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Information on EC 1.1.1.267 - 1-deoxy-D-xylulose-5-phosphate reductoisomerase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9XFS9

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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, {terp/nonMVA}). The mechanism has been shown to be a retroaldol/aldol reaction .
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Arabidopsis thaliana
UNIPROT: Q9XFS9
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
Synonyms
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, sadxr, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1-deoxy-D-xylulose 5-phosphate reductoisomerase
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DOXP reductoisomerase
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1-deoxy-D-xylulose 5-phosphate isomeroreductase
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-
-
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2-C-methyl-D-erythritol 4-phosphate synthase
-
-
-
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2C-methyl-D-erythritol-4-phosphate synthase
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deoxyxylulose 5-phosphate reductoisomerase
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-
-
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DXP reductoisomerase
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
-
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oxidation
-
-
-
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reduction
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-
-
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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].
CAS REGISTRY NUMBER
COMMENTARY hide
210756-42-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-deoxy-D-xylulose 5-phosphate + NAD(P)H + H+
2-C-methyl-D-erythritol 4-phosphate + NAD(P)+
show the reaction diagram
the forward reaction is preferred
-
-
r
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
show the reaction diagram
2C-methyl-D-erythritol 4-phosphate + 2C-methyl-D-erythritol 4-phosphate + NADP+
? + NADPH
show the reaction diagram
-
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
show the reaction diagram
-
reaction mixtures containing 0.23-0.25 mM IspC from Escherichia coli, Mycobacterium tuberculosis or Arabidopsis thaliana
-
-
?
glycolaldehyde phosphate + hydroxyacetone + NADPH
? + NADP+
show the reaction diagram
-
reaction mixtures containing 0.21-0.34 mM IspC from Escherichia coli, Mycobacterium tuberculosis or Arabidopsis thaliana
-
-
?
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1-deoxy-D-xylulose 5-phosphate + NADPH + H+
2-C-methyl-D-erythritol 4-phosphate + NADP+
show the reaction diagram
additional information
?
-
participation in the control of the 2-C-methyl-D-erythritol 4-phosphate pathway
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
14% of the activity with NADPH
NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
a divalent cation is absolutely required, optimal at 10 mM, the enzyme prefers Mn2+ or Mg2+
Mn2+
a divalent cation is absolutely required, the enzyme prefers Mn2+ or Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
the enzyme is inducible by light
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.132
1-deoxy-D-xylulose 5-phosphate
pH 8.0, 37°C, recombinant pseudomature enzyme
0.972
2-C-methyl-D-erythritol 4-phosphate
pH 8.0, 37°C, recombinant pseudomature enzyme
0.47 - 1
NADP+
pH 8.0, 37°C, recombinant pseudomature enzyme
0.03
NADPH
pH 8.0, 37°C, recombinant pseudomature enzyme
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.4
1-deoxy-D-xylulose 5-phosphate
pH 8.0, 37°C, recombinant pseudomature enzyme
1.6
2-C-methyl-D-erythritol 4-phosphate
pH 8.0, 37°C, recombinant pseudomature enzyme
1.6
NADP+
pH 8.0, 37°C, recombinant pseudomature enzyme
4.4
NADPH
pH 8.0, 37°C, recombinant pseudomature enzyme
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000085
fosmidomycin
pH 8.0, 37°C, recombinant pseudomature enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.1
purified recombinant pseudomature enzyme, reverse reaction
5.6
purified recombinant pseudomature enzyme, forward reaction
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35 - 42
90% of maximal activity within this range
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DXR_ARATH
477
0
51964
Swiss-Prot
Chloroplast (Reliability: 3)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
N-terminal transit peptide for plastid localization
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
maximally stable at
673562
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
purifed recombinant enzyme, 24 h, 78% remaining activity
37
purifed recombinant enzyme, 24 h, 30% remaining activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, purifed recombinant enzyme, 0.1 M Tris-HCl, pH 7.5, with 50 mM KCl, 10% v/v glycerol, and 10 mM DTT, 6 months, 56% remaining activity
-80°C, purifed recombinant enzyme, 0.1 M Tris-HCl, pH 7.5, with 50 mM KCl, 10% v/v glycerol, and 10 mM DTT, 6 months, no loss of activity
4°C, purifed recombinant enzyme, 0.1 M Tris-HCl, pH 7.5, with 50 mM KCl, 10% v/v glycerol, and 10 mM DTT, 6 months, 4% remaining activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme in the pseudomature form without plastid-targeting sequence 62fold from Escherichia coli
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ispC, DNA and amino acid sequence determination and analysis, functional expression of the His-tagged enzyme in the pseudomature form without plastid-targeting sequence in recombinant Escherichia coli
gene ispC, expression analysis, light-dependent expression pattern, overview
into vector pMW118, expressed in Escherichia coli DYM1 transformant
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Carretero-Paulet, L.; Ahumada, I.; Cunillera, N.; Rodriguez-Concepcion, M.; Ferrer, A.; Boronat, A.; Campos, N.
Expression and molecular analysis of the Arabidopsis DXR gene encoding 1-deoxy-D-xylulose 5-phosphate reductoisomerase, the first committed enzyme of the 2-C-methyl-D-erythritol 4-phosphate pathway
Plant Physiol.
129
1581-1591
2002
Arabidopsis thaliana (Q9XFS9)
Manually annotated by BRENDA team
Rohdich, F.; Lauw, S.; Kaiser, J.; Feicht, R.; Koehler, P.; Bacher, A.; Eisenreich, W.
Isoprenoid biosynthesis in plants - 2C-methyl-D-erythritol-4-phosphate synthase (IspC protein) of Arabidopsis thaliana
FEBS J.
273
4446-4458
2006
Arabidopsis thaliana (Q9XFS9), Arabidopsis thaliana
Manually annotated by BRENDA team
Hsieh, M.H.; Goodman, H.M.
The Arabidopsis IspH homolog is involved in the plastid nonmevalonate pathway of isoprenoid biosynthesis
Plant Physiol.
138
641-653
2005
Arabidopsis thaliana (Q9XFS9)
Manually annotated by BRENDA team
Sando, T.; Takeno, S.; Watanabe, N.; Okumoto, H.; Kuzuyama, T.; Yamashita, A.; Hattori, M.; Ogasawara, N.; Fukusaki, E.; Kobayashi, A.
Cloning and characterization of the 2-C-methyl-D-erythritol 4-phosphate (MEP) pathway genes of a natural-rubber producing plant, Hevea brasiliensis
Biosci. Biotechnol. Biochem.
72
2903-2917
2008
Arabidopsis thaliana (Q9XFS9), Arabidopsis thaliana, Escherichia coli (P45568), Escherichia coli, Hevea brasiliensis (A9ZN08), Hevea brasiliensis
Manually annotated by BRENDA team
Lauw, S.; Illarionova, V.; Bacher, A.; Rohdich, F.; Eisenreich, W.
Biosynthesis of isoprenoids: studies on the mechanism of 2C-methyl-D-erythritol-4-phosphate synthase
FEBS J.
275
4060-4073
2008
Arabidopsis thaliana, Bacillus subtilis, Mycobacterium tuberculosis, Escherichia coli (P45568), Escherichia coli
Manually annotated by BRENDA team
Xing, S.; Miao, J.; Li, S.; Qin, G.; Tang, S.; Li, H.; Gu, H.; Qu, L.J.
Disruption of the 1-deoxy-D-xylulose-5-phosphate reductoisomerase (DXR) gene results in albino, dwarf and defects in trichome initiation and stomata closure in Arabidopsis
Cell Res.
20
688-700
2010
Arabidopsis thaliana
Manually annotated by BRENDA team
Mendoza-Poudereux, I.; Munoz-Bertomeu, J.; Arrillaga, I.; Segura, J.
Deoxyxylulose 5-phosphate reductoisomerase is not a rate-determining enzyme for essential oil production in spike lavender
J. Plant Physiol.
171
1564-1570
2014
Arabidopsis thaliana
Manually annotated by BRENDA team