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CTP + 1,2-bis-(O-geranylgeranyl)-sn-glycerol 3-phosphate
diphosphate + CDP-1,2-bis-(O-geranylgeranyl)-sn-glycerol
CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate
diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
dCTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate
diphosphate + dCDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
-
-
-
?
additional information
?
-
CTP + 1,2-bis-(O-geranylgeranyl)-sn-glycerol 3-phosphate
diphosphate + CDP-1,2-bis-(O-geranylgeranyl)-sn-glycerol
-
94% of the activity with 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate
-
-
?
CTP + 1,2-bis-(O-geranylgeranyl)-sn-glycerol 3-phosphate
diphosphate + CDP-1,2-bis-(O-geranylgeranyl)-sn-glycerol
-
94% of the activity with 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate
-
-
?
CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate
diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
-
-
-
?
CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate
diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
ApCarS is a CTP transferase
-
-
?
CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate
diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
-
-
-
?
CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate
diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
ApCarS is a CTP transferase
-
-
?
CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate
diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
-
-
-
?
CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate
diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
ApCarS is a CTP transferase
-
-
?
CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate
diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
-
-
-
?
CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate
diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
ApCarS is a CTP transferase
-
-
?
CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate
diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
-
-
-
?
CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate
diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
ApCarS is a CTP transferase
-
-
?
CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate
diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
-
-
-
?
CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate
diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
-
-
-
-
?
CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate
diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
-
the enzyme is involved in the biosynthesis of polar lipids in archaea
-
-
?
CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate
diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
-
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
-
-
?
CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate
diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
-
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
-
-
?
CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate
diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
-
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
-
-
?
CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate
diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
-
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
-
-
?
CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate
diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
-
-
-
-
?
CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate
diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
-
the enzyme is involved in the biosynthesis of polar lipids in archaea
-
-
?
additional information
?
-
purified ApCarS exhibits strong CTP-binding activity, binding site structure, overview
-
-
-
additional information
?
-
-
purified ApCarS exhibits strong CTP-binding activity, binding site structure, overview
-
-
-
additional information
?
-
purified ApCarS exhibits strong CTP-binding activity, binding site structure, overview
-
-
-
additional information
?
-
purified ApCarS exhibits strong CTP-binding activity, binding site structure, overview
-
-
-
additional information
?
-
purified ApCarS exhibits strong CTP-binding activity, binding site structure, overview
-
-
-
additional information
?
-
purified ApCarS exhibits strong CTP-binding activity, binding site structure, overview
-
-
-
additional information
?
-
no substrates: ATP, GTP, TTP
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate
diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate
diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
-
-
-
?
CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate
diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
-
-
-
?
CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate
diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
-
-
-
?
CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate
diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
-
-
-
?
CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate
diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
-
-
-
?
CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate
diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
-
the enzyme is involved in the biosynthesis of polar lipids in archaea
-
-
?
CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate
diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
-
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
-
-
?
CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate
diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
-
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
-
-
?
CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate
diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol
-
the enzyme is involved in the biosynthesis of polar lipids in archaea
-
-
?
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the enzyme comprises a transmembrane (TM) domain with five helices and cytoplasmic loops that together form a large charged cavity. The cytoplasmic cavity primarily comprises TM1, TM2, TM3 and TM4, and is loosely occluded by TM5. The remaining portion of the cavity is formed by two cytoplasmic loops (CLs): CL1 (between TM1 and TM2) and CL2 (between TM3 and TM4). CL1 and CL2 form the cytoplasmic domain (CPD), which caps the transmembrance domain (TMD). CL1, which is longer than CL2, is stabilized by packing against one side of TM3
brenda
-
the enzyme comprises a transmembrane (TM) domain with five helices and cytoplasmic loops that together form a large charged cavity. The cytoplasmic cavity primarily comprises TM1, TM2, TM3 and TM4, and is loosely occluded by TM5. The remaining portion of the cavity is formed by two cytoplasmic loops (CLs): CL1 (between TM1 and TM2) and CL2 (between TM3 and TM4). CL1 and CL2 form the cytoplasmic domain (CPD), which caps the transmembrance domain (TMD). CL1, which is longer than CL2, is stabilized by packing against one side of TM3
-
brenda
-
the enzyme comprises a transmembrane (TM) domain with five helices and cytoplasmic loops that together form a large charged cavity. The cytoplasmic cavity primarily comprises TM1, TM2, TM3 and TM4, and is loosely occluded by TM5. The remaining portion of the cavity is formed by two cytoplasmic loops (CLs): CL1 (between TM1 and TM2) and CL2 (between TM3 and TM4). CL1 and CL2 form the cytoplasmic domain (CPD), which caps the transmembrance domain (TMD). CL1, which is longer than CL2, is stabilized by packing against one side of TM3
-
brenda
-
the enzyme comprises a transmembrane (TM) domain with five helices and cytoplasmic loops that together form a large charged cavity. The cytoplasmic cavity primarily comprises TM1, TM2, TM3 and TM4, and is loosely occluded by TM5. The remaining portion of the cavity is formed by two cytoplasmic loops (CLs): CL1 (between TM1 and TM2) and CL2 (between TM3 and TM4). CL1 and CL2 form the cytoplasmic domain (CPD), which caps the transmembrance domain (TMD). CL1, which is longer than CL2, is stabilized by packing against one side of TM3
-
brenda
-
the enzyme comprises a transmembrane (TM) domain with five helices and cytoplasmic loops that together form a large charged cavity. The cytoplasmic cavity primarily comprises TM1, TM2, TM3 and TM4, and is loosely occluded by TM5. The remaining portion of the cavity is formed by two cytoplasmic loops (CLs): CL1 (between TM1 and TM2) and CL2 (between TM3 and TM4). CL1 and CL2 form the cytoplasmic domain (CPD), which caps the transmembrance domain (TMD). CL1, which is longer than CL2, is stabilized by packing against one side of TM3
-
brenda
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
structural comparisons and analyses, combined with functional studies, not only elucidated the mechanism governing the biosynthesis of phospholipids with ether-bonded isoprenoid chains by CTP transferase, but also provided insights into the evolution of this enzyme superfamily from archaea to bacteria and eukaryotes
evolution
-
structural comparisons and analyses, combined with functional studies, not only elucidated the mechanism governing the biosynthesis of phospholipids with ether-bonded isoprenoid chains by CTP transferase, but also provided insights into the evolution of this enzyme superfamily from archaea to bacteria and eukaryotes
-
evolution
-
structural comparisons and analyses, combined with functional studies, not only elucidated the mechanism governing the biosynthesis of phospholipids with ether-bonded isoprenoid chains by CTP transferase, but also provided insights into the evolution of this enzyme superfamily from archaea to bacteria and eukaryotes
-
evolution
-
structural comparisons and analyses, combined with functional studies, not only elucidated the mechanism governing the biosynthesis of phospholipids with ether-bonded isoprenoid chains by CTP transferase, but also provided insights into the evolution of this enzyme superfamily from archaea to bacteria and eukaryotes
-
evolution
-
structural comparisons and analyses, combined with functional studies, not only elucidated the mechanism governing the biosynthesis of phospholipids with ether-bonded isoprenoid chains by CTP transferase, but also provided insights into the evolution of this enzyme superfamily from archaea to bacteria and eukaryotes
-
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
metabolism
-
the enzyme is involved in the biosynthesis of polar lipids in archaea
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
-
metabolism
-
the enzyme is involved in the biosynthesis of polar lipids in archaea
-
physiological function
ApCarS is a CTP transferase
physiological function
-
ApCarS is a CTP transferase
-
physiological function
-
ApCarS is a CTP transferase
-
physiological function
-
ApCarS is a CTP transferase
-
physiological function
-
ApCarS is a CTP transferase
-
additional information
the enzyme comprises a transmembrane domain with five helices and cytoplasmic loops that together form a large charged cavity providing a binding site for CTP, modeling of the specific lipophilic substrate-binding site. Archaeol binds within two hydrophobic membrane-embedded grooves formed by the flexible transmembrane helix 5 (TM5), together with TM1 and TM4. CTP binds to one side of the central cavity of ApCarS and stabilizes the CPD through tight contacts. Recognition of CTP by ApCarS occurs through a combination of extensive polar and hydrophobic interactions, detailed overview
additional information
-
the enzyme comprises a transmembrane domain with five helices and cytoplasmic loops that together form a large charged cavity providing a binding site for CTP, modeling of the specific lipophilic substrate-binding site. Archaeol binds within two hydrophobic membrane-embedded grooves formed by the flexible transmembrane helix 5 (TM5), together with TM1 and TM4. CTP binds to one side of the central cavity of ApCarS and stabilizes the CPD through tight contacts. Recognition of CTP by ApCarS occurs through a combination of extensive polar and hydrophobic interactions, detailed overview
additional information
-
the enzyme comprises a transmembrane domain with five helices and cytoplasmic loops that together form a large charged cavity providing a binding site for CTP, modeling of the specific lipophilic substrate-binding site. Archaeol binds within two hydrophobic membrane-embedded grooves formed by the flexible transmembrane helix 5 (TM5), together with TM1 and TM4. CTP binds to one side of the central cavity of ApCarS and stabilizes the CPD through tight contacts. Recognition of CTP by ApCarS occurs through a combination of extensive polar and hydrophobic interactions, detailed overview
-
additional information
-
the enzyme comprises a transmembrane domain with five helices and cytoplasmic loops that together form a large charged cavity providing a binding site for CTP, modeling of the specific lipophilic substrate-binding site. Archaeol binds within two hydrophobic membrane-embedded grooves formed by the flexible transmembrane helix 5 (TM5), together with TM1 and TM4. CTP binds to one side of the central cavity of ApCarS and stabilizes the CPD through tight contacts. Recognition of CTP by ApCarS occurs through a combination of extensive polar and hydrophobic interactions, detailed overview
-
additional information
-
the enzyme comprises a transmembrane domain with five helices and cytoplasmic loops that together form a large charged cavity providing a binding site for CTP, modeling of the specific lipophilic substrate-binding site. Archaeol binds within two hydrophobic membrane-embedded grooves formed by the flexible transmembrane helix 5 (TM5), together with TM1 and TM4. CTP binds to one side of the central cavity of ApCarS and stabilizes the CPD through tight contacts. Recognition of CTP by ApCarS occurs through a combination of extensive polar and hydrophobic interactions, detailed overview
-
additional information
-
the enzyme comprises a transmembrane domain with five helices and cytoplasmic loops that together form a large charged cavity providing a binding site for CTP, modeling of the specific lipophilic substrate-binding site. Archaeol binds within two hydrophobic membrane-embedded grooves formed by the flexible transmembrane helix 5 (TM5), together with TM1 and TM4. CTP binds to one side of the central cavity of ApCarS and stabilizes the CPD through tight contacts. Recognition of CTP by ApCarS occurs through a combination of extensive polar and hydrophobic interactions, detailed overview
-
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A29W
site-directed mutagenesis, the mutant shows no 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) substrate binding activity
D100A
site-directed mutagenesis, the mutant shows weak 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) substrate binding activity compared to wild-type
D122A
site-directed mutagenesis, the mutant shows no 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) substrate binding activity
D125A
site-directed mutagenesis, the mutant shows no 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) substrate binding activity
F126A
site-directed mutagenesis, the mutant shows no 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) substrate binding activity
H157A
site-directed mutagenesis, the mutant exhibits enhanced DGGGP-binding activity compared to wild-type
K57A
site-directed mutagenesis, the mutant shows weak 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) substrate binding activity compared to wild-type
L124W
site-directed mutagenesis, the mutant shows no 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) substrate binding activity
L156W
site-directed mutagenesis, the mutant shows no 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) substrate binding activity
N28A
site-directed mutagenesis, the mutant shows weak 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) substrate binding activity compared to wild-type
Q123A
site-directed mutagenesis, the mutant exhibits enhanced DGGGP-binding activity compared to wild-type
D100A
-
site-directed mutagenesis, the mutant shows weak 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) substrate binding activity compared to wild-type
-
D125A
-
site-directed mutagenesis, the mutant shows no 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) substrate binding activity
-
H157A
-
site-directed mutagenesis, the mutant exhibits enhanced DGGGP-binding activity compared to wild-type
-
K57A
-
site-directed mutagenesis, the mutant shows weak 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) substrate binding activity compared to wild-type
-
N28A
-
site-directed mutagenesis, the mutant shows weak 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) substrate binding activity compared to wild-type
-
D100A
-
site-directed mutagenesis, the mutant shows weak 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) substrate binding activity compared to wild-type
-
D125A
-
site-directed mutagenesis, the mutant shows no 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) substrate binding activity
-
H157A
-
site-directed mutagenesis, the mutant exhibits enhanced DGGGP-binding activity compared to wild-type
-
K57A
-
site-directed mutagenesis, the mutant shows weak 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) substrate binding activity compared to wild-type
-
N28A
-
site-directed mutagenesis, the mutant shows weak 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) substrate binding activity compared to wild-type
-
D100A
-
site-directed mutagenesis, the mutant shows weak 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) substrate binding activity compared to wild-type
-
D125A
-
site-directed mutagenesis, the mutant shows no 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) substrate binding activity
-
H157A
-
site-directed mutagenesis, the mutant exhibits enhanced DGGGP-binding activity compared to wild-type
-
K57A
-
site-directed mutagenesis, the mutant shows weak 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) substrate binding activity compared to wild-type
-
N28A
-
site-directed mutagenesis, the mutant shows weak 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) substrate binding activity compared to wild-type
-
D100A
-
site-directed mutagenesis, the mutant shows weak 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) substrate binding activity compared to wild-type
-
D125A
-
site-directed mutagenesis, the mutant shows no 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) substrate binding activity
-
H157A
-
site-directed mutagenesis, the mutant exhibits enhanced DGGGP-binding activity compared to wild-type
-
K57A
-
site-directed mutagenesis, the mutant shows weak 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) substrate binding activity compared to wild-type
-
N28A
-
site-directed mutagenesis, the mutant shows weak 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) substrate binding activity compared to wild-type
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Morii, H.; Nishihara, M.; Koga, Y.
CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase in the methanogenic archaeon Methanothermobacter thermoautotrophicus
J. Biol. Chem.
275
36568-36574
2000
Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus DSM 1053
brenda
Morii, H.; Koga, Y.
CDP-2,3-di-O-geranylgeranyl-sn-glycerol:L-serine O-archaetidyltransferase (archaetidylserine synthase) in the methanogenic archaeon Methanothermobacter thermautotrophicus
J. Bacteriol.
185
1181-1189
2003
Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus DSM 1053
brenda
Jain, S.; Caforio, A.; Fodran, P.; Lolkema, J.S.; Minnaard, A.J.; Driessen, A.J.
Identification of CDP-archaeol synthase, a missing link of ether lipid biosynthesis in Archaea
Chem. Biol.
21
1392-1401
2014
Archaeoglobus fulgidus (O28534)
brenda
Ren, S.; Caforio, A.; Yang, Q.; Sun, B.; Yu, F.; Zhu, X.; Wang, J.; Dou, C.; Fu, Q.; Huang, N.; Sun, Q.; Nie, C.; Qi, S.; Gong, X.; He, J.; Wei, Y.; Driessen, A.J.; Cheng, W.
Structural and mechanistic insights into the biosynthesis of CDP-archaeol in membranes
Cell Res.
27
1378-1391
2017
Aeropyrum pernix (Q9YF05), Aeropyrum pernix, Aeropyrum pernix ATCC 700893 (Q9YF05), Aeropyrum pernix DSM 11879 (Q9YF05), Aeropyrum pernix JCM 9820 (Q9YF05), Aeropyrum pernix NBRC 100138 (Q9YF05)
brenda