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Literature summary for 2.7.7.67 extracted from

  • Morii, H.; Nishihara, M.; Koga, Y.
    CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase in the methanogenic archaeon Methanothermobacter thermoautotrophicus (2000), J. Biol. Chem., 275, 36568-36574.
    View publication on PubMed

General Stability

General Stability Organism
freezing and thawing causes a small loss (5–10%) of activity Methanothermobacter thermautotrophicus

Inhibitors

Inhibitors Comment Organism Structure
additional information dithiothreitol shows no effect on the activity Methanothermobacter thermautotrophicus
Triton X-100 0.1%, 96% inhibition Methanothermobacter thermautotrophicus

Localization

Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

Metals/Ions Comment Organism Structure
K+ the enzyme requires Mg2+ (1-2 mM) and K+ (0.5 mM) for maximal activity Methanothermobacter thermautotrophicus
Mg2+ the enzyme requires Mg2+ (1-2 mM) and K+ (0.5 mM) for maximal activity Methanothermobacter thermautotrophicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate Methanothermobacter thermautotrophicus the enzyme catalyses one of the steps in the biosynthesis of polar lipids in archaea, which are characterized by having an sn-glycerol 1-phosphate backbone rather than an sn-glycerol 3-phosphate backbone as is found in bacteria and eukaryotes diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
-
?
CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate Methanothermobacter thermautotrophicus DSM 1053 the enzyme catalyses one of the steps in the biosynthesis of polar lipids in archaea, which are characterized by having an sn-glycerol 1-phosphate backbone rather than an sn-glycerol 3-phosphate backbone as is found in bacteria and eukaryotes diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
-
?

Organism

Organism UniProt Comment Textmining
Methanothermobacter thermautotrophicus
-
-
-
Methanothermobacter thermautotrophicus DSM 1053
-
-
-

Storage Stability

Storage Stability Organism
-20°C, activity in membrane fraction is stable for several months Methanothermobacter thermautotrophicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CTP + 1,2-bis-(O-geranylgeranyl)-sn-glycerol 3-phosphate 94% of the activity with 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate Methanothermobacter thermautotrophicus diphosphate + CDP-1,2-bis-(O-geranylgeranyl)-sn-glycerol
-
?
CTP + 1,2-bis-(O-geranylgeranyl)-sn-glycerol 3-phosphate 94% of the activity with 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate Methanothermobacter thermautotrophicus DSM 1053 diphosphate + CDP-1,2-bis-(O-geranylgeranyl)-sn-glycerol
-
?
CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate the enzyme catalyses one of the steps in the biosynthesis of polar lipids in archaea, which are characterized by having an sn-glycerol 1-phosphate backbone rather than an sn-glycerol 3-phosphate backbone as is found in bacteria and eukaryotes Methanothermobacter thermautotrophicus diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
-
?
CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate unsaturation of the hydrocarbon chains of the substrate is critical. Archaetidic acid with saturated (2,3-phytanyl-glycerophosphate ether) or monounsaturated (2,3-phytyl-glycerophosphate ether) isoprenoid chains of the same carbon number are poor substrates as are analogs with monounsaturated straight chains (2,3-oleyl-glycerophosphate ether), even though they had the same stereostructure as the fully active natural substrate. As to the ester analogs of the substrate, the glycerophosphate esters with geranylgeranioyl chains show high activities. In this case, the 1,2-geranylgeranyl analog shows a half-maximal activity. The activities to the ester analogs of the substrate with oleoyl chains are also in low levels. The results suggest that the enzyme does not recognize ether or ester bonds between glycerophosphate and hydrocarbon chains nor the stereostructure of the glycerophosphate backbone but mainly targets substrates with geranylgeranyl chains Methanothermobacter thermautotrophicus diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
-
?
CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate the enzyme catalyses one of the steps in the biosynthesis of polar lipids in archaea, which are characterized by having an sn-glycerol 1-phosphate backbone rather than an sn-glycerol 3-phosphate backbone as is found in bacteria and eukaryotes Methanothermobacter thermautotrophicus DSM 1053 diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
-
?
CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate unsaturation of the hydrocarbon chains of the substrate is critical. Archaetidic acid with saturated (2,3-phytanyl-glycerophosphate ether) or monounsaturated (2,3-phytyl-glycerophosphate ether) isoprenoid chains of the same carbon number are poor substrates as are analogs with monounsaturated straight chains (2,3-oleyl-glycerophosphate ether), even though they had the same stereostructure as the fully active natural substrate. As to the ester analogs of the substrate, the glycerophosphate esters with geranylgeranioyl chains show high activities. In this case, the 1,2-geranylgeranyl analog shows a half-maximal activity. The activities to the ester analogs of the substrate with oleoyl chains are also in low levels. The results suggest that the enzyme does not recognize ether or ester bonds between glycerophosphate and hydrocarbon chains nor the stereostructure of the glycerophosphate backbone but mainly targets substrates with geranylgeranyl chains Methanothermobacter thermautotrophicus DSM 1053 diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
55
-
-
Methanothermobacter thermautotrophicus

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
45 65 45°C: about 30% of maximal activity, 65°C: about 55% of maximal activity Methanothermobacter thermautotrophicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
-
Methanothermobacter thermautotrophicus

pH Range

pH Minimum pH Maximum Comment Organism
8 9 pH 8.0: about 60% of maximal activity, pH 9.0: about 55% of maximal activity Methanothermobacter thermautotrophicus

General Information

General Information Comment Organism
metabolism the enzyme catalyses one of the steps in the biosynthesis of polar lipids in archaea, which are characterized by having an sn-glycerol 1-phosphate backbone rather than an sn-glycerol 3-phosphate backbone as is found in bacteria and eukaryotes Methanothermobacter thermautotrophicus