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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
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.267 1-deoxy-D-xylulose-5-phosphate reductoisomerase
IUBMB Comments
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, click here). The mechanism has been shown to be a retroaldol/aldol reaction .
The enzyme appears in viruses and cellular organisms
- 1.1.1.267
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isoprenoids
- fosmidomycin
- plasmodium
- falciparum
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antimalarial
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terpenoids
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isopentenyl
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non-mevalonate
- mevalonate
- isoprene
- phosphonate
- drug development
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dimethylallyl
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mevalonate-independent
- medicine
- biotechnology
Reaction Schemes
showSynonyms
1-deoxy-d-xylulose 5-phosphate reductoisomerase, 1-deoxy-d-xylulose-5-phosphate reductoisomerase, 1-deoxy-d-xylulose-5-phosphate, pfdxr, dxp reductoisomerase, mep synthase, cadxr, doxp reductoisomerase, deoxyxylulose 5-phosphate reductoisomerase, mtdxr, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1-deoxy-D-xylulose 5-phosphate isomeroreductase
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1-deoxy-D-xylulose 5-phosphate reductoisomerase
1-deoxy-D-xylulose-5-phosphate reductoisomerase
1-deoxyxylulose 5-phosphate reductoisomerase
1-deoxyxylulose-5-phosphate reductoisomerase
2-C-methyl-D-erythritol 4-phosphate synthase
2C-methyl-D-erythritol-4-phosphate synthase
deoxyxylulose 5-phosphate reductoisomerase
DOXP reductoisomerase
DOXP-reductoisomerase
DXP reductoisomerase
DXR
DXR1
FtIspC
IspC
MEP synthase
MtbIspC
MtDXR
Rv2870c
VvDxr
YpIspC
2-C-methyl-D-erythritol 4-phosphate synthase
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deoxyxylulose 5-phosphate reductoisomerase
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DXP 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+
mechanism
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2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH + H+
stereochemistry
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2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH + H+
reaction 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+
steady-state random mechanism
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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
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
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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+
retro-aldol/aldol mechanism
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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+
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
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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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reduction
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
methylerythritol phosphate pathway I, methylerythritol phosphate pathway II
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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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(3R,4S)-dihydroxy-5-oxohexylphosphonic acid + NADPH
? + NADP+
-
Substrates: -
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1,2-dideoxy-D-threo-3-hexulose 6-phosphate + NADPH + H+
2-C-ethyl-D-erythritol 4-phosphate + NADP+
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Substrates: 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 + NADPH
? + NADP+
-
Substrates: -
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?
1-deoxy-D-xylulose-5-phosphate + NADH
methyl-D-erythritol-4-phosphate + NAD+
-
Substrates: -
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r
1-deoxy-L-erythrulose + NADPH + H+
? + NADP+
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Substrates: reaction of the truncated substrate 1-deoxy-L-erythrulose in the presence and absence of phosphite dianion, overview
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1-fluoro-1-deoxy-D-xylulose-5-phosphate + NADPH
? + NADP+
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Substrates: -
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?
3-[2H]-D-1-deoxyxylulose-5-phosphate + NAD(P)H
? + NAD(P)+
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Substrates: -
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?
4-[2H]-D-1-deoxyxylulose-5-phosphate + NAD(P)H
? + NAD(P)+
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Substrates: -
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?
methyl-D-erythritol-4-phosphate + NADP+
1-deoxy-D-xylulose-5-phosphate + NADPH
-
Substrates: -
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r
1-deoxy-D-xylulose 5-phosphate + NAD(P)H + H+
2-C-methyl-D-erythritol 4-phosphate + NAD(P)+
Substrates: the forward reaction is preferred
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r
1-deoxy-D-xylulose 5-phosphate + NAD(P)H + H+
2-C-methyl-D-erythritol 4-phosphate + NAD(P)+
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Substrates: 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)+
-
Substrates: -
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?
1-deoxy-D-xylulose 5-phosphate + NAD(P)H + H+
2-C-methyl-D-erythritol 4-phosphate + NAD(P)+
Substrates: NADPH is the preferred cofactor
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?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
Substrates: -
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?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
Substrates: -
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?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
Substrates: second committed step in isopentenyl diphosphate biosynthesis via the plastidial nonmevalonate pathway of isoprenoid biosynthesis, overview
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?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
Substrates: second step of the deoxyxylulose 5-phosphate/methylerythritol 4-phosphate pathway with end product isopentenylphosphate
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r
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
Substrates: -
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?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
Substrates: -
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?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
Substrates: -
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?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
Substrates: -
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?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
Substrates: -
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?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
Substrates: -
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Products: -
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
Substrates: -
Products: -
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ir
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
Substrates: -
Products: -
Products: -
r
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
Substrates: -
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?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
Substrates: -
Products: -
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?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
Substrates: -
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?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
Substrates: -
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?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
Substrates: -
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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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Substrates: 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+
Substrates: 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+
-
Substrates: i.e. DXP
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1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
Substrates: i.e. DXP
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r
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
Substrates: -
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?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
Substrates: -
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?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
Substrates: -
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?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
Substrates: -
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1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
Substrates: the enzyme catalyzes the second committed step in the 2C-methyl-D-erythritol 4-phosphate pathway for biosynthesis of isopentenyl diphosphate
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1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
Substrates: -
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1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
Substrates: -
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ir
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
Substrates: -
Products: -
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?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
Substrates: -
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?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
Substrates: -
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?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
Substrates: -
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?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
Substrates: 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+
-
Substrates: 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+
-
Substrates: 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+
-
Substrates: 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
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1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
Substrates: -
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?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
Substrates: first committed step in the mevalonate-independent isopentenyl diphosphate biosynthetic pathway, overview
Products: -
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r
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
Substrates: the forward direction is preferred
Products: -
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r
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
Substrates: -
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1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
Substrates: 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+
Substrates: -
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1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
Substrates: -
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?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
Substrates: -
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Products: -
?
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
Substrates: -
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1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
Substrates: -
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1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
Substrates: -
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ir
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
Substrates: -
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1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
Substrates: -
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1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
Substrates: -
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1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
Substrates: -
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1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
Substrates: second step of the deoxyxylulose 5-phosphate/methylerythritol 4-phosphate pathway with end product isopentenylphosphate, overview
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1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
Substrates: 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
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1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
Substrates: -
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1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
Substrates: -
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1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
MH018577
Substrates: -
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1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
Substrates: -
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1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
Substrates: second step of the methylerythritol 4-phosphate pathway
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1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
Substrates: step in the methylerythritol 4-phosphate pathway
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1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
Substrates: i.e. DXP
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1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
Substrates: -
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1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
Substrates: -
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1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
Substrates: -
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1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
-
Substrates: -
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1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
Substrates: -
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1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
Substrates: i.e. DXP
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1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
Substrates: -
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1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
Substrates: i.e. DXP
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1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
Substrates: -
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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+
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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
methyl-D-erythritol-4-phosphate + NADP+
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1-deoxy-D-xylulose-5-phosphate + NADPH
methyl-D-erythritol-4-phosphate + NADP+
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1-deoxy-D-xylulose-5-phosphate + NADPH
methyl-D-erythritol-4-phosphate + NADP+
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1-deoxy-D-xylulose-5-phosphate + NADPH
methyl-D-erythritol-4-phosphate + NADP+
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1-fluoro-1-deoxy-D-xylulose 5-phosphate + NADPH
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Substrates: i.e. CF-DXP
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1-fluoro-1-deoxy-D-xylulose 5-phosphate + NADPH
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Substrates: i.e. CF-DXP, results in about 25% of the activity with 1-deoxy-D-xylulose 5-phosphate
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2C-methyl-D-erythritol 4-phosphate + 2C-methyl-D-erythritol 4-phosphate + NADP+
? + NADPH
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Substrates: in reaction mixtures containing 0.150.25 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
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2C-methyl-D-erythritol 4-phosphate + 2C-methyl-D-erythritol 4-phosphate + NADP+
? + NADPH
Substrates: 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
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2C-methyl-D-erythritol 4-phosphate + 2C-methyl-D-erythritol 4-phosphate + NADP+
? + NADPH
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Substrates: 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
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2C-methyl-D-erythritol 4-phosphate + hydroxyacetone + NADP+
? + NADPH
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Substrates: reaction mixtures containing 0.23-0.25 mM IspC from Escherichia coli, Mycobacterium tuberculosis or Arabidopsis thaliana
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2C-methyl-D-erythritol 4-phosphate + hydroxyacetone + NADP+
? + NADPH
Substrates: reaction mixtures containing 0.23-0.25 mM IspC from Escherichia coli, Mycobacterium tuberculosis or Arabidopsis thaliana
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2C-methyl-D-erythritol 4-phosphate + hydroxyacetone + NADP+
? + NADPH
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Substrates: reaction mixtures containing 0.23-0.25 mM IspC from Escherichia coli, Mycobacterium tuberculosis or Arabidopsis thaliana
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glycolaldehyde phosphate + hydroxyacetone + NADPH
? + NADP+
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Substrates: reaction mixtures containing 0.21-0.34 mM IspC from Escherichia coli, Mycobacterium tuberculosis or Arabidopsis thaliana
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glycolaldehyde phosphate + hydroxyacetone + NADPH
? + NADP+
Substrates: reaction mixtures containing 0.21-0.34 mM IspC from Escherichia coli, Mycobacterium tuberculosis or Arabidopsis thaliana
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glycolaldehyde phosphate + hydroxyacetone + NADPH
? + NADP+
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Substrates: reaction mixtures containing 0.21-0.34 mM IspC from Escherichia coli, Mycobacterium tuberculosis or Arabidopsis thaliana
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additional information
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Substrates: participation in the control of the 2-C-methyl-D-erythritol 4-phosphate pathway
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additional information
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Substrates: 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 206216) is able to fold into at least three different conformations
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additional information
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Substrates: used for the synthesis of [1-13C1]2C-methyl-D-erythritol 4-phosphate and [3-13C1]2C-methyl-D-erythritol 4-phosphate
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Substrates: 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+
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: DXR has rate-limiting roles in isopentenyl diphosphate and dimethylallyl diphosphate synthesis
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additional information
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Substrates: 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
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additional information
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Substrates: development and evaluation of a high-throughput screening assay for simultaneous selection of inhibitors of the enzyme, overview
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Substrates: DXR is involved in the 2-C-methyl-D-erythritol 4-phosphate pathway
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additional information
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Substrates: DXR is involved in the 2-C-methyl-D-erythritol 4-phosphate pathway
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additional information
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Substrates: product identification by mass spectrometry (HPLC-MS)
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