeranylgeranylglycerophospholipid reductase of the thermoacidophilic archaeon Thermoplasma acidophilum
J. Biochem.
139
1073-1081
2006
Thermoplasma acidophilum, Thermoplasma acidophilum (Q9HKS9)
brenda
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