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2-C-methyl-D-erythritol 4-phosphate + ATP
diphosphate + 4-(adenine 5'-diphospho)-2-C-methyl-D-erythritol
2-C-methyl-D-erythritol 4-phosphate + CTP
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
dCTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(deoxycytidine 5'-diphospho)-2-C-methyl-D-erythritol
additional information
?
-
2-C-methyl-D-erythritol 4-phosphate + ATP
diphosphate + 4-(adenine 5'-diphospho)-2-C-methyl-D-erythritol
-
13% activity compared to CTP as substrate, 30°C, 15 min, pH8
-
-
?
2-C-methyl-D-erythritol 4-phosphate + ATP
diphosphate + 4-(adenine 5'-diphospho)-2-C-methyl-D-erythritol
-
13% activity compared to CTP as substrate, 30°C, 15 min, pH8
-
-
?
2-C-methyl-D-erythritol 4-phosphate + CTP
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
30°C, 15 min, pH8
coupled to hydrolysis of diphosphate to phosphate followed by complex formation with ammonium molybdate-malachite green (absorbance at 630 nm)
-
?
2-C-methyl-D-erythritol 4-phosphate + CTP
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
30°C, 15 min, pH8
coupled to hydrolysis of diphosphate to phosphate followed by complex formation with ammonium molybdate-malachite green (absorbance at 630 nm)
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
essential enzyme in the mevalonate-independent pathway of isoprenoid biosynthesis
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
ATP, UTP, GTP, ITP, dTTP, dGTP, dCTP ann dATP tested as substrates besides CTP
-
r
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
essential enzyme in the mevalonate-independent pathway of isoprenoid biosynthesis
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
r
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
essential enzyme in he mevalonate-independent pathway of isoprenoid biosynthesis
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
essential enzyme in the mevalonate-independent pathway of isoprenoid biosynthesis
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
essential enzyme in the mevalonate-independent pathway of isoprenoid biosynthesis
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
Francisella tularensis subsp. novicida Utah 112
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
Plasmodium falciparum Tanzania (20000708)
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
intermediate in the deoxyxylulose pathway of isoprenoid biosynthesis
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
third step of biosynthesis
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
third step of biosynthesis
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
part of mevalonate-indpendent pathway for isoprenoid biosynthesis
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
part of mevalonate-indpendent pathway for isoprenoid biosynthesis
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
part of mevalonate-indpendent pathway for isoprenoid biosynthesis
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
part of mevalonate-indpendent pathway for isoprenoid biosynthesis
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
intermediate in the deoxyxylulose pathway of isoprenoid biosynthesis
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
part of mevalonate-indpendent pathway for isoprenoid biosynthesis
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
part of mevalonate-indpendent pathway for isoprenoid biosynthesis
-
?
dCTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(deoxycytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
dCTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(deoxycytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
additional information
?
-
-
lipoate-protein ligase attaches octanoate to the dehydrogenase subunit and sulfur insertion protein LipA then converts octanoate to lipoate. LipA acts on both octanoate and octanoyl-proteins
-
-
?
additional information
?
-
-
using an assay method for determination of the catalytic activity measuring the production of radiolabeled 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol from 14C-labeled 2-C-methyl-D-erythritol 4-phosphate, and separation of non-radioactive 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol from CTP by C18 reverse phase HPLC with a mobile phase of 0.1 M ammonium bicarbonate (98%) and acetonitrile (2%) at pH 7.4
-
-
?
additional information
?
-
-
monofunctional enzyme
-
-
?
additional information
?
-
-
GTP, UTP and ITP are no substrates
-
-
?
additional information
?
-
-
monofunctional enzyme
-
-
?
additional information
?
-
-
GTP, UTP and ITP are no substrates
-
-
?
additional information
?
-
substrate molecular docking study, binding site mapping and analysis
-
-
-
additional information
?
-
the fluorimetric assay directly measures diphosphate
-
-
-
additional information
?
-
Plasmodium falciparum Tanzania (20000708)
substrate molecular docking study, binding site mapping and analysis
-
-
-
additional information
?
-
the PvIspD enzyme is highly specific for CTP, 20% of the activity with CTP is shown with dCTP, and below 10% activity with ATP, dATP, dGTP, and dTTP
-
-
-
additional information
?
-
-
the PvIspD enzyme is highly specific for CTP, 20% of the activity with CTP is shown with dCTP, and below 10% activity with ATP, dATP, dGTP, and dTTP
-
-
-
additional information
?
-
the PvIspD enzyme is highly specific for CTP, 20% of the activity with CTP is shown with dCTP, and below 10% activity with ATP, dATP, dGTP, and dTTP
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
essential enzyme in the mevalonate-independent pathway of isoprenoid biosynthesis
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
essential enzyme in the mevalonate-independent pathway of isoprenoid biosynthesis
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
essential enzyme in he mevalonate-independent pathway of isoprenoid biosynthesis
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
essential enzyme in the mevalonate-independent pathway of isoprenoid biosynthesis
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
essential enzyme in the mevalonate-independent pathway of isoprenoid biosynthesis
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
Francisella tularensis subsp. novicida Utah 112
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
Plasmodium falciparum Tanzania (20000708)
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
-
?
CTP + 2-C-methyl-D-erythritol 4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
intermediate in the deoxyxylulose pathway of isoprenoid biosynthesis
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
third step of biosynthesis
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
third step of biosynthesis
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
part of mevalonate-indpendent pathway for isoprenoid biosynthesis
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
part of mevalonate-indpendent pathway for isoprenoid biosynthesis
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
part of mevalonate-indpendent pathway for isoprenoid biosynthesis
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
part of mevalonate-indpendent pathway for isoprenoid biosynthesis
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
intermediate in the deoxyxylulose pathway of isoprenoid biosynthesis
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
part of mevalonate-indpendent pathway for isoprenoid biosynthesis
-
?
CTP + 2-C-methyl-D-erythritol-4-phosphate
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
part of mevalonate-indpendent pathway for isoprenoid biosynthesis
-
?
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.
(1R,3S)-1-(2,3,4-trifluorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(2,4-dibromophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(2,4-dichlorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxamide
-
(1R,3S)-1-(2,4-dichlorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(2,4-dichlorophenyl)-N,N-dimethyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxamide
about 5% inhibition at 0.001 mM
(1R,3S)-1-(2,4-dichlorophenyl)-N-ethyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxamide
-
(1R,3S)-1-(2,4-dichlorophenyl)-N-methyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxamide
-
(1R,3S)-1-(2,4-difluorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(2-bromo-4,5-difluorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(2-bromo-4-chlorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(2-bromo-4-chlorophenyl)-N-methyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxamide
-
(1R,3S)-1-(2-bromo-4-iodophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(2-chloro-4-fluorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(2-chloro-4-fluorophenyl)-N-methyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxamide
-
(1R,3S)-1-(2-chloro-4-hydroxyphenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(2-chloro-4-methoxyphenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(2-chloro-4-methylphenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(2-chloro-4-methylphenyl)-N-methyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxamide
-
(1R,3S)-1-(2-chlorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(2-fluoro-4-iodophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(3,4-dimethoxyphenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(3-chloropyridin-4-yl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(4-bromo-2-chlorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(4-bromo-2-chlorophenyl)-N-methyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxamide
-
(1R,3S)-1-(4-carboxy-2-chlorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(4-chloro-2,6-difluorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(4-chloro-2-fluorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(4-chloro-2-methoxyphenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(4-chloro-2-methylphenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(4-chlorophenyl)-1-methyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(4-chlorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-(4-fluoro-2-iodophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-methyl-1-phenyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-phenyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-[(2,4-dichlorophenyl)methyl]-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-[2,4-bis(dimethoxymethyl)phenyl]-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-[2,4-bis(trifluoromethyl)phenyl]-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-1-[2,4-di(propan-2-yl)phenyl]-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(1R,3S)-MMV008138
(1R,3S)-MMV008138 targets the enzyme 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (IspD) in the MEP pathway. The Malaria Box compound MMV008138 targets the apicoplast and that parasite growth inhibition by this compound can be reversed by supplementation of IPP. The compound inhibits Plasmodium falciparum Dd2 strain growth with an IC50 value of 250 nM
-
(1S,3S)-1-(5-chlorothiophen-2-yl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
-
(2,4-dichloro-phenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indol-2-ium-3-carboxylate
-
(3-(acetylhydroxyamino)propyl)phosphonic acid
FR900098
-
1-(2,4-dichlorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole
about 7% inhibition at 0.001 mM
1-[(1R,3S)-1-(2,4-dichlorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indol-3-yl]-2-hydroxyethan-1-one
-
1H-pyrrolo(2,3-b)quinoxaline
-
-
7-hydroxy-[1,2,4] triazolo[1,5-a] pyrimidine
azolopyrimidine, docking reveals strong hydrogen bonds with CTP-specific (T326, K406, R431, and K548) and MEP-specific (D428, R431, T525, and K548) amino acid residues of PvIspD protein. A salt-bridge formation is also observed with K406 and D428 residues similar to CTP
-
9H-pyrrolo[2,3f]quinoxaline
-
-
aurintricarboxylic acid
-
cefepime
interaction with residues T525 and K548
D-erythritol 1-phosphate
-
domiphen bromide
interaction with residue Thr 525
-
methyl hydroxytriazaindolizine
-
-
prop-2-yn-1-yl trihydrogen diphosphate
schembl1651692
propyl trihydrogen diphosphate
-
-
pyrrolo[1,2-a]quinoxaline
-
-
quercetin
quercetin is retained as a lead molecule for inhibition of IspD, 96% inhibition at 0.1 mM
rifampicin
a prokaryotic transcription inhibitor, interaction with residues T326, R431, T525, and K548
rosuvastatin
RST, significantly interacts at the active site of the enzyme. Active-site residues Gly16, Arg83, Thr84, and Thy190 are potentially contributing to the protein-ligand interaction
triazolopyrimidine derivative
PubChem CID 330031
-
tunicamycin
interaction with residues V323, T324, T326, D338, L381, L384, K406, and T491
(2,4-dichloro-phenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indol-2-ium-3-carboxylate
MMV008138, PfIspD is the sole intracellular target of MMV008138, target-based resistance. IspD binding mode analysis, overview. 1R,3S-MMV008138 directly inhibits purified recombinant Plasmodium falciparum IspD (PfIspD), competitively with its CTP substrate. The metabolic effects of 1R,3S-MMV008138 are specific to MEP pathway inhibition, 1R,3S-MMV008138 inhibits malaria parasite growth as a consequence of MEP pathway inhibition. 1R,3S-MMV008138 is also active against Plasmodium vivax but not against bacterial IspD homologues
-
(2,4-dichloro-phenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indol-2-ium-3-carboxylate
MMV008138, Plasmodium vivax IspD (PvIspD) is potently inhibited by 1R,3S-MMV008138. IspD binding mode analysis, overview
-
fosmidomycin
-
fosmidomycin
about 4% inhibition at 0.01 mM
fosmidomycin
3-[formyl(hydroxy)amino]propylphosphonic acid
fosmidomycin
Fos, a well-known inhibitor of DXR/IspC enzyme. Strong interaction of Fos with PvIspD enzyme, where hydrogen bonds are observed between Fos and amino acid residues D428, R431, Q493, T523, D524, T525 and K548 of PvIspD enzyme. residues R431 and K548 which form the salt bridge with CTP are observed to form a bridge with the negatively charged phosphate group of Fos
MMV008138
-
-
MMV008138
weak inhibition of Plasmodium vivax IspD, the compound is a competitive inhibitor of PvIspD at lower concentrations of CTP, interaction with residues D428, T525, and K548
-
additional information
high-throughput screening to identify inhibitors of MEP cytidylyltransferase (IspD)
-
additional information
bench-scale high-throughput screening to identify inhibitors of MEP cytidylyltransferase (IspD) using purified, recombinant IspD, a commercially available 1280 compound molecular library, and a 150 sample, in-house prepared, natural product extract library. The enzyme activity is not affected by 0.01% Triton X-100, but inhibition is attenuated in the presence of Triton X-100 for all inhibitors, except 6-hydroxy-DL-DOPA
-
additional information
no inhibition of Mycobacetrium tuberculosis IspD by (2,4-dichloro-phenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indol-2-ium-3-carboxylate, MMV008138
-
additional information
inhibitor screening and enzyme-inhibitor molecular docking study using enzyme structure with bound CTP and Mg2+ (PDB ID 3Q7U). The attached CTP and Mg2+ ion are deleted from the structure, followed by refinement of the protein subunit. The crucial active site residues Gly16, Arg83, Thr84, and Thy190 play a vital role in the protein-ligand stabilization process
-
additional information
the PfISPD genetic locus is refractory to disruption in malaria parasites, providing independent genetic validation for efforts targeting this enzyme. Phosphonic acid antibiotic fosmidomycin is a substrate mimic and inhibitor of DXR.13 The inhibition of downstream enzyme IspD is also metabolically apparent in fosmidomycin-treated cells, although IspD homologues are not directly inhibited by fosmidomycin in vitro
-
additional information
-
the PfISPD genetic locus is refractory to disruption in malaria parasites, providing independent genetic validation for efforts targeting this enzyme. Phosphonic acid antibiotic fosmidomycin is a substrate mimic and inhibitor of DXR.13 The inhibition of downstream enzyme IspD is also metabolically apparent in fosmidomycin-treated cells, although IspD homologues are not directly inhibited by fosmidomycin in vitro
-
additional information
inhibitor design and inhibition structure-activity relationships analysis, overview. In addition to (1R,3S)-configuration, potent growth inhibition requires 2',4'-disubstitution of the D-ring, featuring at least one electron-withdrawing substituent. Neither (1R,3S)-1-phenyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid (bearing an unsubstituted phenyl ring) nor (1R,3S)-1-[2,4-di(propan-2-yl)phenyl]-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid (bearing 2',4'-dimethyl substitution) inhibit Plasmodium falciparum growth at 0.01 mM. The 2'-chloro substituted analogue (1R,3S)-1-(2-chlorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid shows weak growth inhibition, and (1R,3S)-1-(2-chloro-4-methylphenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid (2'-chloro-4'-methyl substituted) nearly recapitulates the potency of (1R,3S)-MMV008138. The carboxy substituent at C3 of the C-ring also proves to be essential, replacement with CO2Me (3a) or H (11a) abrogates growth inhibition potency. But weak growth inhibition is restored with the first amide analogue (1R,3S)-1-(2,4-dichlorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxamide, and methyl amide derivative (1R,3S)-1-(2,4-dichlorophenyl)-N-methyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxamide proves equipotent to (1R,3S)-MMV008138. Not inhibitory: (1R,3S)-1-(3,4-dichlorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid, methyl (1R,3S)-1-(2,4-dichlorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylate.
-
additional information
inhibitor molecular docking study
-
additional information
docking study
-
additional information
-
docking study
-
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0.012 - 131.5
2-C-methyl-D-erythritol 4-phosphate
0.00314 - 3.26
2-C-methyl-D-erythritol-4-phosphate
0.131 - 0.5
4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
additional information
additional information
-
0.012
2-C-methyl-D-erythritol 4-phosphate
pH 7.4, 37°C
0.02513
2-C-methyl-D-erythritol 4-phosphate
pH 7.9, 37°C, recombinant enzyme
0.043
2-C-methyl-D-erythritol 4-phosphate
-
-
0.043
2-C-methyl-D-erythritol 4-phosphate
calculated affinity
0.061
2-C-methyl-D-erythritol 4-phosphate
-
pH 7.5, 30°C
0.1248
2-C-methyl-D-erythritol 4-phosphate
recombinant detagged enzyme, pH 8.0, 30°C
0.178
2-C-methyl-D-erythritol 4-phosphate
-
pH 8.0, 37°C
0.2915
2-C-methyl-D-erythritol 4-phosphate
recombinant detagged enzyme, pH 8.0, 30°C
0.31
2-C-methyl-D-erythritol 4-phosphate
R20K mutant enzyme, pH 6.5, 23°C
0.37
2-C-methyl-D-erythritol 4-phosphate
wild type enzyme, pH 6.5, 23°C
0.74
2-C-methyl-D-erythritol 4-phosphate
R19K mutant enzyme, pH 6.5, 23°C
2.98
2-C-methyl-D-erythritol 4-phosphate
R19A mutant enzyme, pH 6.5, 23°C
3
2-C-methyl-D-erythritol 4-phosphate
K27S mutant enzyme, pH 6.5, 23°C
3.28
2-C-methyl-D-erythritol 4-phosphate
R20A mutant enzyme, pH 6.5, 23°C
15.5
2-C-methyl-D-erythritol 4-phosphate
D106E mutant enzyme, pH 6.5, 23°C
49
2-C-methyl-D-erythritol 4-phosphate
T140V mutant enzyme, pH 6.5, 23°C
131.5
2-C-methyl-D-erythritol 4-phosphate
R109A mutant enzyme, pH 6.5, 23°C
0.00314
2-C-methyl-D-erythritol-4-phosphate
-
-
0.032
2-C-methyl-D-erythritol-4-phosphate
-
-
3.26
2-C-methyl-D-erythritol-4-phosphate
-
-
0.131
4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
0.5
4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
-
-
0.003
CTP
-
0.02305
CTP
pH 7.9, 37°C, recombinant enzyme
0.092
CTP
calculated affinity
0.1328
CTP
recombinant detagged enzyme, pH 8.0, 30°C
0.2309
CTP
recombinant detagged enzyme, pH 8.0, 30°C
0.76
CTP
wild type enzyme, pH 6.5, 23°C
0.85
CTP
R19K mutant enzyme, pH 6.5, 23°C
1.1
CTP
K27S mutant enzyme, pH 6.5, 23°C
1.4
CTP
D106E mutant enzyme, pH 6.5, 23°C
2
CTP
T140V mutant enzyme, pH 6.5, 23°C
2.8
CTP
R19A mutant enzyme, pH 6.5, 23°C
3
CTP
R109A mutant enzyme, pH 6.5, 23°C
3.7
CTP
R20K mutant enzyme, pH 6.5, 23°C
6.6
CTP
R20A mutant enzyme, pH 6.5, 23°C
additional information
additional information
kinetic analysis
-
additional information
additional information
-
kinetic analysis
-
additional information
additional information
kinetic analysis
-
additional information
additional information
-
kinetic analysis
-
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0.4 - 52.7
2-C-methyl-D-erythritol 4-phosphate
1.4 - 16.8
2-C-methyl-D-erythritol-4-phosphate
additional information
ATP
-
13% activity compared to CTP
0.4
2-C-methyl-D-erythritol 4-phosphate
R109A mutant enzyme, pH 6.5, 23°C
0.75
2-C-methyl-D-erythritol 4-phosphate
K27S mutant enzyme, pH 6.5, 23°C
0.9
2-C-methyl-D-erythritol 4-phosphate
D106E mutant enzyme, pH 6.5, 23°C
1
2-C-methyl-D-erythritol 4-phosphate
-
pH 8.0, 37°C
4
2-C-methyl-D-erythritol 4-phosphate
T140V mutant enzyme, pH 6.5, 23°C
7.6
2-C-methyl-D-erythritol 4-phosphate
pH 7.4, 37°C
21.4
2-C-methyl-D-erythritol 4-phosphate
R20K mutant enzyme, pH 6.5, 23°C
36.35
2-C-methyl-D-erythritol 4-phosphate
recombinant detagged enzyme, pH 8.0, 30°C
36.8
2-C-methyl-D-erythritol 4-phosphate
R19A mutant enzyme, pH 6.5, 23°C
38.45
2-C-methyl-D-erythritol 4-phosphate
recombinant detagged enzyme, pH 8.0, 30°C
47.2
2-C-methyl-D-erythritol 4-phosphate
R19K mutant enzyme, pH 6.5, 23°C
48.4
2-C-methyl-D-erythritol 4-phosphate
wild type enzyme, pH 6.5, 23°C
52.7
2-C-methyl-D-erythritol 4-phosphate
R20A mutant enzyme, pH 6.5, 23°C
1.4
2-C-methyl-D-erythritol-4-phosphate
-
-
16.8
2-C-methyl-D-erythritol-4-phosphate
-
-
0.26
CTP
R109A mutant enzyme, pH 6.5, 23°C
0.93
CTP
D106E mutant enzyme, pH 6.5, 23°C
1.8
CTP
T140V mutant enzyme, pH 6.5, 23°C
2.05
CTP
K27S mutant enzyme, pH 6.5, 23°C
3.4
CTP
-
slightly lower than from bacterial and plant sources
27.5
CTP
R19A mutant enzyme, pH 6.5, 23°C
40.2
CTP
R20A mutant enzyme, pH 6.5, 23°C
46.4
CTP
R19K mutant enzyme, pH 6.5, 23°C
53.6
CTP
R20K mutant enzyme, pH 6.5, 23°C
54.1
CTP
wild type enzyme, pH 6.5, 23°C
71.24
CTP
recombinant detagged enzyme, pH 8.0, 30°C
79.5
CTP
recombinant detagged enzyme, pH 8.0, 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.000084
(1R,3S)-1-(2,4-dibromophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
Plasmodium falciparum
pH 7.4, 37°C
0.001
(1R,3S)-1-(2,4-dichlorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxamide
Plasmodium falciparum
pH 7.4, 37°C
0.000044
(1R,3S)-1-(2,4-dichlorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
Plasmodium falciparum
pH 7.4, 37°C
0.001
(1R,3S)-1-(2,4-dichlorophenyl)-N-ethyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxamide
Plasmodium falciparum
pH 7.4, 37°C
0.000057
(1R,3S)-1-(2,4-dichlorophenyl)-N-methyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxamide
Plasmodium falciparum
pH 7.4, 37°C
0.00023
(1R,3S)-1-(2,4-difluorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
Plasmodium falciparum
pH 7.4, 37°C
0.000031
(1R,3S)-1-(2-bromo-4-chlorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
Plasmodium falciparum
pH 7.4, 37°C
0.000031
(1R,3S)-1-(2-bromo-4-chlorophenyl)-N-methyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxamide
Plasmodium falciparum
pH 7.4, 37°C
0.0001
(1R,3S)-1-(2-chloro-4-fluorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
Plasmodium falciparum
pH 7.4, 37°C
0.00028
(1R,3S)-1-(2-chloro-4-fluorophenyl)-N-methyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxamide
Plasmodium falciparum
pH 7.4, 37°C
0.000082
(1R,3S)-1-(2-chloro-4-methylphenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
Plasmodium falciparum
pH 7.4, 37°C
0.00036
(1R,3S)-1-(2-chloro-4-methylphenyl)-N-methyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxamide
Plasmodium falciparum
pH 7.4, 37°C
0.001
(1R,3S)-1-(2-chlorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
Plasmodium falciparum
pH 7.4, 37°C
0.00013
(1R,3S)-1-(2-fluoro-4-iodophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
Plasmodium falciparum
pH 7.4, 37°C
0.000034
(1R,3S)-1-(4-bromo-2-chlorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
Plasmodium falciparum
pH 7.4, 37°C
0.000021
(1R,3S)-1-(4-bromo-2-chlorophenyl)-N-methyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxamide
Plasmodium falciparum
pH 7.4, 37°C
0.00014
(1R,3S)-1-(4-chloro-2-fluorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
Plasmodium falciparum
pH 7.4, 37°C
0.00026
(1R,3S)-1-(4-chloro-2-methylphenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
Plasmodium falciparum
pH 7.4, 37°C
0.00051
(1R,3S)-1-(4-chlorophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
Plasmodium falciparum
pH 7.4, 37°C
0.00014
(1R,3S)-1-(4-fluoro-2-iodophenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
Plasmodium falciparum
pH 7.4, 37°C
0.005
(1R,3S)-1-phenyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
Plasmodium falciparum
pH 7.4, 37°C
0.005
(1R,3S)-1-[2,4-bis(dimethoxymethyl)phenyl]-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
Plasmodium falciparum
pH 7.4, 37°C
0.005
(1R,3S)-1-[2,4-bis(trifluoromethyl)phenyl]-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
Plasmodium falciparum
pH 7.4, 37°C
0.001
(1R,3S)-1-[2,4-di(propan-2-yl)phenyl]-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylic acid
Plasmodium falciparum
pH 7.4, 37°C
0.000047 - 0.00032
(2,4-dichloro-phenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indol-2-ium-3-carboxylate
-
0.000047
(2,4-dichloro-phenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indol-2-ium-3-carboxylate
Plasmodium falciparum
recombinant wild-type enzyme, pH 7.0, 37°C
-
0.0001
(2,4-dichloro-phenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indol-2-ium-3-carboxylate
Plasmodium falciparum
recombinant IspD mutant L244I, pH 7.0, 37°C
-
0.00031
(2,4-dichloro-phenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indol-2-ium-3-carboxylate
Plasmodium vivax
recombinant wild-type enzyme, pH 7.0, 37°C
-
0.00032
(2,4-dichloro-phenyl)-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indol-2-ium-3-carboxylate
Plasmodium falciparum
recombinant IspD mutant E688Q, pH 7.0, 37°C
-
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evolution
-
the enzyme is a member of the cytidylyltransferase family of enzymes that utilize cytidine 5'-triphosphate (CTP) to synthesize molecules that are typically precursors to membrane phospholipids
evolution
structure, function and mechanism of Plasmodium IspD homologs from their evolutionary imprints, e.g. Theileria annulata. Structure-based phylogeny for PlIspD homologues, constructed by using the maximum likelihood algorithm with the Dayhoff model structure and structure motifs prediction and characterization of PlIspD homologues, overview
evolution
Plasmodium falciparum Tanzania (20000708)
-
structure, function and mechanism of Plasmodium IspD homologs from their evolutionary imprints, e.g. Theileria annulata. Structure-based phylogeny for PlIspD homologues, constructed by using the maximum likelihood algorithm with the Dayhoff model structure and structure motifs prediction and characterization of PlIspD homologues, overview
-
malfunction
the inhibition of DXR (EC 1.1.1.267, MEP synthase) dramatically reduces IspD function in cells. Phosphonic acid antibiotic fosmidomycin is a substrate mimic and inhibitor of DXR. The inhibition of downstream enzyme IspD is also metabolically apparent in fosmidomycin-treated cells, although IspD homologues are not directly inhibited by fosmidomycin in vitro
malfunction
the inhibition of DXR (EC 1.1.1.267, MEP synthase) dramatically reduces IspD function in cells. Phosphonic acid antibiotic fosmidomycin is a substrate mimic and inhibitor of DXR. The inhibition of downstream enzyme IspD is also metabolically apparent in fosmidomycin-treated cells, although IspD homologues are not directly inhibited by fosmidomycin in vitro
malfunction
the inhibition of DXR (EC 1.1.1.267, MEP synthase) dramatically reduces IspD function in cells. Phosphonic acid antibiotic fosmidomycin is a substrate mimic and inhibitor of DXR.13 The inhibition of downstream enzyme IspD is also metabolically apparent in fosmidomycin-treated cells, although IspD homologues are not directly inhibited by fosmidomycin in vitro. 1R,3S-MMV008138-treated parasites supplemented with 0.2 mM isopentenyl diphosphate (IPP) are viable, but 1R,3S-MMV008138 treatment of such IPP-rescued cells still results in a significant reduction in methylerythritol cyclic diphosphate (MEcPP) levels, the most distal MEP metabolite detected
malfunction
-
the inhibition of DXR (EC 1.1.1.267, MEP synthase) dramatically reduces IspD function in cells. Phosphonic acid antibiotic fosmidomycin is a substrate mimic and inhibitor of DXR. The inhibition of downstream enzyme IspD is also metabolically apparent in fosmidomycin-treated cells, although IspD homologues are not directly inhibited by fosmidomycin in vitro
-
malfunction
-
the inhibition of DXR (EC 1.1.1.267, MEP synthase) dramatically reduces IspD function in cells. Phosphonic acid antibiotic fosmidomycin is a substrate mimic and inhibitor of DXR. The inhibition of downstream enzyme IspD is also metabolically apparent in fosmidomycin-treated cells, although IspD homologues are not directly inhibited by fosmidomycin in vitro
-
malfunction
-
the inhibition of DXR (EC 1.1.1.267, MEP synthase) dramatically reduces IspD function in cells. Phosphonic acid antibiotic fosmidomycin is a substrate mimic and inhibitor of DXR. The inhibition of downstream enzyme IspD is also metabolically apparent in fosmidomycin-treated cells, although IspD homologues are not directly inhibited by fosmidomycin in vitro
-
metabolism
the MEP cytidylyltransferase, or IspD catalyzes the second committed step of the methyl erythritol phosphate (MEP) pathway. The MEP pathway is essential for the production of isoprenoids
metabolism
the MEP cytidylyltransferase, or IspD catalyzes the second committed step of the methyl erythritol phosphate (MEP) pathway. The MEP pathway is essential for the production of isoprenoids
metabolism
Francisella tularensis subsp. novicida Utah 112
-
the MEP cytidylyltransferase, or IspD catalyzes the second committed step of the methyl erythritol phosphate (MEP) pathway. The MEP pathway is essential for the production of isoprenoids
-
physiological function
2C-methyl-D-erythritol-4-phosphate cytidylyltransferase is the third enzyme in the MEP pathway for isoprenoid biosynthesis
physiological function
enzyme is part of the MEP pathway of biosynthesis of isoprenoid precursors
physiological function
2-C-methyl-D-erythritol 4-phosphate cytidyltransferase (IspD) is an essential enzyme in the mevalonate-independent pathway of isoprenoid biosynthesis. This enzyme catalyzes 2-C-methyl-derythritol 4-phosphate (MEP) and cytosine triphosphate (CTP) to 4-diphosphocytidyl-2-C-methyl-derythritol (CDPME) and diphosphate
physiological function
2-C-methyl-D-erythritol 4-phosphate cytidyltransferase (IspD) is an essential enzyme in the mevalonate-independent pathway of isoprenoid biosynthesis. This enzyme catalyzes 2-C-methyl-derythritol 4-phosphate (MEP) and cytosine triphosphate (CTP) to 4-diphosphocytidyl-2-C-methyl-derythritol (CDPME) and diphosphate
physiological function
enzyme 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (IspD) acts in the MEP pathway and converts MEP and cytidine triphosphate (CTP) to cytidine diphosphate methylerythritol (CDP-ME) and diphosphate
physiological function
enzyme IspD (MEP cytidyltransferase) catalyzes the cytidylation of MEP to cytidine diphosphate methylerythritol (CDP-ME)
physiological function
enzyme IspD (MEP cytidyltransferase) catalyzes the cytidylation of MEP to cytidine diphosphate methylerythritol (CDP-ME)
physiological function
enzyme IspD (MEP cytidyltransferase) catalyzes the cytidylation of MEP to cytidine diphosphate methylerythritol (CDP-ME)
physiological function
enzyme MCT plays an influential role in isoprenoid biosynthesis
physiological function
-
2-C-methyl-D-erythritol 4-phosphate cytidyltransferase (IspD) is an essential enzyme in the mevalonate-independent pathway of isoprenoid biosynthesis. This enzyme catalyzes 2-C-methyl-derythritol 4-phosphate (MEP) and cytosine triphosphate (CTP) to 4-diphosphocytidyl-2-C-methyl-derythritol (CDPME) and diphosphate
-
physiological function
-
enzyme IspD (MEP cytidyltransferase) catalyzes the cytidylation of MEP to cytidine diphosphate methylerythritol (CDP-ME)
-
physiological function
-
2-C-methyl-D-erythritol 4-phosphate cytidyltransferase (IspD) is an essential enzyme in the mevalonate-independent pathway of isoprenoid biosynthesis. This enzyme catalyzes 2-C-methyl-derythritol 4-phosphate (MEP) and cytosine triphosphate (CTP) to 4-diphosphocytidyl-2-C-methyl-derythritol (CDPME) and diphosphate
-
physiological function
-
2C-methyl-D-erythritol-4-phosphate cytidylyltransferase is the third enzyme in the MEP pathway for isoprenoid biosynthesis
-
physiological function
-
enzyme IspD (MEP cytidyltransferase) catalyzes the cytidylation of MEP to cytidine diphosphate methylerythritol (CDP-ME)
-
physiological function
-
enzyme IspD (MEP cytidyltransferase) catalyzes the cytidylation of MEP to cytidine diphosphate methylerythritol (CDP-ME)
-
additional information
molecular dynamics simulation, homology PvIspD structure prediction by comparative modeling technique using the Escherichia coli IspD crystal structure (PDB ID 1I52) as template, and three-dimensional modeling of PvIspD. The conserved domain (NCBI) analysis of translated sequences (619 a.a.) shows the presence of Glycosyl transferase family A (GT-A) domain spanning the amino acid residues 191-558. The two signature motifs of the IspD proteins in this domain viz. GXG and [IVT]-[LIVMC]-[IVT]-[HS]-D-[SGAV]-[AV]-R are also observed in PVX_081425 and all Indian PvIspD sequences by PROSITE as 199GXG201 and 424ILVHDGAR431. Key residues R431 and K548 form the salt bridge with CTP
additional information
-
molecular dynamics simulation, homology PvIspD structure prediction by comparative modeling technique using the Escherichia coli IspD crystal structure (PDB ID 1I52) as template, and three-dimensional modeling of PvIspD. The conserved domain (NCBI) analysis of translated sequences (619 a.a.) shows the presence of Glycosyl transferase family A (GT-A) domain spanning the amino acid residues 191-558. The two signature motifs of the IspD proteins in this domain viz. GXG and [IVT]-[LIVMC]-[IVT]-[HS]-D-[SGAV]-[AV]-R are also observed in PVX_081425 and all Indian PvIspD sequences by PROSITE as 199GXG201 and 424ILVHDGAR431. Key residues R431 and K548 form the salt bridge with CTP
additional information
the concerted movements of the P-loop and loops close to the active site are essential in the reaction catalyzed by IspD. The intact P-loop is observed in the apo structure of IspD enzyme. The P-loop comprising residues 8-21 in the apo form I are refined satisfactorily, the B-factor of 30 A2 is almost the same as the average B-factor of all the protein atoms, this loop is highly conserved in the IspD enzymes. BsIspD structure, overview. The active site of BsIspD is covered by P-loop; hydrogen bonding interactions are formed between P-loop and adjacent residues. Upon CTP binding, conformational changes are observed on P-loop, L1-loop and L2-loop. The N-terminal half of the P-loop flips upward from active pocket and the C-terminal half flips down right, the active pocket is open to accommodate the CTP. A cleft is formed between L1-loop and P-loop, favoring for the binding of the cytosine base of CTP, at the same time, the residue Arg15 in the P-loop forms hydrogen bond to the residue Thr211 in L2-loop
additional information
-
the concerted movements of the P-loop and loops close to the active site are essential in the reaction catalyzed by IspD. The intact P-loop is observed in the apo structure of IspD enzyme. The P-loop comprising residues 8-21 in the apo form I are refined satisfactorily, the B-factor of 30 A2 is almost the same as the average B-factor of all the protein atoms, this loop is highly conserved in the IspD enzymes. BsIspD structure, overview. The active site of BsIspD is covered by P-loop; hydrogen bonding interactions are formed between P-loop and adjacent residues. Upon CTP binding, conformational changes are observed on P-loop, L1-loop and L2-loop. The N-terminal half of the P-loop flips upward from active pocket and the C-terminal half flips down right, the active pocket is open to accommodate the CTP. A cleft is formed between L1-loop and P-loop, favoring for the binding of the cytosine base of CTP, at the same time, the residue Arg15 in the P-loop forms hydrogen bond to the residue Thr211 in L2-loop
additional information
the enzyme's catalytic pocket, which actively participates in interaction with ligands, mainly consists of polar amino acid residues, three-dimensional modeling of the IspD protein
additional information
the Pf ISPD genetic locus is refractory to disruption in malaria parasites, providing independent genetic validation for efforts targeting this enzyme
additional information
-
the Pf ISPD genetic locus is refractory to disruption in malaria parasites, providing independent genetic validation for efforts targeting this enzyme
additional information
-
the concerted movements of the P-loop and loops close to the active site are essential in the reaction catalyzed by IspD. The intact P-loop is observed in the apo structure of IspD enzyme. The P-loop comprising residues 8-21 in the apo form I are refined satisfactorily, the B-factor of 30 A2 is almost the same as the average B-factor of all the protein atoms, this loop is highly conserved in the IspD enzymes. BsIspD structure, overview. The active site of BsIspD is covered by P-loop; hydrogen bonding interactions are formed between P-loop and adjacent residues. Upon CTP binding, conformational changes are observed on P-loop, L1-loop and L2-loop. The N-terminal half of the P-loop flips upward from active pocket and the C-terminal half flips down right, the active pocket is open to accommodate the CTP. A cleft is formed between L1-loop and P-loop, favoring for the binding of the cytosine base of CTP, at the same time, the residue Arg15 in the P-loop forms hydrogen bond to the residue Thr211 in L2-loop
-
additional information
-
molecular dynamics simulation, homology PvIspD structure prediction by comparative modeling technique using the Escherichia coli IspD crystal structure (PDB ID 1I52) as template, and three-dimensional modeling of PvIspD. The conserved domain (NCBI) analysis of translated sequences (619 a.a.) shows the presence of Glycosyl transferase family A (GT-A) domain spanning the amino acid residues 191-558. The two signature motifs of the IspD proteins in this domain viz. GXG and [IVT]-[LIVMC]-[IVT]-[HS]-D-[SGAV]-[AV]-R are also observed in PVX_081425 and all Indian PvIspD sequences by PROSITE as 199GXG201 and 424ILVHDGAR431. Key residues R431 and K548 form the salt bridge with CTP
-
additional information
-
the concerted movements of the P-loop and loops close to the active site are essential in the reaction catalyzed by IspD. The intact P-loop is observed in the apo structure of IspD enzyme. The P-loop comprising residues 8-21 in the apo form I are refined satisfactorily, the B-factor of 30 A2 is almost the same as the average B-factor of all the protein atoms, this loop is highly conserved in the IspD enzymes. BsIspD structure, overview. The active site of BsIspD is covered by P-loop; hydrogen bonding interactions are formed between P-loop and adjacent residues. Upon CTP binding, conformational changes are observed on P-loop, L1-loop and L2-loop. The N-terminal half of the P-loop flips upward from active pocket and the C-terminal half flips down right, the active pocket is open to accommodate the CTP. A cleft is formed between L1-loop and P-loop, favoring for the binding of the cytosine base of CTP, at the same time, the residue Arg15 in the P-loop forms hydrogen bond to the residue Thr211 in L2-loop
-
additional information
-
the enzyme's catalytic pocket, which actively participates in interaction with ligands, mainly consists of polar amino acid residues, three-dimensional modeling of the IspD protein
-
additional information
-
the enzyme's catalytic pocket, which actively participates in interaction with ligands, mainly consists of polar amino acid residues, three-dimensional modeling of the IspD protein
-
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monomer
-
sedimentation velocity experiments, both wild-type and mutant D152A
?
-
x * 29000, SDS-PAGE, x * 25472 is predicted from sequence of c DNA
?
x * 25737 is predicted from sequence of c DNA
dimer
two crystal structures of BsIspD are determined in orthorhombic crystal form with space group P212121 and P21212, named apo form I and II, respectively. In the apo form I, two molecules in the asymmetric unit are related by 2fold sysmetry and form a dimer. In the apo form II, only one molecule is retained in the asymmetric unit, the functional dimer is formed by the sysmetry operation
dimer
-
two crystal structures of BsIspD are determined in orthorhombic crystal form with space group P212121 and P21212, named apo form I and II, respectively. In the apo form I, two molecules in the asymmetric unit are related by 2fold sysmetry and form a dimer. In the apo form II, only one molecule is retained in the asymmetric unit, the functional dimer is formed by the sysmetry operation
-
dimer
-
two crystal structures of BsIspD are determined in orthorhombic crystal form with space group P212121 and P21212, named apo form I and II, respectively. In the apo form I, two molecules in the asymmetric unit are related by 2fold sysmetry and form a dimer. In the apo form II, only one molecule is retained in the asymmetric unit, the functional dimer is formed by the sysmetry operation
-
dimer
-
2 * 26000, SDS-PAGE
dimer
-
each subunit contains a globular core domain with an alpha/beta sturcture and and one smaller subdomain
dimer
crystal structure analysis
dimer
-
2 * 25700, crystal structure analysis
dimer
-
2 * 26000, SDS-PAGE
-
dimer
the beta-domains of the monomers are mainly responsible for the formation of the dimer
dimer
-
the beta-domains of the monomers are mainly responsible for the formation of the dimer
-
dimer
-
the beta-domains of the monomers are mainly responsible for the formation of the dimer
-
hexamer
-
-
hexamer
-
6 * 41700, crystal structure analysis
homodimer
-
-
additional information
the subunit structure of BsIspD is of a compact alpha/beta fold from which a long beta-meander extended. The core of the enzyme consists of a seven beta-sheets ( beta2, beta1, beta4, beta9, beta5, beta8, beta10 ) where all strands are parallel, apart from beta8 and beta2. The beta-meander lay between antiparallel strands beta6 and beta7 and made the major contribution to the dimer interface, and the lesser contribution came from the side-chain interactions of the residues on the alpha-helix fragment at the C-terminus. BsIspD structure, overview
additional information
-
the subunit structure of BsIspD is of a compact alpha/beta fold from which a long beta-meander extended. The core of the enzyme consists of a seven beta-sheets ( beta2, beta1, beta4, beta9, beta5, beta8, beta10 ) where all strands are parallel, apart from beta8 and beta2. The beta-meander lay between antiparallel strands beta6 and beta7 and made the major contribution to the dimer interface, and the lesser contribution came from the side-chain interactions of the residues on the alpha-helix fragment at the C-terminus. BsIspD structure, overview
additional information
-
the subunit structure of BsIspD is of a compact alpha/beta fold from which a long beta-meander extended. The core of the enzyme consists of a seven beta-sheets ( beta2, beta1, beta4, beta9, beta5, beta8, beta10 ) where all strands are parallel, apart from beta8 and beta2. The beta-meander lay between antiparallel strands beta6 and beta7 and made the major contribution to the dimer interface, and the lesser contribution came from the side-chain interactions of the residues on the alpha-helix fragment at the C-terminus. BsIspD structure, overview
-
additional information
-
the subunit structure of BsIspD is of a compact alpha/beta fold from which a long beta-meander extended. The core of the enzyme consists of a seven beta-sheets ( beta2, beta1, beta4, beta9, beta5, beta8, beta10 ) where all strands are parallel, apart from beta8 and beta2. The beta-meander lay between antiparallel strands beta6 and beta7 and made the major contribution to the dimer interface, and the lesser contribution came from the side-chain interactions of the residues on the alpha-helix fragment at the C-terminus. BsIspD structure, overview
-
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Cane, D.E.; Chow, C.; Lillo, A.; Kang, I.
Molecular cloning, expression and characterization of the first three genes in the mevalonate-independent isoprenoid pathway in Streptomyces coelicolor
Bioorg. Med. Chem.
9
1467-1477
2001
Escherichia coli, Streptomyces coelicolor, Streptomyces coelicolor CH999
brenda
Richard, S.B.; Bowman, M.E.; Kwiatkowski, W.; Kang, L.; Chow, C.; Lillo, A.M.; Cane, D.E.; Noel, J.P.
Structure of 4-diphosphocytidyl-2-C-methylerythritol synthetase involved in mevalonate-independent isoprenoid biosynthesis
Nature Struct. Biol.
8
641-648
2001
Escherichia coli, Mycobacterium tuberculosis, Plasmodium falciparum
brenda
Kemp, L.E.; Bond, C.S.; Hunter, W.N.
Crystallization and preliminary x-ray diffraction studies of recombinant Escherichia coli 4-diphosphocytidyl-2-C-methyl-D-erythritol synthetase
Acta Crystallogr. Sect. D
57
1189-1191
2001
Escherichia coli
brenda
Rohdich, F.; Wungsintaweekul, J.; Eisenreich, W.; Richter, G.; Schuhr, C.A.; Hecht, S.; Zenk, M.H.; Bacher, A.
Biosynthesis of terpenoids: 4-diphosphocytidyl-2C-methyl-D-erythritol synthase of Arabidopsis thaliana
Proc. Natl. Acad. Sci. USA
97
6451-6456
2000
Arabidopsis thaliana, Escherichia coli (Q46893), Escherichia coli
brenda
Kuzuyama, T.; Takagi, M.; Kaneda, K.; Dairi, T.; Seto, H.
Formation of 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol from 2-C-methyl-D-erythritol 4-phosphate by 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase, a new enzyme in the nonmevalonate pathway
Tetrahedron Lett.
41
703-706
2000
Escherichia coli
-
brenda
Rohdich, F.; Wungsintaweekul, J.; Fellermeier, M.; Sagner, S.; Herz, S.; Kis, K.; Eisenreich, W.; Bacher, A.; Zenk, M.H.
Cytidine 5'-triphosphate-dependent biosynthesis of isoprenoids: YgbP protein of Escherichia coli catalyzes the formation of 4-diphosphocytidyl-2-C-methylerythritol
Proc. Natl. Acad. Sci. USA
96
11758-11763
1999
Arabidopsis thaliana, Escherichia coli, Escherichia coli DH5-alpha
brenda
Gabrielsen, M.; Bond, C.S.; Hallyburton, I.; Hecht, S.; Bacher, A.; Eisenreich, W.; Rohdich, F.; Hunter, W.N.
Hexameric assembly of the bifunctional methylerythritol 2,4-cyclodiphosphate synthase and protein-protein associations in the deoxy-xylulose-dependent pathway of isoprenoid precursor biosynthesis
J. Biol. Chem.
279
52753-52761
2004
Agrobacterium tumefaciens, Campylobacter jejuni, Escherichia coli (Q46893), Escherichia coli
brenda
Kemp, L.E.; Bond, C.S.; Hunter, W.N.
Structure of a tetragonal crystal form of Escherichia coli 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Acta Crystallogr. Sect. D
59
607-610
2003
Escherichia coli
brenda
Bernal, C.; Palacin, C.; Boronat, A.; Imperial, S.
A colorimetric assay for the determination of 4-diphosphocytidyl-2-C-methyl-D-erythritol 4-phosphate synthase activity
Anal. Biochem.
337
55-61
2005
Escherichia coli
brenda
Richard, S.B.; Lillo, A.M.; Tetzlaff, C.N.; Bowman, M.E.; Noel, J.P.; Cane, D.E.
Kinetic analysis of Escherichia coli 2-C-methyl-D-erythritol-4-phosphate cytidyltransferase, wild type and mutants, reveals roles of active site amino acids
Biochemistry
43
12189-12197
2004
Escherichia coli (Q46893), Escherichia coli
brenda
Zhao, X.; Miller, J.R.; Jiang, Y.; Marletta, M.A.; Cronan, J.E.
Assembly of the covalent linkage between lipoic acid and its cognate enzymes
Chem. Biol.
10
1293-1302
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
Gabrielsen, M.; Kaiser, J.; Rohdich, F.; Eisenreich, W.; Laupitz, R.; Bacher, A.; Bond, C.S.; Hunter, W.N.
The crystal structure of a plant 2C-methyl-D-erythritol 4-phosphate cytidylyltransferase exhibits a distinct quaternary structure compared to bacterial homologues and a possible role in feedback regulation for cytidine monophosphate
FEBS J.
273
1065-1073
2006
Arabidopsis thaliana (P69834), Arabidopsis thaliana
brenda
Illarionova, V.; Kaiser, J.; Ostrozhenkova, E.; Bacher, A.; Fischer, M.; Eisenreich, W.; Rohdich, F.
Nonmevalonate terpene biosynthesis enzymes as antiinfective drug targets: substrate synthesis and high-throughput screening methods
J. Org. Chem.
71
8824-8834
2006
Escherichia coli
brenda
Kim, S.M.; Kuzuyama, T.; Chang, Y.J.; Kwon, H.J.; Kim, S.U.
Cloning and functional characterization of 2-C-methyl-D-erythritol 4-phosphate cytidyltransferase (GbMECT) gene from Ginkgo biloba
Phytochemistry
67
1435-1441
2006
Ginkgo biloba (Q0R5D7), Ginkgo biloba
brenda
Sando, T.; Takeno, S.; Watanabe, N.; Okumoto, H.; Kuzuyama, T.; Yamashita, A.; Hattori, M.; Ogasawara, N.; Fukusaki, E.; Kobayashi, A.
Cloning and characterization of the 2-C-methyl-D-erythritol 4-phosphate (MEP) pathway genes of a natural-rubber producing plant, Hevea brasiliensis
Biosci. Biotechnol. Biochem.
72
2903-2917
2008
Hevea brasiliensis (A9ZN09), Hevea brasiliensis (A9ZN10), Hevea brasiliensis
brenda
Shi, W.; Feng, J.; Zhang, M.; Lai, X.; Xu, S.; Zhang, X.; Wang, H.
Biosynthesis of isoprenoids: characterization of a functionally active recombinant 2-C-methyl-D-erythritol 4-phosphate cytidyltransferase (IspD) from Mycobacterium tuberculosis H37Rv
J. Biochem. Mol. Biol.
40
911-920
2007
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
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Obiol-Pardo, C.; Cordero, A.; Rubio-Martinez, J.; Imperial, S.
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