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Enzyme Nomenclature
Information on EC 1.1.1.267 - 1-deoxy-D-xylulose-5-phosphate reductoisomerase
for references in articles please use BRENDA:EC1.1.1.267
Word Map on EC 1.1.1.267
- 1.1.1.267
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isoprenoids
- fosmidomycin
- plasmodium
- falciparum
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non-mevalonate
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isopentenyl
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terpenoids
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antimalarial
- mevalonate
- isoprene
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mevalonate-independent
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dimethylallyl
- drug development
- biotechnology
- medicine
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
1.1.1.267
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RECOMMENDED NAME
GeneOntology No.
1-deoxy-D-xylulose-5-phosphate reductoisomerase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH + H+
stereochemistry
-
2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH + H+
mechanism
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2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH + H+
steady-state random mechanism
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2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH + H+
active site structure
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2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH + H+
the conserved active site residue Trp204 is important in catalysis
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2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH + H+
the reaction does not exhibit burst kinetics for either substrate, indicating that product release is not rate-limiting, the rearrangement step, which precedes hydride transfer, is rate-limiting for 1-deoxy-D-xylulose 5-phosphate but becomes partially ratelimiting for 1-fluoro-1-deoxy-D-xylulose 5-phosphate, thus, rearrangement appears to be enhanced by substitution of a hydrogen atom in the methyl group of 1-deoxy-D-xylulose 5-phosphate by fluorine, consistent with a retro-aldol/aldol mechanism for the rearrangement during conversion of 1-deoxy-D-xylulose 5-phosphate to 2-C-methyl-D-erythritol 4-phosphate
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2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH + H+
reaction mechanism via 2-C-methylerythrose 4-phosphate intermediate
-
2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH + H+
highly conserved active site structure, active site residues Asp157, Glu159, and Glu241, residue His219 is essential for placing the substrate in the active site for optimal catalysis
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2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH + H+
reaction mechanism
-
2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH + H+
retro-aldol/aldol mechanism
-
2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH + H+
random substrate binding and ordered release of NADP+ followed by partially rate-limiting release of 2-C-methyl-D-erythritol 4-phosphate, transient generation of MtDXR-NADPH-MEP ternary complex, kinetic analysis and modeling, overview
-
2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH + H+
random ordered mechanism, though binding of NADPH first is preferential at 0.2 mM due to its low Km. Conformational equilibrium between a predominant, inactive open form and a minor, active closed form of the unliganded enzyme, overview
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2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH + H+
active site structure
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-
2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH + H+
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
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redox reaction
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-
-
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reduction
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
2-C-methyl-D-erythritol-4-phosphate:NADP+ oxidoreductase (isomerizing)
The enzyme requires Mn2+, Co2+ or Mg2+ for activity, with the first being most effective. The enzyme from several eubacteria, including Escherichia coli, forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis (for diagram, {terp/nonMVA}). The mechanism has been shown to be a retroaldol/aldol reaction [2].
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CAS REGISTRY NUMBER
COMMENTARY
210756-42-6
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
from medicinal garden of Guangzhou University of Chinese Medicine, China
UniProt
-
286421, 286422, 286423, 286427, 656890, 672040, 675577, 675580, 684434, 689434, 697249, 712689, 723812, 724558, 740472, 741430
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UniProt
isoform DXS2a, type II enzyme. Induced expression after treatment with chitosan, methyl salicylate, and fungal pathogen Ceratocystis polonica
SwissProt
isoform DXS2b, type II enzyme. Induced expression after treatment with chitosan and methyl salicylate, but not by fungal pathogen Ceratocystis polonica
SwissProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
additional information
metabolism
the enzyme catalyzes the second regulation step in the 2-C-methyl-D-erythritol 4-phosphate pathway and the the first committed step of the 2-C-methyl-D-erythritol 4-phosphate pathway for isoprenoid biosynthesis
metabolism
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the 1-deoxy-D-xylulose-5-phosphate reductoisomerase is the second enzyme in the nonmevalonate isoprene biosynthesis pathway, catalyzing the reductive isomerization of 1-deoxy-D-xylulose-5-phosphate to 2-methyl-D-erythritol-4-phosphate for making isopentenyl diphosphate and dimethylallyl diphosphate
metabolism
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the 1-deoxy-D-xylulose-5-phosphate reductoisomerase is the second enzyme in the nonmevalonate isoprene biosynthesis pathway, catalyzing the reductive isomerization of 1-deoxy-D-xylulose-5-phosphate to 2-methyl-D-erythritol-4-phosphate for making isopentenyl diphosphate and dimethylallyl diphosphate
metabolism
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1-deoxy-D-xylulose-5-phosphate, DXP, reductoisomerase catalyzes the first committed step in the 2-C-methyl-D-erythritol 4-phosphate pathway involving a skeletal rearrangement of DXP via a retroaldol/aldol process followed by reduction by NADPH to yield 2-C-methyl-D-erythritol 4-phosphate
metabolism
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the enzyme is involved in the isoprenoid biosynthetic DOXP/MEP pathway
metabolism
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the enzyme is involved in a parasite-specific, isoprenoid biosynthetic DOXP/MEP pathway
physiological function
involved in the 2-C-methyl-D-erythritol 4-phosphate pathway
physiological function
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a dxr gene T-DNA insertion mutant shows albino and dwarf phenotype. The mutant does not bolt, has a significantly reduced number of trichomes and most of the stomata cannot close normally in the leaves. Two transgenic co-suppression lines produce more yellow inflorescences and albino sepals with no trichomes. The transcription levels of genes involved in trichome initiation are strongly affected in the mutants. Exogenous application of gibberellic acid GA3 can partially rescue the dwarf phenotype and the trichome initiation of the insertion mutant, and exogenous application of abscisic acid can rescue the stomata closure defect
physiological function
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1-deoxy-D-xylulose-5-phosphate reductoisomerase in the non-mevalonate isoprene biosynthesis pathway is essential to the organism
physiological function
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in transgenic spike lavender plants (Lavandula latifolia) constitutively expressing the Arabidopsis thaliana DXR gene, a clear correlation between transcript accumulation and monoterpene production cannot be established. The DXR enzyme does not play a crucial role in the synthesis of plastidial monoterpene precursors
additional information
two substrate-binding domains, LPADSEHSAI and NKGLEVIEAHY, locate in its mid-region of the enzyme molecule, which is highly homologous to DXRs from other plants and similar to the DXR from Escherichia coli
additional information
-
two substrate-binding domains, LPADSEHSAI and NKGLEVIEAHY, locate in its mid-region of the enzyme molecule, which is highly homologous to DXRs from other plants and similar to the DXR from Escherichia coli
additional information
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role of the nonreacting phosphorylmethyl group in catalysis, overview
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,2-dideoxy-D-threo-3-hexulose 6-phosphate + NADPH + H+
2-C-ethyl-D-erythritol 4-phosphate + NADP+
-
i.e. 1-methyl-1-deoxy-D-xylulose 5-phosphate or M-DXP, a substrate analogue whichis inactive with the wild-type but active with mutant W204F
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-
?
1-deoxy-D-xylulose 5-phosphate + NAD(P)H + H+
2-C-methyl-D-erythritol 4-phosphate + NAD(P)+
1-deoxy-D-xylulose-5-phosphate + NADH
methyl-D-erythritol-4-phosphate + NAD+
-
-
-
-
r
1-deoxy-L-erythrulose + NADPH + H+
? + NADP+
-
reaction of the truncated substrate 1-deoxy-L-erythrulose in the presence and absence of phosphite dianion, overview
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-
?
methyl-D-erythritol-4-phosphate + NADP+
1-deoxy-D-xylulose-5-phosphate + NADPH
-
-
-
-
r
1-deoxy-D-xylulose 5-phosphate + NAD(P)H + H+
2-C-methyl-D-erythritol 4-phosphate + NAD(P)+
the forward reaction is preferred
-
-
r
1-deoxy-D-xylulose 5-phosphate + NAD(P)H + H+
2-C-methyl-D-erythritol 4-phosphate + NAD(P)+
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inverse secondary kinetic isotope effects for both 3-[2H] and 4-[2H]-D-1-deoxyxylulose-5-phosphate during DXR-catalyzed isomerization indicates that the enzyme operates through a retro-aldol/aldol mechanism
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-
?
1-deoxy-D-xylulose 5-phosphate + NAD(P)H + H+
2-C-methyl-D-erythritol 4-phosphate + NAD(P)+
-
-
-
-
?
1-deoxy-D-xylulose 5-phosphate + NAD(P)H + H+
2-C-methyl-D-erythritol 4-phosphate + NAD(P)+
NADPH is the preferred cofactor
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
second committed step in isopentenyl diphosphate biosynthesis via the plastidial nonmevalonate pathway of isoprenoid biosynthesis, overview
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
second step of the deoxyxylulose 5-phosphate/methylerythritol 4-phosphate pathway with end product isopentenylphosphate
-
-
r
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
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ir
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
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ir
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
ir
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
ir
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
ir
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
-
r
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
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involved in the biosynthesis of isopentenylphosphate
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-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
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key enzyme in the bacterial nonmevalonate pathway to terpenoids, DXR introduces the key branching structure required for the eventual production of isopentenyl diphosphate
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-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
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i.e. DXP
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?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
i.e. DXP
-
-
r
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
the enzyme catalyzes the second committed step in the 2C-methyl-D-erythritol 4-phosphate pathway for biosynthesis of isopentenyl diphosphate
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
ir
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
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ir
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
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first committed step in the mevalonate-independent isopentenyl diphosphate biosynthetic pathway, overview
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r
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
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second step of the deoxyxylulose 5-phosphate/methylerythritol 4-phosphate pathway with end product isopentenylphosphate
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-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
the forward direction is preferred
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r
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
NADPH and 2-C-methyl-D-erythritol 4-phosphate bind to the free enzyme and the two bind together to generate a nonproductive ternary complex
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
first committed step in the mevalonate-independent isopentenyl diphosphate biosynthetic pathway, overview
-
-
r
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
the forward direction is preferred
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r
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
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?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
second step of the deoxyxylulose 5-phosphate/methylerythritol 4-phosphate pathway with end product isopentenylphosphate
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
ir
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
second step of the deoxyxylulose 5-phosphate/methylerythritol 4-phosphate pathway with end product isopentenylphosphate, overview
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
the enzyme catalyzes the first committed step in the biosynthesis of isopentenyl diphosphate in the plastidial 2C-methyl-D-erythritol 4-phosphate pathway leading to production of forskolin, overview
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
ir
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
second step of the methylerythritol 4-phosphate pathway
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
step in the methylerythritol 4-phosphate pathway
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
i.e. DXP
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
ir
1-deoxy-D-xylulose-5-phosphate + NADPH
methyl-D-erythritol-4-phosphate + NADP+
-
-
-
-
?
1-deoxy-D-xylulose-5-phosphate + NADPH
methyl-D-erythritol-4-phosphate + NADP+
-
-
-
-
r
1-deoxy-D-xylulose-5-phosphate + NADPH
methyl-D-erythritol-4-phosphate + NADP+
-
-
-
-
r
1-deoxy-D-xylulose-5-phosphate + NADPH
methyl-D-erythritol-4-phosphate + NADP+
-
-
-
-
?
1-fluoro-1-deoxy-D-xylulose 5-phosphate + NADPH
?
-
i.e. CF-DXP, results in about 25% of the activity with 1-deoxy-D-xylulose 5-phosphate
-
-
r
2C-methyl-D-erythritol 4-phosphate + 2C-methyl-D-erythritol 4-phosphate + NADP+
? + NADPH
-
in reaction mixtures containing 0.15–0.25 mM IspC from Escherichia coli, Mycobacterium tuberculosis or Arabidopsis thaliana, the reversible reaction can be followed over thousands of reaction cycles. No fragment exchange, and the frequency of exchange, if any, is less than 5 p.p.m. per catalytic cycle
-
-
r
2C-methyl-D-erythritol 4-phosphate + 2C-methyl-D-erythritol 4-phosphate + NADP+
? + NADPH
-
in reaction mixtures containing 0.15-0.25 mM IspC from Escherichia coli, Mycobacterium tuberculosis or Arabidopsis thaliana, the reversible reaction can be followed over thousands of reaction cycles. No fragment exchange, and the frequency of exchange, if any, is less than 5 p.p.m. per catalytic cycle
-
-
r
2C-methyl-D-erythritol 4-phosphate + 2C-methyl-D-erythritol 4-phosphate + NADP+
? + NADPH
-
in reaction mixtures containing 0.15-0.25 mM IspC from Escherichia coli, Mycobacterium tuberculosis or Arabidopsis thaliana, the reversible reaction can be followed over thousands of reaction cycles. No fragment exchange, and the frequency of exchange, if any, is less than 5 p.p.m. per catalytic cycle
-
-
r
2C-methyl-D-erythritol 4-phosphate + hydroxyacetone + NADP+
? + NADPH
-
reaction mixtures containing 0.23-0.25 mM IspC from Escherichia coli, Mycobacterium tuberculosis or Arabidopsis thaliana
-
-
?
2C-methyl-D-erythritol 4-phosphate + hydroxyacetone + NADP+
? + NADPH
-
reaction mixtures containing 0.23-0.25 mM IspC from Escherichia coli, Mycobacterium tuberculosis or Arabidopsis thaliana
-
-
?
2C-methyl-D-erythritol 4-phosphate + hydroxyacetone + NADP+
? + NADPH
-
reaction mixtures containing 0.23-0.25 mM IspC from Escherichia coli, Mycobacterium tuberculosis or Arabidopsis thaliana
-
-
?
glycolaldehyde phosphate + hydroxyacetone + NADPH
? + NADP+
-
reaction mixtures containing 0.21-0.34 mM IspC from Escherichia coli, Mycobacterium tuberculosis or Arabidopsis thaliana
-
-
?
glycolaldehyde phosphate + hydroxyacetone + NADPH
? + NADP+
-
reaction mixtures containing 0.21-0.34 mM IspC from Escherichia coli, Mycobacterium tuberculosis or Arabidopsis thaliana
-
-
?
glycolaldehyde phosphate + hydroxyacetone + NADPH
? + NADP+
-
reaction mixtures containing 0.21-0.34 mM IspC from Escherichia coli, Mycobacterium tuberculosis or Arabidopsis thaliana
-
-
?
additional information
?
-
participation in the control of the 2-C-methyl-D-erythritol 4-phosphate pathway
-
-
-
additional information
?
-
-
IspC does not catalyze the isomerisation of 1-deoxy-D-xylulose 5-phosphate to give 1-deoxy-L-ribulose 5-phosphate. Active site of IspC is located close to the surface, a flexible loop at the active site (amino acids 206–216) is able to fold into at least three different conformations
-
-
-
additional information
?
-
-
used for the synthesis of [1-13C1]2C-methyl-D-erythritol 4-phosphate and [3-13C1]2C-methyl-D-erythritol 4-phosphate
-
-
-
additional information
?
-
-
reaction depends on NADPH although it does not involve a reduction step, putative aldehyde intermediate is converted to methyl-D-erythritol-4-phosphate in the presence of NADPH and to 1-deoxy-D-xylolose-5-phosphate in the presence of NADP+
-
-
-
additional information
?
-
-
1,1,1-trifluoro-1-deoxy-D-xylulose 5-phosphoric acid, 1,1-difluoro-1-deoxy-D-xylulose 5-phosphoric acid, and 1,2-dideoxy-D-hexulose 6-phosphate are poor substrates
-
-
-
additional information
?
-
-
IspC does not catalyze the isomerisation of 1-deoxy-D-xylulose 5-phosphate to give 1-deoxy-L-ribulose 5-phosphate. Active site of IspC is located close to the surface, a flexible loop at the active site (amino acids 206-216) is able to fold into at least three different conformations
-
-
-
additional information
?
-
C3-C4 substrate binding mode in which DXP chelates a DXR-bound divalent cation via its hydroxyl groups at C3 and C4. The conversion of 1-deoxy-D-xylulose 5-phosphate to 2-methyl-D-erythritol 4-phosphate max include a pseudo-single molecule transition state of the retro-aldol intermediates
-
-
-
additional information
?
-
C3-C4 substrate binding mode in which DXP chelates a DXR-bound divalent cation via its hydroxyl groups at C3 and C4. The conversion of 1-deoxy-D-xylulose 5-phosphate to 2-methyl-D-erythritol 4-phosphate max include a pseudo-single molecule transition state of the retro-aldol intermediates
-
-
-
additional information
?
-
-
DXR has rate-limiting roles in isopentenyl diphosphate and dimethylallyl diphosphate synthesis
-
-
-
additional information
?
-
-
IspC does not catalyze the isomerisation of 1-deoxy-D-xylulose 5-phosphate to give 1-deoxy-L-ribulose 5-phosphate. Active site of IspC is located close to the surface, a flexible loop at the active site (amino acids 206-216) is able to fold into at least three different conformations
-
-
-
additional information
?
-
-
development and evaluation of a high-throughput screening assay for simultaneous selection of inhibitors of the enzyme, overview
-
-
-
additional information
?
-
DXR is involved in the 2-C-methyl-D-erythritol 4-phosphate pathway
-
-
-
additional information
?
-
-
DXR is involved in the 2-C-methyl-D-erythritol 4-phosphate pathway
-
-
-
additional information
?
-
DXR can accelerate the biosynthesis of lycopene. DXR is an effective regulatory site for the synthesis and accumulation of diterpenoid compounds such as tanshinone
-
-
-
additional information
?
-
-
substrate synthesis and product identification method, overview
-
-
-
additional information
?
-
-
a retroaldol/aldol mechanism for the DXR catalyzed rearrangement of 1-deoxy-D-xylulose 5-phosphate to 2-C-methyl-D-erythritol 4-phosphate. DXR first cleaves the C3-C4 bond of 1-deoxy-D-xylulose 5-phosphate in a retroaldol manner to generate a three-carbon and a two-carbon phosphate bimolecular intermediate. These two species are then reunited by an aldol reaction to form a new C-C bond, yielding the same aldehyde intermediate methylerythrose phosphate. Subsequent reduction of methylerythrose phosphate by NADPH affords 2-C-methyl-D-erythritol 4-phosphate
-
-
-
additional information
?
-
-
mono-((2S,3S)-3-fluoromethyl-2,4-dihydroxy-3-methyl-butyl) ester is not a substrate for DXR
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
Q9XFS9
participation in the control of the 2-C-methyl-D-erythritol 4-phosphate pathway
-
-
-
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
Q9XFS9
second committed step in isopentenyl diphosphate biosynthesis via the plastidial nonmevalonate pathway of isoprenoid biosynthesis, overview
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
Q9XFS9
second step of the deoxyxylulose 5-phosphate/methylerythritol 4-phosphate pathway with end product isopentenylphosphate
-
-
r
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
ir
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
ir
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
ir
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
ir
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
P45568
-
-
ir
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
-
r
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
involved in the biosynthesis of isopentenylphosphate
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
key enzyme in the bacterial nonmevalonate pathway to terpenoids, DXR introduces the key branching structure required for the eventual production of isopentenyl diphosphate
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
Q5J7B3
the enzyme catalyzes the second committed step in the 2C-methyl-D-erythritol 4-phosphate pathway for biosynthesis of isopentenyl diphosphate
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
ir
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
ir
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
first committed step in the mevalonate-independent isopentenyl diphosphate biosynthetic pathway, overview
-
-
r
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
second step of the deoxyxylulose 5-phosphate/methylerythritol 4-phosphate pathway with end product isopentenylphosphate
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
first committed step in the mevalonate-independent isopentenyl diphosphate biosynthetic pathway, overview
-
-
r
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
second step of the deoxyxylulose 5-phosphate/methylerythritol 4-phosphate pathway with end product isopentenylphosphate
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
ir
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
O96693
second step of the deoxyxylulose 5-phosphate/methylerythritol 4-phosphate pathway with end product isopentenylphosphate, overview
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
Q6R3F4
the enzyme catalyzes the first committed step in the biosynthesis of isopentenyl diphosphate in the plastidial 2C-methyl-D-erythritol 4-phosphate pathway leading to production of forskolin, overview
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
ir
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
second step of the methylerythritol 4-phosphate pathway
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
step in the methylerythritol 4-phosphate pathway
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
C6G1Y8
-
-
-
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
-
-
ir
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
-
NADPH has a vital role in tight binding of the inhibitor fosmidomycin within the enzyme active site
NADPH
sequence contains a highly conserved NADPH-binding motif in the N-terminal region
NADPH
the NADPH-binding domains are critical to the catalytic activity of DXR. Two highly conserved NADPH-binding domains, GSTGSIGT and LAAGSNV, locate in the N-terminal region of AvDXR
NADPH
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
activates, a divalent cation is required for activity, can partially substitute for Mn2+
Co2+
Mg2+
Mn2+
Zn2+
activates, a divalent cation is required for activity, can partially substitute for Mn2+
additional information
Co2+
activates, a divalent cation is required for activity, can partially substitute for Mn2+
Mg2+
a divalent cation is absolutely required, optimal at 10 mM, the enzyme prefers Mn2+ or Mg2+
Mg2+
activates, a divalent cation is required for activity, can partially substitute for Mn2+
Mg2+
-
a divalent metal ion is absolutely required for activity, involved in catalysis
Mn2+
a divalent cation is absolutely required, the enzyme prefers Mn2+ or Mg2+
Mn2+
activates, a divalent cation is required for activity, best cation, can partially be substituted by other divalent cations
Mn2+
-
a divalent metal ion is absolutely required for activity, involved in catalysis
additional information
-
Mn2+, Ca2+, Co2+, Zn2+, and Fe2+ ions are unable to support activity
additional information
-
divalent cations required for acitvity, activity decreases in the following order: Co2+, Mn2+, Mg2+, Ba2+, Ca2+, Cu2+
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2R,3R)-4-amino-2,3-dihydroxybutyl dihydrogen phosphate
-
very weak inhibitor, IC50: 5 mM, above
(2R,3S)-2,3-dihydroxy-4-(hydroxyamino)-4-oxobutyl dihydrogen phosphate
-
very weak inhibitor, IC50: 5 mM, above
(2R,3S)-4-amino-2,3-dihydroxy-4-oxobutyl dihydrogen phosphate
-
IC50: 0.253 mM
(3-(N-hydroxyacetamido)-1-phenyl)propylphosphonic acid
-
92% inhibition at 0.1 mM
1,1,1-trifluoro-1-deoxy-D-xylulose 5-phosphoric acid
-
i.e. CF3-DXP, very low inhibition
1,1-difluoro-1-deoxy-D-xylulose 5-phosphoric acid
-
i.e. CF2-DXP, very low inhibition
2-[(5Z)-5-(3,4-dihydroxybenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]-N-hydroxyacetamide
inhibitor keeps its inhibition capacity in the presence of Triton X-100 and shows antimicrobial activity against Escherichia coli
3-(N-hydroxyacetamido)-1-(3,4-dichlorophenyl)propylphosphonic acid
-
-
3-(N-hydroxyformamido)-1-(2-bromophenyl)propylphosphonic acid
-
93% inhibition at 0.1 mM
3-(N-hydroxyformamido)-1-(3,4-dichlorophenyl)propylphosphonic acid
-
-
diethyl (1-(3,4-dichlorophenyl)-3-(N-hydroxyacetamido)propyl)phosphonate
-
-
diethyl (1-(3,4-dichlorophenyl)-3-(N-hydroxyformamido)propyl)phosphonate
-
-
diethyl (3-[[3-(hydroxymethyl)phenyl]amino]-3-oxopropyl)phosphonate
-
17.9% inhibition
diethyl [3-[(3-hydroxyphenyl)amino]-3-oxopropyl]phosphonate
-
33.5% inhibition
diethyl [3-[(3-methoxyphenyl)amino]-3-oxopropyl]phosphonate
-
14.1% inhibition
ethyl hydrogen [1-(3,4-dichlorophenyl)-3-[formyl(hydroxy)amino]propyl]phosphonate
-
-
ethyl hydrogen [3-[acetyl(hydroxy)amino]-1-(3,4-dichlorophenyl)propyl]phosphonate
-
-
ethyl hydrogen [3-[acetyl(hydroxy)amino]-1-[2-(pyridin-3-yl)phenyl]propyl]phosphonate
-
20% inhibition at 0.1 mM
fosmidomycin analogues
-
synthesis, stereochemistry, and analysis of inhibitory potency of several fosmidomycin analogues, overview
-
gallocatechin gallate
-
completely suppresses the activity of DXR at 100 microM, and shows around 50% DXR inhibition at 25 microM
N-hydroxy-N-[2-(3-hydroxy-3-oxido-3,4-dihydro-1H-2,3-benzoxaphosphinin-4-yl)ethyl]acetamide
-
12% inhibition at 0.1 mM
phosphate mono-((2S,3S)-3-fluoromethyl-2,4-dihydroxy-3-methyl-butyl) ester
-
is a weak competitive inhibitor of DXR, most likely due to the steric hindrance caused by the substitution of a fluoromethylgroup for a hydroxyl group. Is not an irreversible inactivator (suicide inhibitor) for DXR, fails to act as a mechanism-based inactivator if the retroaldol/aldol mechanism is operative
theaflavin-3'-gallate
-
non-competitive against 1-deoxy-D-xylulose 5-phosphate and un-competitive inhibitors with respect to NADPH
theaflavin-3,3'-digallate
-
non-competitive against 1-deoxy-D-xylulose 5-phosphate and un-competitive inhibitors with respect to NADPH
theaflavin-3-gallate
-
non-competitive against 1-deoxy-D-xylulose 5-phosphate and un-competitive inhibitors with respect to NADPH
[(1-isoquinolinylamino)methylene]-1,1-bisphosphonate
-
50% inhibition at 0.004 mM
[(5Z)-5-(3,4-dihydroxybenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
inhibitor keeps its inhibition capacity in the presence of Triton X-100
[3-(acetyl(hydroxy)amino)propyl]phosphonic acid mono(2-naphthalen-1-yl-ethyl) ester
-
-
[3-(acetyl(hydroxy)amino)propyl]phosphonic acid mono(2-naphthalen-2-yl-ethyl) ester
-
-
[3-[acetyl(hydroxy)amino]-1-(2-bromophenyl)propyl]phosphonic acid
-
38% inhibition at 0.1 mM
[3-[acetyl(hydroxy)amino]-1-(2-cyanophenyl)propyl]phosphonic acid
-
30% inhibition at 0.1 mM
[3-[acetyl(hydroxy)amino]-1-(2-methylphenyl)propyl]phosphonic acid
-
55% inhibition at 0.1 mM
[3-[acetyl(hydroxy)amino]-1-[2-(2-hydroxyethyl)phenyl]propyl]phosphonic acid
-
35% inhibition at 0.1 mM
[3-[acetyl(hydroxy)amino]-1-[2-(hydroxymethyl)phenyl]propyl]phosphonic acid
-
36% inhibition at 0.1 mM
[3-[acetyl(hydroxy)amino]-1-[2-(methoxymethyl)phenyl]propyl]phosphonic acid
-
30% inhibition at 0.1 mM
[3-[acetyl(hydroxy)amino]-1-[2-(pyridin-3-yl)phenyl]propyl]phosphonic acid
-
20% inhibition at 0.1 mM
[3-[acetyl(hydroxy)amino]-1-[2-(thiophen-2-yl)phenyl]propyl]phosphonic acid
-
30% inhibition at 0.1 mM
[3-[acetyl(naphthalen-2-ylmethoxy)amino]propyl]phosphonic acid
compound binds to both the NADPH and DXP sites, while whole-cell inhibitory activity is relatively poor
[3-[hydroxy(3-phenylpropanoyl)amino]propyl]phosphonic acid
-
compound binds to Dxr via a non-bisubstrate mechanism. The diethyl ester of [3-[hydroxy(3-phenylpropanoyl)amino]propyl]phosphonic acid inhibits Mycobacterium tuberculosis growth
[[(5-chloro-2-pyridinyl)amino]methylene]-1,1-bisphosphonate
-
50% inhibition at 0.007 mM
(4-[[3-(hydroxymethyl)phenyl]amino]-4-oxobutyl)phosphonic acid
-
26.8% inhibition
1,2-dideoxy-D-threo-3-hexulose 6-phosphate
-
weak, competitive inhibition, a highly conserved tryptophan residue in the flexible loop is blocked by the substrate analog
1-hydroxy-5-phenylpyridin-2(1H)-one
-
minimal inhibitory concentration for growth 0.02 mM
1-hydroxy-5-phenylpyridin-2(1H)-one
-
minimal inhibitory concentration for growth 0.1 mM
1-hydroxy-5-phenylpyridin-2(1H)-one
-
minimal inhibitory concentration for growth 0.1 mM
1-hydroxy-5-phenylpyridin-2(1H)-one
-
minimal inhibitory concentration for growth 0.05 mM
3-(hydroxy([(2-phenylbutanoyl)amino]acetyl)amino)propylphosphonic acid
-
-
3-(hydroxy([(3-methylbutanoyl)amino]acetyl)amino)propylphosphonic acid
-
-
3-(hydroxy([(4-phenoxybutanoyl)amino]acetyl)amino)propylphosphonic acid
-
-
3-(hydroxy([(4-phenylbutanoyl)amino]acetyl)amino)propylphosphonic acid
-
-
3-[(([(3,4-dimethoxyphenyl)acetyl]amino)acetyl)(hydroxy)amino]propylphosphonic acid
-
-
3-[(([(3,4-dimethoxyphenyl)acetyl]amino)acetyl)(hydroxy)amino]propylphosphonic acid
-
-
3-[([(cyclopropylcarbonyl)amino]acetyl)(hydroxy)amino]propylphosphonic acid
-
-
3-[([(cyclopropylcarbonyl)amino]acetyl)(hydroxy)amino]propylphosphonic acid
-
-
3-[hydroxy(([3-(trifluoromethoxy)benzoyl]amino)acetyl)amino]propylphosphonic acid
-
-
3-[hydroxy(([3-(trifluoromethoxy)benzoyl]amino)acetyl)amino]propylphosphonic acid
-
-
3-[hydroxy(([4-(1H-indol-3-yl)butanoyl]amino)acetyl)amino]propylphosphonic acid
-
-
3-[hydroxy(([4-(1H-indol-3-yl)butanoyl]amino)acetyl)amino]propylphosphonic acid
-
-
4-benzylbenzene-1,2-diol
-
minimal inhibitory concentration for growth 0.2 mM
4-benzylbenzene-1,2-diol
-
minimal inhibitory concentration for growth 0.2 mM
4-benzylbenzene-1,2-diol
-
minimal inhibitory concentration for growth 0.2 mM
biphenyl-3,4-diol
-
minimal inhibitory concentration for growth 0.2 mM
diethyl (2-[[3-(hydroxymethyl)phenyl]amino]-2-oxoethyl)phosphonate
-
40.4% inhibition
diethyl [2-[(3-hydroxyphenyl)amino]-2-oxoethyl]phosphonate
-
24.4% inhibition
fosmidomycin
-
acts by binding strongly to DXR as a slow tight-binding inhibitor, inhibitor-enzyme interaction and structure analysis for design of inhibitors, possibly mimics a transition state in the reaction coordinate of the substrate, the initial rapid equilibrium is subject to negative cooperativity, overview
fosmidomycin
-
IC50: 310 nM for the forward reaction, 0.0027 mM for the reverse reaction, Gram positive bacteria, including Mycobacterium tuberculosis, are resistant against the antibiotic fosmidomycin, which is an inhibitor of the enzyme from most gram-negative bacteria and other organisms
fosmidomycin
-
a natural antibiotic from Streptomyces lavendulae, a specific, mixed type inhibitor, the N-formyl-N-hydroxy amino headgroup of fosmidomycin coordinates Mg2+ ion forming an octahedral complex with active site residues Asp157, Glu159, and Glu241 and a critical binding site water molecule, residue His219 is essential for placing fosmidomycin in the active site for optimal catalysis, mechanism, overview, NADPH has a vital role in tight binding of the inhibitor within the enzyme active site
fosmidomycin
analysis of parasite growth in infected cultured erythrocytes. 50% growth inhibition at about 301 nM
fosmidomycin
IC50: 450 nM, recombinant enzyme, inhibition of growth and forskolin production in vivo
fosmidomycin
-
potent inhibitor but with very short half-life in plasma and low oral availability
FR900098
analysis of parasite growth in infected cultured erythrocytes. 50% growth inhibition at about 118 nM
additional information
-
1,1,1-trifluoro-1-deoxy-D-xylulose 5-phosphoric acid, 1,1-difluoro-1-deoxy-D-xylulose 5-phosphoric acid, and 1,2-dideoxy-D-hexulose 6-phosphate are poor inhibitors, most likely because of the increase in steric bulk at C1
-
additional information
-
neither the sulfone (N-hydroxy-N-[3-(alkylsulfonyl)propyl]acetamides) nor the sulfonamide derivatives (N-hydroxy-N-(3-sulfamoylpropyl) acetamide and N-hydroxy-N-(3-(N-alkylsulfamoyl)propyl)acetamide) of FR900098 display any significant inhibitory activity against DXR at a concentration of 0.03 mM. Importance of the negative charge for the binding of fosmidomycin-like inhibitors to DXR. Uncharged molecules are virtually inactive whereas derivatives that possess only one instead of two negative charges are markedly less active. It is possible to regain some of the activity that is lost by the reduction of the charge by occupation of hitherto unexploited areas of the enzyme
-
additional information
-
inhibitory potencies of a series of aryl- and heteroarylcarbamoylphosphonic acids, their diethyl esters and disodium salts as analogues of the potent DXR inhibitor fosmidomycin, effects of the carboxamide N-substituents and the length of the methylene linker, in silico docking studies, saturation transfer difference NMR spectroscopy and enzyme inhibition assays, overview. Molecular modelling and simulated docking studies. No or poor inhibition by diethyl (4-[[3-(hydroxymethyl)phenyl]amino]-4-oxobutyl)phosphonate, diethyl [5-[(3-hydroxyphenyl)amino]-5-oxopentyl]phosphonate, [3-[(3-hydroxyphenyl)amino]-3-oxopropyl]phosphonic acid, [5-[(3-bromophenyl)amino]-5-oxopentyl]phosphonic acid, diethyl [5-[(3-methoxyphenyl)amino]-5-oxopentyl]phosphonate, [4-[(3-methoxyphenyl)amino]-4-oxobutyl]phosphonic acid, [5-[(3-methoxyphenyl)amino]-5-oxopentyl]phosphonic acid, diethyl [4-[(3-bromophenyl)amino]-4-oxobutyl]phosphonate, [4-[(3-bromophenyl)amino]-4-oxobutyl]phosphonic acid, and [5-[(3-bromophenyl)amino]-5-oxopentyl]phosphonic acid
-
additional information
-
no substrate inhibition by 2-C-methyl-D-erythritol 4-phosphate, NADPH or NADP+
-
additional information
-
development and evaluation of a high-throughput screening spectrometric assay, measuring Dxr activity of Dxr coupled with 1-deoxy-D-xylulose-5-phosphate synthase, Dxs, activity, for simultaneous selection of inhibitors of the enzyme, overview
-
additional information
-
design, synthesis, and X-ray crystallographic studies of alpha-aryl 3,4-dichlorophenyl-substituted fosmidomycin analogues as enzyme inhibitors. The introduction of a 3,4-dichlorophenyl group in the Calpha-position relative to the phosphonate group produces analogues that have a higher in vitro antimalarial activity than fosmidomycin
-
additional information
-
use of the Dxr-fosmidomycin cocrystal structure to design bisubstrate ligands to bind to both the 1-deoxy-D-xylulose-5-phosphate and NADPH sites
-
additional information
-
design and development of inhibitors, structure and docking modeling, overview
-
additional information
-
pyridine-containing fosmidomycin derivative inhibitor design and development using quantitative structure?activity relationship and crystallographic studies, synthesis, overview
-
additional information
-
inhibitory potencies of a series of aryl- and heteroarylcarbamoylphosphonic acids, their diethyl esters and disodium salts as analogues of the potent DXR inhibitor fosmidomycin, effects of the carboxamide N-substituents and the length of the methylene linker, in silico docking studies, saturation transfer difference NMR spectroscopy and enzyme inhibition assays, overview. Molecular modelling and simulated docking studies. No or poor inhibition by diethyl [3-[(3-hydroxyphenyl)amino]-3-oxopropyl]phosphonate, diethyl [2-[(3-methoxyphenyl)amino]-2-oxoethyl]phosphonate, diethyl [3-[(3-methoxyphenyl)amino]-3-oxopropyl]phosphonate, diethyl [2-[(3-bromophenyl)amino]-2-oxoethyl]phosphonate, diethyl (3-[[3-(hydroxymethyl)phenyl]amino]-3-oxopropyl)phosphonate, [4-[(3-methoxyphenyl)amino]-4-oxobutyl]phosphonic acid, and [2-[(3-cyanophenyl)amino]-2-oxoethyl]phosphonic acid
-
additional information
-
inhibitor design and synthesis, structure-activity relationship profile for the inhibition of TgDXR, overview
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
salicylic acid
strongly induces DXR in leaves, reaches the highest level after 48 h of the treatment, and gradually decreases after. Is induced by salicylic acid at least at transcriptional level
methyl jasmonate
A1XG19
strong induction, reaching the highest level after 24 h of the treatment, and gradually decreasing thereafter
additional information
-
transcript accumulation of DXR gene is regulated by mechanical wounding and fungal elicitors. Expression of the DXR gene in rubber trees is not induced by light
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.3
1,2-dideoxy-D-threo-3-hexulose 6-phosphate
-
pH 7.8, 37°C, recombinant mutant W204F
53
1-deoxy-L-erythrulose
-
pH 7.5, 25°C, recombinant enzyme in absence or presence of phosphite dianion
0.227
1-fluoro-1-deoxy-D-xylulose 5-phosphate
-
pH 7.6, 37°C, recombinant enzyme
0.0471
1-deoxy-D-xylulose 5-phosphate
-
pH 7.9, 30°C, recombinant His-tagged enzyme
0.081
1-deoxy-D-xylulose 5-phosphate
-
pH 7.6, 37°C, recombinant His-tagged enzyme
0.115
1-deoxy-D-xylulose 5-phosphate
-
pH 7.5, 25°C, recombinant enzyme
0.132
1-deoxy-D-xylulose 5-phosphate
pH 8.0, 37°C, recombinant pseudomature enzyme
0.147
1-deoxy-D-xylulose 5-phosphate
pH 8.0, 37°C, recombinant enzyme
0.17
1-deoxy-D-xylulose 5-phosphate
-
pH 7.8, 37°C, recombinant wild-type enzyme
0.42
1-deoxy-D-xylulose 5-phosphate
-
pH 7.8, 37°C, recombinant mutant W204F
2.9
1-deoxy-D-xylulose 5-phosphate
-
pH 7.8, 37°C, recombinant mutant W204L
0.004
1-deoxy-D-xylulose-5-phosphate
-
cosubstrate NADPH, presence of Co2+, pH 7.5, 25°C
0.042
1-deoxy-D-xylulose-5-phosphate
-
cosubstrate NADPH, presence of Mg2+, pH 7.5, 25°C
0.05
1-deoxy-D-xylulose-5-phosphate
-
cosubstrate NADH, presence of Co2+, pH 7.5, 25°C
0.1
1-deoxy-D-xylulose-5-phosphate
-
cosubstrate NADPH, presence of Mn2+, pH 7.5, 25°C
0.21
1-deoxy-D-xylulose-5-phosphate
-
cosubstrate NADH, presence of Mg2+, pH 7.5, 25°C
0.24
1-deoxy-D-xylulose-5-phosphate
-
cosubstrate NADH, presence of Mn2+, pH 7.5, 25°C
0.084
2-C-methyl-D-erythritol 4-phosphate
-
pH 7.5, 25°C, recombinant enzyme
0.174
2-C-methyl-D-erythritol 4-phosphate
-
pH 7.9, 30°C, recombinant His-tagged enzyme
0.972
2-C-methyl-D-erythritol 4-phosphate
pH 8.0, 37°C, recombinant pseudomature enzyme
0.042
methyl-D-erythritol-4-phosphate
-
presence of Mg2+, pH 7.5, 25°C
0.42
NADP+
-
pH 7.5, 25°C, recombinant enzyme, with substrate 1-deoxy-D-xylulose 5-phosphate
0.0098
NADPH
-
pH 7.5, 25°C, recombinant enzyme, with substrate 1-deoxy-D-xylulose 5-phosphate
additional information
additional information
-
steady-state and single-turnover kinetics, primary kinetic isotope effects, overview
-
additional information
additional information
-
kinetics, recombinant His-tagged wild-type and mutant enzymes
-
additional information
additional information
-
transient kinetics and kinetic mechanism, stopped-flow fluorescence measurements, overview. Kinetics of pre-steady-state reactions and steady-state kinetics, comparison of simulated and experimental values, burst kinetics model for pre-steady-state kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.04
1,2-dideoxy-D-threo-3-hexulose 6-phosphate
-
pH 7.8, 37°C, recombinant mutant W204F
37
1-fluoro-1-deoxy-D-xylulose 5-phosphate
-
pH 7.6, 37°C, recombinant enzyme
0.16
1-deoxy-D-xylulose 5-phosphate
-
pH 7.8, 37°C, recombinant mutant W204A
0.26
1-deoxy-D-xylulose 5-phosphate
-
pH 7.8, 37°C, recombinant mutant W204L
0.54
1-deoxy-D-xylulose 5-phosphate
-
pH 7.8, 37°C, recombinant mutant W204V
4.4
1-deoxy-D-xylulose 5-phosphate
pH 8.0, 37°C, recombinant pseudomature enzyme
5.25
1-deoxy-D-xylulose 5-phosphate
-
pH 7.5, 25°C, recombinant enzyme
17
1-deoxy-D-xylulose 5-phosphate
-
pH 7.8, 37°C, recombinant wild-type enzyme
29
1-deoxy-D-xylulose 5-phosphate
-
pH 7.6, 37°C, recombinant enzyme
33
1-deoxy-D-xylulose 5-phosphate
-
pH 7.6, 37°C, recombinant His-tagged enzyme
0.00086
1-deoxy-L-erythrulose
-
pH 7.5, 25°C, recombinant enzyme in presence of phosphite dianion
0.00155
1-deoxy-L-erythrulose
-
pH 7.5, 25°C, recombinant enzyme in absence of phosphite dianion
0.95
2-C-methyl-D-erythritol 4-phosphate
-
pH 7.5, 25°C, recombinant enzyme
1.6
2-C-methyl-D-erythritol 4-phosphate
pH 8.0, 37°C, recombinant pseudomature enzyme
0.95
NADP+
-
pH 7.5, 25°C, recombinant enzyme, with substrate 1-deoxy-D-xylulose 5-phosphate
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
11.3
2-C-methyl-D-erythritol 4-phosphate
-
pH 7.5, 25°C, recombinant enzyme
5.7
NADP+
-
pH 7.5, 25°C, recombinant enzyme, with substrate 1-deoxy-D-xylulose 5-phosphate
540
NADPH
-
pH 7.5, 25°C, recombinant enzyme, with substrate 1-deoxy-D-xylulose 5-phosphate
46
1-deoxy-D-xylulose 5-phosphate
-
pH 7.5, 25°C, recombinant enzyme
0.0000292
1-deoxy-L-erythrulose
-
pH 7.5, 25°C, recombinant enzyme in absence of phosphite dianion
0.000163
1-deoxy-L-erythrulose
-
pH 7.5, 25°C, recombinant enzyme in presence of phosphite dianion
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0041
(pyridin-2-ylmethyl)phosphonic acid
-
pH 7.6, 30°C, recombinant enzyme
2
1,1,1-trifluoro-1-deoxy-D-xylulose 5-phosphoric acid
-
pH 7.6, 37°C, recombinant enzyme
3.4
1,1-difluoro-1-deoxy-D-xylulose 5-phosphoric acid
-
pH 7.6, 37°C, recombinant enzyme
0.63
1,2-dideoxy-D-threo-3-hexulose 6-phosphate
-
pH 7.8, 37°C, recombinant wild-type enzyme
1.1
1-deoxy-D-xylulose 5-phosphate
-
pH 7.9, 30°C, recombinant His-tagged enzyme
0.0224
4-benzylbenzene-1,2-diol
-
pH not specified in the publication, temperature not specified in the publication
0.0447
biphenyl-3,4-diol
-
pH not specified in the publication, temperature not specified in the publication
0.000002
phosphoric acid mono-[2-(N-acetyl-N-hydroxy-amino)-ethyl]-ester
-
pH 7.5, 37°C
0.0021
[(5-phenylpyridin-2-yl)methyl]phosphonic acid
-
pH 7.6, 30°C, recombinant enzyme
0.000077
[1-(3,4-dichlorophenyl)-3-[formyl(hydroxy)amino]propyl]phosphonic acid
-
pH 7.6, 30°C, recombinant enzyme
0.00022
[3-[acetyl(hydroxy)amino]-1-(3,4-dichlorophenyl)propyl]phosphonic acid
-
pH 7.6, 30°C, recombinant enzyme
0.0014
1-hydroxy-5-phenylpyridin-2(1H)-one
-
pH not specified in the publication, temperature not specified in the publication
0.0256
1-hydroxy-5-phenylpyridin-2(1H)-one
-
pH 7.6, 30°C, recombinant enzyme
0.000034
fosmidomycin
-
pH 7.5, 22°C, IC50 versus proliferation of Plasmodium falciparum strain Dd2
0.000085
fosmidomycin
pH 8.0, 37°C, recombinant pseudomature enzyme
0.0222
theaflavin-3'-gallate
-
substrate 1-deoxy-D-xylulose 5-phosphate, pH 7.4, 37°C
0.0133
theaflavin-3,3'-digallate
-
substrate 1-deoxy-D-xylulose 5-phosphate, pH 7.4, 37°C
0.03
theaflavin-3-gallate
-
substrate 1-deoxy-D-xylulose 5-phosphate , pH 7.4, 37°C
0.0000019
[3-[acetyl(hydroxy)amino]-1-(pyridin-3-yl)propyl]phosphonic acid
-
pH 7.5, 22°C
0.000042
[3-[acetyl(hydroxy)amino]-1-(pyridin-3-yl)propyl]phosphonic acid
-
pH 7.5, 22°C, IC50 versus proliferation of Plasmodium falciparum strain Dd5
0.00097
[3-[acetyl(hydroxy)amino]-1-(pyridin-3-yl)propyl]phosphonic acid
-
pH 7.6, 30°C, recombinant enzyme
0.000013
[3-[acetyl(hydroxy)amino]-1-(pyridin-4-yl)propyl]phosphonic acid
-
pH 7.5, 22°C
0.000082
[3-[acetyl(hydroxy)amino]-1-(pyridin-4-yl)propyl]phosphonic acid
-
pH 7.5, 22°C, IC50 versus proliferation of Plasmodium falciparum strain Dd6
0.00053
[3-[acetyl(hydroxy)amino]-1-(pyridin-4-yl)propyl]phosphonic acid
-
pH 7.6, 30°C, recombinant enzyme
0.000085
[3-[acetyl(hydroxy)amino]-1-phenylpropyl]phosphonic acid
-
pH 7.5, 22°C
0.00093
[3-[acetyl(hydroxy)amino]-1-phenylpropyl]phosphonic acid
-
pH 7.5, 22°C, IC50 versus proliferation of Plasmodium falciparum strain Dd8
0.000013
[3-[formyl(hydroxy)amino]-1-(pyridin-3-yl)propyl]phosphonic acid
-
pH 7.5, 22°C
0.000055
[3-[formyl(hydroxy)amino]-1-(pyridin-3-yl)propyl]phosphonic acid
-
pH 7.6, 30°C, recombinant enzyme
0.000087
[3-[formyl(hydroxy)amino]-1-(pyridin-3-yl)propyl]phosphonic acid
-
pH 7.5, 22°C, IC50 versus proliferation of Plasmodium falciparum strain Dd3
0.0000089
[3-[formyl(hydroxy)amino]-1-(pyridin-4-yl)propyl]phosphonic acid
-
pH 7.5, 22°C
0.000035
[3-[formyl(hydroxy)amino]-1-(pyridin-4-yl)propyl]phosphonic acid
-
pH 7.5, 22°C, IC50 versus proliferation of Plasmodium falciparum strain Dd4
0.000079
[3-[formyl(hydroxy)amino]-1-(pyridin-4-yl)propyl]phosphonic acid
-
pH 7.6, 30°C, recombinant enzyme
0.00048
[3-[formyl(hydroxy)amino]-1-phenylpropyl]phosphonic acid
-
pH 7.5, 22°C
0.0015
[3-[formyl(hydroxy)amino]-1-phenylpropyl]phosphonic acid
-
pH 7.5, 22°C, IC50 versus proliferation of Plasmodium falciparum strain Dd7
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5
(2R,3R)-4-amino-2,3-dihydroxybutyl dihydrogen phosphate
Escherichia coli
-
very weak inhibitor, IC50: 5 mM, above
5
(2R,3S)-2,3-dihydroxy-4-(hydroxyamino)-4-oxobutyl dihydrogen phosphate
Escherichia coli
-
very weak inhibitor, IC50: 5 mM, above
0.253
(2R,3S)-4-amino-2,3-dihydroxy-4-oxobutyl dihydrogen phosphate
Escherichia coli
-
IC50: 0.253 mM
0.0013
(3-(hydroxy[(pentafluorophenyl)carbonyl]amino)propyl)phosphonic acid
Escherichia coli
-
pH 7.5, 30°C
0.0074
(3-(N-hydroxyacetamido)-1-phenyl)propylphosphonic acid
Mycobacterium tuberculosis
-
pH 7,5, 22°C
0.0054
(3-[hydroxy(5-oxohexanoyl)amino]propyl)phosphonic acid
Escherichia coli
-
pH 7.5, 30°C
0.0051
(3-[hydroxy(6-phenylhexanoyl)amino]propyl)phosphonic acid
Escherichia coli
-
pH 7.5, 30°C
0.0038 - 0.0061
2-[(5Z)-5-(3,4-dihydroxybenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]-N-hydroxyacetamide
0.0007
3-(N-hydroxyacetamido)-1-(3,4-dichlorophenyl)propylphosphonic acid
Mycobacterium tuberculosis
-
pH 7,5, 22°C
0.0056
3-(N-hydroxyformamido)-1-(2-bromophenyl)propylphosphonic acid
Mycobacterium tuberculosis
-
pH 7,5, 22°C
0.00015
3-(N-hydroxyformamido)-1-(3,4-dichlorophenyl)propylphosphonic acid
Mycobacterium tuberculosis
-
pH 7,5, 22°C
0.012 - 0.014
3-[(([(3,4-dimethoxyphenyl)acetyl]amino)acetyl)(hydroxy)amino]propylphosphonic acid
0.0033 - 0.0071
3-[([(cyclopropylcarbonyl)amino]acetyl)(hydroxy)amino]propylphosphonic acid
0.0029 - 0.0051
3-[hydroxy(([3-(trifluoromethoxy)benzoyl]amino)acetyl)amino]propylphosphonic acid
0.0066 - 0.017
3-[hydroxy(([4-(1H-indol-3-yl)butanoyl]amino)acetyl)amino]propylphosphonic acid
0.1
diethyl (1-(3,4-dichlorophenyl)-3-(N-hydroxyacetamido)propyl)phosphonate
Mycobacterium tuberculosis
-
above, pH 7,5, 22°C
0.1
diethyl (1-(3,4-dichlorophenyl)-3-(N-hydroxyformamido)propyl)phosphonate
Mycobacterium tuberculosis
-
above, pH 7,5, 22°C
0.038
ethyl hydrogen [1-(3,4-dichlorophenyl)-3-[formyl(hydroxy)amino]propyl]phosphonate
Mycobacterium tuberculosis
-
pH 7,5, 22°C
0.022
ethyl hydrogen [3-[acetyl(hydroxy)amino]-1-(3,4-dichlorophenyl)propyl]phosphonate
Mycobacterium tuberculosis
-
pH 7,5, 22°C
0.0031 - 0.0044
[(5Z)-5-(3,4-dihydroxybenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
0.0021
[3-(acetyl(hydroxy)amino)propyl]phosphonic acid 3-methylbutyl ester
Escherichia coli
-
at 0.03 mM
0.0024
[3-(acetyl(hydroxy)amino)propyl]phosphonic acid mono(2-naphthalen-1-yl-ethyl) ester
Escherichia coli
-
at 0.03 mM
0.0016
[3-(acetyl(hydroxy)amino)propyl]phosphonic acid mono(2-naphthalen-2-yl-ethyl) ester
Escherichia coli
-
at 0.03 mM
0.0039
[3-(acetyl(hydroxy)amino)propyl]phosphonic acid mono-n-butyl ester
Escherichia coli
-
at 0.03 mM
0.016
[3-(acetyl(hydroxy)amino)propyl]phosphonic acid mono-n-propyl ester
Escherichia coli
-
at 0.03 mM
0.05
[3-(acetyl(hydroxy)amino)propyl]phosphonic acid monomethyl ester
Escherichia coli
-
at 0.03 mM
0.00049
[3-(acetyl(hydroxy)amino)propyl]phosphonic acid monophenethyl ester
Escherichia coli
-
at 0.03 mM
0.023
[3-(acetyl(hydroxy)amino)propyl]phosphonic monoethyl ester
Escherichia coli
-
at 0.03 mM
0.21
[3-[acetyl(hydroxy)amino]-1-(2-bromophenyl)propyl]phosphonic acid
Mycobacterium tuberculosis
-
pH 7,5, 22°C
0.205
[3-[acetyl(hydroxy)amino]-1-(2-methylphenyl)propyl]phosphonic acid
Mycobacterium tuberculosis
-
pH 7,5, 22°C
0.15
[3-[acetyl(hydroxy)amino]-1-[2-(2-hydroxyethyl)phenyl]propyl]phosphonic acid
Mycobacterium tuberculosis
-
pH 7,5, 22°C
0.465
[3-[acetyl(hydroxy)amino]-1-[2-(hydroxymethyl)phenyl]propyl]phosphonic acid
Mycobacterium tuberculosis
-
pH 7,5, 22°C
0.0178
[3-[hydroxy(3-phenylpropanoyl)amino]propyl]phosphonic acid
Mycobacterium tuberculosis
-
pH not specified in the publication, temperature not specified in the publication
0.0038
2-[(5Z)-5-(3,4-dihydroxybenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]-N-hydroxyacetamide
Escherichia coli
Q1RG16
pH 7.5, 37°C
0.0061
2-[(5Z)-5-(3,4-dihydroxybenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]-N-hydroxyacetamide
Escherichia coli
Q1RG16
presence of 0.01% Triton X-100, pH 7.5, 37°C
0.0093
3-(hydroxy([(2-phenylbutanoyl)amino]acetyl)amino)propylphosphonic acid
Plasmodium falciparum
-
-
0.02
3-(hydroxy([(2-phenylbutanoyl)amino]acetyl)amino)propylphosphonic acid
Escherichia coli
-
-
0.0096
3-(hydroxy([(3-methylbutanoyl)amino]acetyl)amino)propylphosphonic acid
Plasmodium falciparum
-
-
0.012
3-(hydroxy([(3-methylbutanoyl)amino]acetyl)amino)propylphosphonic acid
Escherichia coli
-
-
0.0004
3-(hydroxy([(4-phenoxybutanoyl)amino]acetyl)amino)propylphosphonic acid
Plasmodium falciparum
-
-
0.001
3-(hydroxy([(4-phenoxybutanoyl)amino]acetyl)amino)propylphosphonic acid
Escherichia coli
-
-
0.019
3-(hydroxy([(4-phenylbutanoyl)amino]acetyl)amino)propylphosphonic acid
Escherichia coli
-
-
0.02
3-(hydroxy([(4-phenylbutanoyl)amino]acetyl)amino)propylphosphonic acid
Plasmodium falciparum
-
-
0.012
3-[(([(3,4-dimethoxyphenyl)acetyl]amino)acetyl)(hydroxy)amino]propylphosphonic acid
Plasmodium falciparum
-
-
0.014
3-[(([(3,4-dimethoxyphenyl)acetyl]amino)acetyl)(hydroxy)amino]propylphosphonic acid
Escherichia coli
-
-
0.0033
3-[([(cyclopropylcarbonyl)amino]acetyl)(hydroxy)amino]propylphosphonic acid
Plasmodium falciparum
-
-
0.0071
3-[([(cyclopropylcarbonyl)amino]acetyl)(hydroxy)amino]propylphosphonic acid
Escherichia coli
-
-
0.0029
3-[hydroxy(([3-(trifluoromethoxy)benzoyl]amino)acetyl)amino]propylphosphonic acid
Plasmodium falciparum
-
-
0.0051
3-[hydroxy(([3-(trifluoromethoxy)benzoyl]amino)acetyl)amino]propylphosphonic acid
Escherichia coli
-
-
0.0066
3-[hydroxy(([4-(1H-indol-3-yl)butanoyl]amino)acetyl)amino]propylphosphonic acid
Plasmodium falciparum
-
-
0.017
3-[hydroxy(([4-(1H-indol-3-yl)butanoyl]amino)acetyl)amino]propylphosphonic acid
Escherichia coli
-
-
0.00031
fosmidomycin
Mycobacterium tuberculosis
-
IC50: 310 nM for the forward reaction, 0.0027 mM for the reverse reaction, Gram positive bacteria, including Mycobacterium tuberculosis, are resistant against the antibiotic fosmidomycin, which is an inhibitor of the enzyme from most gram-negative bacteri
0.00044
fosmidomycin
Plasmodium falciparum
-
pH 7.5, 22°C, IC50 versus proliferation of Plasmodium falciparum strain Dd2
0.00045
fosmidomycin
Plectranthus barbatus
Q6R3F4
IC50: 450 nM, recombinant enzyme, inhibition of growth and forskolin production in vivo
0.00117
fosmidomycin
Plasmodium falciparum
-
pH 7.5, 22°C, IC50 versus proliferation of Plasmodium falciparum strain 3D7
0.0027
fosmidomycin
Mycobacterium tuberculosis
-
IC50: 310 nM for the forward reaction, 0.0027 mM for the reverse reaction, Gram positive bacteria, including Mycobacterium tuberculosis, are resistant against the antibiotic fosmidomycin, which is an inhibitor of the enzyme from most gram-negative bacteri
0.0031
[(5Z)-5-(3,4-dihydroxybenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
Escherichia coli
Q1RG16
pH 7.5, 37°C
0.0044
[(5Z)-5-(3,4-dihydroxybenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
Escherichia coli
Q1RG16
presence of 0.01% Triton X-100, pH 7.5, 37°C
0.00031
[3-[acetyl(hydroxy)amino]-1-(pyridin-3-yl)propyl]phosphonic acid
Plasmodium falciparum
-
pH 7.5, 22°C, IC50 versus proliferation of Plasmodium falciparum strain Dd2
0.00044
[3-[acetyl(hydroxy)amino]-1-(pyridin-3-yl)propyl]phosphonic acid
Plasmodium falciparum
-
pH 7.5, 22°C, IC50 versus proliferation of Plasmodium falciparum strain 3D7
0.00046
[3-[acetyl(hydroxy)amino]-1-(pyridin-4-yl)propyl]phosphonic acid
Plasmodium falciparum
-
pH 7.5, 22°C, IC50 versus proliferation of Plasmodium falciparum strain Dd2
0.00063
[3-[acetyl(hydroxy)amino]-1-(pyridin-4-yl)propyl]phosphonic acid
Plasmodium falciparum
-
pH 7.5, 22°C, IC50 versus proliferation of Plasmodium falciparum strain 3D7
0.0017
[3-[acetyl(hydroxy)amino]-1-phenylpropyl]phosphonic acid
Plasmodium falciparum
-
pH 7.5, 22°C, IC50 versus proliferation of Plasmodium falciparum strain Dd2
0.0035
[3-[acetyl(hydroxy)amino]-1-phenylpropyl]phosphonic acid
Plasmodium falciparum
-
pH 7.5, 22°C, IC50 versus proliferation of Plasmodium falciparum strain 3D7
0.00018
[3-[formyl(hydroxy)amino]-1-(pyridin-3-yl)propyl]phosphonic acid
Plasmodium falciparum
-
pH 7.5, 22°C, IC50 versus proliferation of Plasmodium falciparum strain Dd2
0.00034
[3-[formyl(hydroxy)amino]-1-(pyridin-3-yl)propyl]phosphonic acid
Plasmodium falciparum
-
pH 7.5, 22°C, IC50 versus proliferation of Plasmodium falciparum strain 3D7
0.00017
[3-[formyl(hydroxy)amino]-1-(pyridin-4-yl)propyl]phosphonic acid
Plasmodium falciparum
-
pH 7.5, 22°C, IC50 versus proliferation of Plasmodium falciparum strain Dd2
0.00018
[3-[formyl(hydroxy)amino]-1-(pyridin-4-yl)propyl]phosphonic acid
Plasmodium falciparum
-
pH 7.5, 22°C, IC50 versus proliferation of Plasmodium falciparum strain 3D7
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
quantitative analysis of forskolin production in plant tissues
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.5
7.6
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
high level of mRNA expression for 1-deoxy-D-xylulose 5-phosphate synthase and 2C-methyl-D-erythritol 4-phosphate synthase in leaf and twig
additional information
constitutive expression, not affected by wounding or fungal application
in mature plant, higher expression in leaf than in flower and latex
in mature plant, higher expression in leaf than in flower and latex
-
mRNA in young latex containing tissues, inflorescence and seedling stems, are higher than those in the latex from the tree and is barely detectable in the mature leaves
high level of mRNA expression for 1-deoxy-D-xylulose 5-phosphate synthase and 2C-methyl-D-erythritol 4-phosphate synthase in leaf and twig
in mature plant, high expression; in seedling, higher expression in stem and leaf than in root. In mature plant, higher expression in leaf than in flower and latex
in seedling, higher expression in stem and leaf than in root; in seedling, highest expression in root
cultured hairy root. Transcription level is up-regulated after exposure to hyperosmotic stress and a yeast elicitor
in seedling, higher expression in stem and leaf than in root
additional information
no expression of enzyme or 2C-methyl-D-erythritol 4-phosphate synthase in root
additional information
-
no expression of enzyme or 2C-methyl-D-erythritol 4-phosphate synthase in root
additional information
-
expressed in all photosynthetic tissues except pod wall and root
additional information
-
RIF10 and RIF1 mutants with defects in plastid RNA processing, protein accumulation, and protein degradation, accumulate higher levels of DXR
additional information
semi-quantitative RT-PCR expression pattern analysis
additional information
-
semi-quantitative RT-PCR expression pattern analysis
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
a putative chloroplast transit peptide with a conserved cleavage site of CS-M motif is located at the N-terminus of AvDXR
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sequence contains a N-terminal plastid targeting sequence, plastidial localization of green fluorescent protein fusion protein
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Dxr gene transformed into Arabidopsis cells is located in the chloroplasts. Hevea brasiliensis DXR may be expressed and localized in latex Frey-Wyssling plastid-like particles
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)