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4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol + ATP
2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol + ADP
-
-
-
ir
4-diphosphocytidyl-2C-methyl-D-erythritol + ATP
4-diphosphocytidyl-2C-methyl-D-erythritol 2-phosphate + ADP
non-mevalonate pathway of isoprenoid precursor synthesis
-
-
ir
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
additional information
?
-
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
-
?
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
fourth reaction step of the 2-C-methyl-D-erythritol 4-phosphate pathway
-
-
?
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
the enzyme is essential in the nonmevalonate pathway of isopentenyl diphosphate and dimethylallyl diphosphate biosynthesis
-
-
?
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
i.e. CDP-ME
-
-
?
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
non-mevalonate pathway for isoprenoid biosynthesis
-
-
?
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
-
?
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
involved in terpenoid biosynthesis via deoxyxylulose phosphate pathway
-
-
?
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
the enzyme is essential in the nonmevalonate pathway of isopentenyl diphosphate and dimethylallyl diphosphate biosynthesis, pathway overview
-
-
?
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
i.e. CDP-ME, the cytosine group plays an essential role in substrate recognition by the enzyme
-
-
?
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
the enzyme is essential in the nonmevalonate pathway of isopentenyl diphosphate and dimethylallyl diphosphate biosynthesis, pathway overview
-
-
?
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
i.e. CDP-ME, the cytosine group plays an essential role in substrate recognition by the enzyme
-
-
?
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
-
?
additional information
?
-
-
in Agrobacterium tumefaciens the ispD and ispF genes are fused to encode a bifunctional enzyme that catalyzes the first (synthesis of 4-diphosphocytidyl-2-C-methyl D-erythritol) and third (synthesis of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate) steps of isoprenoid biosynthetic pathway. Enzyme-generated intermediates are not transferred from the IspD active site in IspDF to the active site of IspE or from the active site in IspE to the active site of the IspF module of IspDF
-
-
?
additional information
?
-
no conversion of isopentenyl phosphate into isopentenyl diphosphate
-
-
?
additional information
?
-
-
no conversion of isopentenyl phosphate into isopentenyl diphosphate
-
-
?
additional information
?
-
-
no activity with 4-(adenine 5'-phosphate)-2-C-methyl-D-erythritol and 4-(uridine 5'-phosphate)-2-C-methyl-D-erythritol
-
-
?
additional information
?
-
-
no activity with 4-(adenine 5'-phosphate)-2-C-methyl-D-erythritol and 4-(uridine 5'-phosphate)-2-C-methyl-D-erythritol
-
-
?
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4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol + ATP
2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol + ADP
-
-
-
ir
4-diphosphocytidyl-2C-methyl-D-erythritol + ATP
4-diphosphocytidyl-2C-methyl-D-erythritol 2-phosphate + ADP
non-mevalonate pathway of isoprenoid precursor synthesis
-
-
ir
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
additional information
?
-
-
in Agrobacterium tumefaciens the ispD and ispF genes are fused to encode a bifunctional enzyme that catalyzes the first (synthesis of 4-diphosphocytidyl-2-C-methyl D-erythritol) and third (synthesis of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate) steps of isoprenoid biosynthetic pathway. Enzyme-generated intermediates are not transferred from the IspD active site in IspDF to the active site of IspE or from the active site in IspE to the active site of the IspF module of IspDF
-
-
?
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
-
?
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
fourth reaction step of the 2-C-methyl-D-erythritol 4-phosphate pathway
-
-
?
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
the enzyme is essential in the nonmevalonate pathway of isopentenyl diphosphate and dimethylallyl diphosphate biosynthesis
-
-
?
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
non-mevalonate pathway for isoprenoid biosynthesis
-
-
?
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
involved in terpenoid biosynthesis via deoxyxylulose phosphate pathway
-
-
?
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
the enzyme is essential in the nonmevalonate pathway of isopentenyl diphosphate and dimethylallyl diphosphate biosynthesis, pathway overview
-
-
?
ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
the enzyme is essential in the nonmevalonate pathway of isopentenyl diphosphate and dimethylallyl diphosphate biosynthesis, pathway overview
-
-
?
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(4E)-3-methyl-4-[(5-phenylfuran-2-yl)methylidene]-1,2-oxazol-5(4H)-one
(4Z)-4-(furan-2-ylmethylidene)-3-phenyl-1,2-oxazol-5(4H)-one
(4Z)-4-[(5-methylfuran-2-yl)methylidene]-3-phenyl-1,2-oxazol-5(4H)-one
6-(benzylsulfanyl)-2-(2-hydroxyphenyl)-4-oxo-3,4-dihydro-2H-1,3-thiazine-5-carbonitrile
ethyl [4-amino-2-oxo-5-(3-[[(2,2,2-trifluoroethyl)sulfonyl]amino]prop-1-en-1-yl)pyrimidin-1(2H)-yl]acetate
-
mixed type
N-[3-(4-amino-1-benzyl-2-oxo-1,2-dihydropyrimidin-5-yl)prop-2-en-1-yl]ethanesulfonamide
-
mixed-type
N-[3-[4-amino-2-oxo-1-(1H-pyrazol-5-ylmethyl)-1,2-dihydropyrimidin-5-yl]prop-2-en-1-yl]ethanesulfonamide
-
competitive
N-[3-[4-amino-2-oxo-1-(tetrahydro-2-thienyl)-1,2-dihydropyrimidin-5-yl]prop-2-en-1-yl]-1,1,1-trifluoromethanesulfonamide
-
competitive
N-[3-[4-amino-2-oxo-1-(tetrahydro-2-thienyl)-1,2-dihydropyrimidin-5-yl]prop-2-en-1-yl]-2,2,2-trifluoroethanesulfonamide
-
competitive
N-[3-[4-amino-2-oxo-1-(tetrahydro-2-thienyl)-1,2-dihydropyrimidin-5-yl]prop-2-en-1-yl]benzenesulfonamide
-
competitive
N-[3-[4-amino-2-oxo-1-(tetrahydro-2-thienyl)-1,2-dihydropyrimidin-5-yl]prop-2-en-1-yl]cyclopropanesulfonamide
-
competitive
N-[3-[4-amino-2-oxo-1-(tetrahydro-2-thienyl)-1,2-dihydropyrimidin-5-yl]prop-2-en-1-yl]ethanesulfonamide
-
competitive
N-[3-[4-amino-2-oxo-1-(tetrahydro-2-thienyl)-1,2-dihydropyrimidin-5-yl]prop-2-en-1-yl]methanesulfonamide
-
competitive
N-[3-[4-amino-2-oxo-1-(tetrahydro-2-thienyl)-1,2-dihydropyrimidin-5-yl]prop-2-en-1-yl]propane-1-sulfonamide
-
mixed-type
N-[3-[4-amino-2-oxo-1-(tetrahydrofuran-2-ylmethyl)-1,2-dihydropyrimidin-5-yl]prop-2-en-1-yl]-2,2,2-trifluoroethanesulfonamide
-
competitive
(4E)-3-methyl-4-[(5-phenylfuran-2-yl)methylidene]-1,2-oxazol-5(4H)-one
-
-
(4E)-3-methyl-4-[(5-phenylfuran-2-yl)methylidene]-1,2-oxazol-5(4H)-one
-
-
(4Z)-4-(furan-2-ylmethylidene)-3-phenyl-1,2-oxazol-5(4H)-one
-
-
(4Z)-4-(furan-2-ylmethylidene)-3-phenyl-1,2-oxazol-5(4H)-one
-
-
(4Z)-4-[(5-methylfuran-2-yl)methylidene]-3-phenyl-1,2-oxazol-5(4H)-one
-
-
(4Z)-4-[(5-methylfuran-2-yl)methylidene]-3-phenyl-1,2-oxazol-5(4H)-one
-
-
6-(benzylsulfanyl)-2-(2-hydroxyphenyl)-4-oxo-3,4-dihydro-2H-1,3-thiazine-5-carbonitrile
-
at an external concentration of 50 microM, compound is able to inhibit the growth of Escherichia coli in culture for at least six hours
6-(benzylsulfanyl)-2-(2-hydroxyphenyl)-4-oxo-3,4-dihydro-2H-1,3-thiazine-5-carbonitrile
-
-
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0.0042
ethyl [4-amino-2-oxo-5-(3-[[(2,2,2-trifluoroethyl)sulfonyl]amino]prop-1-en-1-yl)pyrimidin-1(2H)-yl]acetate
-
competitive inhibition constant
0.0037
N-[3-(4-amino-1-benzyl-2-oxo-1,2-dihydropyrimidin-5-yl)prop-2-en-1-yl]ethanesulfonamide
-
competitive inhibition constant
0.0016
N-[3-[4-amino-2-oxo-1-(1H-pyrazol-5-ylmethyl)-1,2-dihydropyrimidin-5-yl]prop-2-en-1-yl]ethanesulfonamide
-
competitive inhibition constant
0.0012
N-[3-[4-amino-2-oxo-1-(tetrahydro-2-thienyl)-1,2-dihydropyrimidin-5-yl]prop-2-en-1-yl]-1,1,1-trifluoromethanesulfonamide
-
competitive inhibition constant
0.00036
N-[3-[4-amino-2-oxo-1-(tetrahydro-2-thienyl)-1,2-dihydropyrimidin-5-yl]prop-2-en-1-yl]-2,2,2-trifluoroethanesulfonamide
-
competitive inhibition constant
0.0163
N-[3-[4-amino-2-oxo-1-(tetrahydro-2-thienyl)-1,2-dihydropyrimidin-5-yl]prop-2-en-1-yl]benzenesulfonamide
-
competitive inhibition constant
0.00029
N-[3-[4-amino-2-oxo-1-(tetrahydro-2-thienyl)-1,2-dihydropyrimidin-5-yl]prop-2-en-1-yl]cyclopropanesulfonamide
-
competitive inhibition constant
0.00064
N-[3-[4-amino-2-oxo-1-(tetrahydro-2-thienyl)-1,2-dihydropyrimidin-5-yl]prop-2-en-1-yl]ethanesulfonamide
-
competitive inhibition constant
0.0026
N-[3-[4-amino-2-oxo-1-(tetrahydro-2-thienyl)-1,2-dihydropyrimidin-5-yl]prop-2-en-1-yl]methanesulfonamide
-
competitive inhibition constant
0.0082
N-[3-[4-amino-2-oxo-1-(tetrahydro-2-thienyl)-1,2-dihydropyrimidin-5-yl]prop-2-en-1-yl]propane-1-sulfonamide
-
competitive inhibition constant
0.0323
N-[3-[4-amino-2-oxo-1-(tetrahydrofuran-2-ylmethyl)-1,2-dihydropyrimidin-5-yl]prop-2-en-1-yl]-2,2,2-trifluoroethanesulfonamide
-
competitive inhibition constant
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0055 - 0.006
(4E)-3-methyl-4-[(5-phenylfuran-2-yl)methylidene]-1,2-oxazol-5(4H)-one
0.007 - 0.012
(4Z)-4-(furan-2-ylmethylidene)-3-phenyl-1,2-oxazol-5(4H)-one
0.008 - 0.013
(4Z)-4-[(5-methylfuran-2-yl)methylidene]-3-phenyl-1,2-oxazol-5(4H)-one
0.009 - 0.018
6-(benzylsulfanyl)-2-(2-hydroxyphenyl)-4-oxo-3,4-dihydro-2H-1,3-thiazine-5-carbonitrile
0.0055
(4E)-3-methyl-4-[(5-phenylfuran-2-yl)methylidene]-1,2-oxazol-5(4H)-one
Escherichia coli
-
pH not specified in the publication, 22°C
0.006
(4E)-3-methyl-4-[(5-phenylfuran-2-yl)methylidene]-1,2-oxazol-5(4H)-one
Yersinia pestis
-
pH not specified in the publication, 22°C
0.007
(4Z)-4-(furan-2-ylmethylidene)-3-phenyl-1,2-oxazol-5(4H)-one
Escherichia coli
-
pH not specified in the publication, 22°C
0.012
(4Z)-4-(furan-2-ylmethylidene)-3-phenyl-1,2-oxazol-5(4H)-one
Yersinia pestis
-
pH not specified in the publication, 22°C
0.008
(4Z)-4-[(5-methylfuran-2-yl)methylidene]-3-phenyl-1,2-oxazol-5(4H)-one
Escherichia coli
-
pH not specified in the publication, 22°C
0.013
(4Z)-4-[(5-methylfuran-2-yl)methylidene]-3-phenyl-1,2-oxazol-5(4H)-one
Yersinia pestis
-
pH not specified in the publication, 22°C
0.009
6-(benzylsulfanyl)-2-(2-hydroxyphenyl)-4-oxo-3,4-dihydro-2H-1,3-thiazine-5-carbonitrile
Yersinia pestis
-
pH not specified in the publication, 22°C
0.018
6-(benzylsulfanyl)-2-(2-hydroxyphenyl)-4-oxo-3,4-dihydro-2H-1,3-thiazine-5-carbonitrile
Escherichia coli
-
pH not specified in the publication, 22°C
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metabolism
-
enzyme catalyses the fourth reaction step of the 2C-methylerythritol 4-phosphate (MEP) pathway for the biosynthesis of isopentenyl pyrophosphate and its isomer dimethylallyl pyrophosphate
metabolism
-
key enzyme in the biosynthesis pathway of terpenoids
metabolism
CDPME kinase (IspE) catalyzes the phosphorylation of CDPME to 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDPME2P) as part of the MEP pathway, overview. In Bacillus subtilis, no stable complexes of BsIspD/BsIspE, BsIspD/BsIspF, and BsIspD/BsIspE/BsIspF are observed, interaction analysis, overview
metabolism
CDPME kinase (IspE) catalyzes the phosphorylation of CDPME to 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDPME2P) as part of the MEP pathway, overview. In Escherichia coli, no stable complexes of EcIspD/EcIspE, EcIspE/EcIspF, and EcIspD/EcIspE/EcIspF are observed, only the dual mixture of BsIspE and BsIspF seems to merge into a single band, interaction analysis, overview
metabolism
the enzyme 4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase is the fourth enzyme in the methyl erythritol phosphate pathway (MEP pathway) of plant terpenoid biosynthesis
metabolism
-
CDPME kinase (IspE) catalyzes the phosphorylation of CDPME to 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDPME2P) as part of the MEP pathway, overview. In Bacillus subtilis, no stable complexes of BsIspD/BsIspE, BsIspD/BsIspF, and BsIspD/BsIspE/BsIspF are observed, interaction analysis, overview
-
metabolism
-
CDPME kinase (IspE) catalyzes the phosphorylation of CDPME to 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDPME2P) as part of the MEP pathway, overview. In Bacillus subtilis, no stable complexes of BsIspD/BsIspE, BsIspD/BsIspF, and BsIspD/BsIspE/BsIspF are observed, interaction analysis, overview
-
physiological function
-
the MEP pathway is essential in the malaria parasite Plasmodium falciparum and in most eubacteria, including the causal agents for diverse and serious human diseases like leprosy, bacterial meningitis, various gastrointestinal and sexually transmitted infections, tuberculosis, and certain types of pneumonia
physiological function
Vitis vinifera x Vitis vinifera
-
involved in terpenoid metabolism
physiological function
-
involved in terpenoid metabolism
physiological function
CDPME kinase (IspE) catalyzes the phosphorylation of CDPME to 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDPME2P)
physiological function
CDPME kinase (IspE) catalyzes the phosphorylation of CDPME to 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDPME2P)
physiological function
-
CDPME kinase (IspE) catalyzes the phosphorylation of CDPME to 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDPME2P)
-
physiological function
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CDPME kinase (IspE) catalyzes the phosphorylation of CDPME to 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDPME2P)
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additional information
three-dimensional structure and active site structure predictions. The active site of PvIspE consists of total 32 amino acid residues, 16 amino acid residues involved in ATP binding (Y225, P226, D230, N231, I232, K258, I262, F263, S264, G265, G267, G268, G269, N272, D304, S349) and 16 amino acid residues interacts with the substrate CDM (K136, N138, L141, H150, N151, M157, S270, G302, S303, D304, K319, S349, R350, Y353, L413, G444)
additional information
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three-dimensional structure and active site structure predictions. The active site of PvIspE consists of total 32 amino acid residues, 16 amino acid residues involved in ATP binding (Y225, P226, D230, N231, I232, K258, I262, F263, S264, G265, G267, G268, G269, N272, D304, S349) and 16 amino acid residues interacts with the substrate CDM (K136, N138, L141, H150, N151, M157, S270, G302, S303, D304, K319, S349, R350, Y353, L413, G444)
additional information
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three-dimensional structure and active site structure predictions. The active site of PvIspE consists of total 32 amino acid residues, 16 amino acid residues involved in ATP binding (Y225, P226, D230, N231, I232, K258, I262, F263, S264, G265, G267, G268, G269, N272, D304, S349) and 16 amino acid residues interacts with the substrate CDM (K136, N138, L141, H150, N151, M157, S270, G302, S303, D304, K319, S349, R350, Y353, L413, G444)
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AaIspE is crystallized by vapor diffusion. Ordered and reproducible crystals of AaIspE are obtained and multiple-wavelength anomalous dispersion methods are applied to obtain the initial phases. 3 medium-resolution complex crystal structures are determined. The crystals are isomorphous with two molecules in the asymmetric unit.
in complex with ADP, to 2.0 A resolution, and comparison with a monoclinic crystal form of a ternary complex of Escherichia coli 4-diphosphocytidyl-2C-methyl-D-erythritol kinase also with two molecules in the asymmetric unit. The molecular packing is different in the two forms. In the asymmetric unit of the triclinic crystal form the substrate-binding sites are occluded by structural elements of the partner, suggesting that the triclinic dimer is an artefact of the crystal lattice. The surface area of interaction in the triclinic form is almost double that observed in the monoclinic form
purified recombinant enzyme in ternary complex with substrate and non-hydrolyzable ATP analogue adenosine 5'-[beta,gamma-imino]triphosphate, i.e. AMP-PNP, 25 mg/ml protein in 50 mM Tris-HCl, pH 7.7, 50 mM NaCl, 3 mM AMP-PNP, and 2 mM substrate 4-(cytidine 5'-phosphate)-2-C-methyl-D-erythritol, hanging drop vapour diffusion method, 0.001 ml protein solution mixed with equal volume of reservoir solution containing 20% polyethylene glycol 8000, 0.2 M magnesium acetate, 0.1 M sodium cacodylate, pH 6.5, and 0.0002 ml of 0.25 sulfo-betaine, cryoprotection at -173°C by 20% glycerol, X-ray diffraction structure determination and analysis at 2.0 A resolution
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structure-activity relationship studies with inhibitors 6-(benzylsulfanyl)-2-(2-hydroxyphenyl)-4-oxo-3,4-dihydro-2H-1,3-thiazine-5-carbonitrile and (4E)-3-methyl-4-[(5-phenylfuran-2-yl)methylidene]-1,2-oxazol-5(4H)-one
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the structure is resolved by X-ray diffraction at a resolution of 2.01 A
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free enzyme, in complex with substrates 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol, ADP and with adenyl imidodiphosphate, to 1.0, 1.54, 1.0, and 1.0 A resolution, respectively. The structures present a characteristic galactose/homoserine/mevalonate/phosphomevalonate kinase superfamily alpha/beta-fold with a catalytic center located in a cleft between two domains and display clear substrate and ATP binding pockets
purified recombinant selenomethionine-labeled enzyme, hanging drop vapour diffusion method, 20°C, 0.002 ml protein solution containing 2.2 mg/ml protein, 20 ml Tris-HCl, pH 8.0, and 50 mM NaCl, are mixed with 0.001 ml mother liquor containing 33 mM Tris-HCl, pH 8.5, 67 mM sodium acetate, 13% isopropanol, 8% butanol, and 13% PEG 4000, cryoprotection at -173°C in 30% glycerol, X-ray diffraction structure determination and analysis at 1.7 A resolution
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structure-activity relationship studies with inhibitors 6-(benzylsulfanyl)-2-(2-hydroxyphenyl)-4-oxo-3,4-dihydro-2H-1,3-thiazine-5-carbonitrile and (4E)-3-methyl-4-[(5-phenylfuran-2-yl)methylidene]-1,2-oxazol-5(4H)-one
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D152A
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inactive mutant enzyme
A382T
naturally occuring mutation, neutral
G402R
naturally occuring mutation, neutral
K492T
naturally occuring mutation, neutral
L405Q
naturally occuring mutation, neutral
R336S
naturally occuring mutation, neutral
T351M
naturally occuring mutation, neutral
A382T
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naturally occuring mutation, neutral
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G402R
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naturally occuring mutation, neutral
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K492T
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naturally occuring mutation, neutral
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T351M
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naturally occuring mutation, neutral
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additional information
two non-synonymous mutations at codons 382 (A->T) and 492 (K->T) are found in all the isolates of Delhi, Chennai, Nadiad, Sonapur Goa, and Mangaluru. Apart from these, two more mutations are observed in all the isolates of Goa and Mangaluru namely one substitution at codon 351(T->M) and another synonymous mutation at codon 344 (S) TCT->TCC. In Rourkela which is one of the highly malaria endemic and isolated tribal regions of India, four non-synonymous mutations at codons 336 (R->S), 351 (T->M), 402 (G->R) and 405 (L->Q) are detected in all isolates. Domain architecture and mutation mapping, overview
additional information
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two non-synonymous mutations at codons 382 (A->T) and 492 (K->T) are found in all the isolates of Delhi, Chennai, Nadiad, Sonapur Goa, and Mangaluru. Apart from these, two more mutations are observed in all the isolates of Goa and Mangaluru namely one substitution at codon 351(T->M) and another synonymous mutation at codon 344 (S) TCT->TCC. In Rourkela which is one of the highly malaria endemic and isolated tribal regions of India, four non-synonymous mutations at codons 336 (R->S), 351 (T->M), 402 (G->R) and 405 (L->Q) are detected in all isolates. Domain architecture and mutation mapping, overview
additional information
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two non-synonymous mutations at codons 382 (A->T) and 492 (K->T) are found in all the isolates of Delhi, Chennai, Nadiad, Sonapur Goa, and Mangaluru. Apart from these, two more mutations are observed in all the isolates of Goa and Mangaluru namely one substitution at codon 351(T->M) and another synonymous mutation at codon 344 (S) TCT->TCC. In Rourkela which is one of the highly malaria endemic and isolated tribal regions of India, four non-synonymous mutations at codons 336 (R->S), 351 (T->M), 402 (G->R) and 405 (L->Q) are detected in all isolates. Domain architecture and mutation mapping, overview
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Rohdich, F.; Wungsintaweekul, J.; Luttgen, H.; Fischer, M.; Eisenreich, W.; Schuhr, C.A.; Fellermeier, M.; Schramek, N.; Zenk, M.H.; Bacher, A.
Biosynthesis of terpenoids: 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase from tomato
Proc. Natl. Acad. Sci. USA
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Solanum lycopersicum (P93841), Solanum lycopersicum
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Kuzuyama, T.; Takagi, M.; Kaneda, K.; Watanabe, H.; Dairi, T.; Seto, H.
Studies on the nonmevalonate pathway: conversion of 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol to its 2-phospho derivative by 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase
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Escherichia coli
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Escherichia coli
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Crystal structure of 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase, an enzyme in the non-mevalonate pathway of isoprenoid synthesis
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Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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Biosynthesis of isoprenoids: crystal structure of 4-diphosphocytidyl-2C-methyl-D-erythritol kinase
Proc. Natl. Acad. Sci. USA
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9173-9178
2003
Escherichia coli
brenda
Lherbet, C.; Pojer, F.; Richard, S.B.; Noel, J.P.; Poulter, C.D.
Absence of substrate channeling between active sites in the Agrobacterium tumefaciens IspDF and IspE enzymes of the methyl erythritol phosphate pathway
Biochemistry
45
3548-3553
2006
Agrobacterium tumefaciens
brenda
Hirsch, A.K.; Lauw, S.; Gersbach, P.; Schweizer, W.B.; Rohdich, F.; Eisenreich, W.; Bacher, A.; Diederich, F.
Nonphosphate inhibitors of IspE protein, a kinase in the non-mevalonate pathway for isoprenoid biosynthesis and a potential target for antimalarial therapy
ChemMedChem
2
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2007
Escherichia coli
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Aquifex aeolicus (O67060), Aquifex aeolicus
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Two copies of 4-(cytidine 5-diphospho)-2-C-methyl-D: -erythritol kinase (CMK) gene in Ginkgo biloba: molecular cloning and functional characterization
Planta
228
941-950
2008
Ginkgo biloba (A6XAA8), Ginkgo biloba (A6XAA9), Ginkgo biloba
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Mimicking direct protein-protein and solvent-mediated interactions in the CDP-methylerythritol kinase homodimer: a pharmacophore-directed virtual screening approach
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2009
Escherichia coli
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Vitis vinifera x Vitis vinifera, Vitis vinifera x Vitis riparia
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A triclinic crystal form of Escherichia coli 4-diphosphocytidyl-2C-methyl-D-erythritol kinase and reassessment of the quaternary structure
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2010
Escherichia coli (P62615), Escherichia coli
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Identification of novel small molecule inhibitors of 4-diphosphocytidyl-2-C-methyl-D-erythritol (CDP-ME) kinase of Gram-negative bacteria
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Escherichia coli, Yersinia pestis, Escherichia coli DH5-alpha
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Crystal structure of 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (IspE) from Mycobacterium tuberculosis
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Mycobacterium tuberculosis (P9WKG7), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WKG7)
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Cloning and expression analysis of 4-(cytidine-5-diphospho)-2-C-methyl-D-erythritol kinase gene in Tripterygium wilfordii
Zhongguo Zhong Yao Za Zhi
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Tripterygium wilfordii
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Crystal structure of IspF from Bacillus subtilis and absence of protein complex assembly amongst IspD/IspE/IspF enzymes in the MEP pathway
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Structural modeling identifies Plasmodium vivax 4-diphosphocytidyl-2C-methyl-d-erythritol kinase (IspE) as a plausible new antimalarial drug target
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Plasmodium vivax (A5KAU8), Plasmodium vivax, Plasmodium vivax Salvador I (A5KAU8)
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Cloning and expression analysis of 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase gene in cc
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Cinnamomum camphora (A0A1J0I9Y0)
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