Information on EC 2.2.1.7 - 1-deoxy-D-xylulose-5-phosphate synthase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
2.2.1.7
-
RECOMMENDED NAME
GeneOntology No.
1-deoxy-D-xylulose-5-phosphate synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
pyruvate + D-glyceraldehyde 3-phosphate = 1-deoxy-D-xylulose 5-phosphate + CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
condensation
-
-
acyloin-type condensation reaction
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
methylerythritol phosphate pathway I
-
-
methylerythritol phosphate pathway II
-
-
pyridoxal 5'-phosphate biosynthesis I
-
-
thiazole biosynthesis I (facultative anaerobic bacteria)
-
-
thiazole biosynthesis II (aerobic bacteria)
-
-
isoprenoid biosynthesis
-
-
vitamin B1 metabolism
-
-
Thiamine metabolism
-
-
Terpenoid backbone biosynthesis
-
-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
-
-
Biosynthesis of antibiotics
-
-
SYSTEMATIC NAME
IUBMB Comments
pyruvate:D-glyceraldehyde-3-phosphate acetaldehydetransferase (decarboxylating)
Requires thiamine diphosphate. The enzyme forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis (for diagram, {terp/nonMVA}).
CAS REGISTRY NUMBER
COMMENTARY hide
202218-79-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain KCCM 10413, gene dxs11
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain PY79
-
-
Manually annotated by BRENDA team
strain PY79
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
A0A0N9Z801
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
peppermint
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
cultivar Xanthi
UniProt
Manually annotated by BRENDA team
strain CL190
-
-
Manually annotated by BRENDA team
strain CL190
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
knockout mutations with lethal albino plants
metabolism
-
the enzyme primarily exerts the control flux of the methylerythritol 4-phosphate pathway
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
hydroxypyruvate + D-glyceraldehyde 3-phosphate
D-xylulose 5-phosphate + CO2
show the reaction diagram
-
7.2% of the activity with pyruvate
-
-
?
pyruvate + 1-methyl-2-nitrosobenzene
N-hydroxy-N-(2-methylphenyl)acetamide + CO2
show the reaction diagram
-
-
-
-
?
pyruvate + 1-nitrosonaphthalen-2-ol
N-hydroxy-N-(2-hydroxynaphthalen-1-yl)acetamide + CO2
show the reaction diagram
-
-
-
-
?
pyruvate + 2-hydroxy-4,6-dinitrobenzaldehyde
? + CO2
show the reaction diagram
-
-
-
-
?
pyruvate + 3,5-dimethyl-4-nitroso-1-(propan-2-yl)-1H-pyrazole
N-[3,5-dimethyl-1-(propan-2-yl)-1H-pyrazol-4-yl]-N-hydroxyacetamide + CO2
show the reaction diagram
-
-
-
-
?
pyruvate + 6-bromo-1-nitrosonaphthalen-2-ol
N-(6-bromo-2-hydroxynaphthalen-1-yl)-N-hydroxyacetamide + CO2
show the reaction diagram
-
-
-
-
?
pyruvate + 6-hydroxy-5-nitrosonaphthalene-2-sulfonamide
N-hydroxy-N-(2-hydroxy-6-sulfamoylnaphthalen-1-yl)acetamide + CO2
show the reaction diagram
-
-
-
-
?
pyruvate + 7-methoxy-1-nitrosonaphthalen-2-ol
N-hydroxy-N-(2-hydroxy-7-methoxynaphthalen-1-yl)acetamide + CO2
show the reaction diagram
-
-
-
-
?
pyruvate + D-erythrose
1-deoxy-D-fructose + CO2
show the reaction diagram
-
17% of the activity with D-glyceraldehyde
-
-
?
pyruvate + D-erythrose 4-phosphate
1-deoxy-D-fructose 6-phosphate + CO2
show the reaction diagram
pyruvate + D-glyceraldehyde
1-deoxy-D-xylulose + CO2
show the reaction diagram
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate
show the reaction diagram
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
show the reaction diagram
pyruvate + D-ribose 5-phosphate
1-deoxy-D-sedoheptulose 7-phosphate + CO2
show the reaction diagram
pyruvate + DL-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
show the reaction diagram
pyruvate + glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
show the reaction diagram
pyruvate + glycolaldehyde
1-deoxy-L-erythrulose + CO2
show the reaction diagram
-
71% of the activity with D-glyceraldehyde
-
-
?
pyruvate + L-glyceraldehyde
1-deoxy-D-xylulose + CO2
show the reaction diagram
-
-
-
-
?
pyruvate + N,N-dimethyl-4-nitrosoaniline
N-[4-(dimethylamino)phenyl]-N-hydroxyacetamide + CO2
show the reaction diagram
-
-
-
-
?
pyruvate + nitrosobenzene
? + CO2
show the reaction diagram
-
-
-
-
?
pyruvate + nitrosobenzene
N-hydroxy-N-phenylacetamide + CO2
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
pyruvate + D-glyceraldehyde
1-deoxy-D-xylulose + CO2
show the reaction diagram
-
the reaction product, 1-deoxy-D-xylulose 5-phosphate, is a precursor to isoprenoids and vitamins
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
show the reaction diagram
additional information
?
-
Q5J7B4
gingkolides are diterpenoids and potent platelet-activating factor antagonists
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thiamine diphosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
thiamine diphosphate
required for enzymatic activity
Zn2+
-
divalent cation required, supports activity to a lower level than Mn2+ or Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(1E,1'E)-O,O'-(ethane-1,2-diyl)bis[2,4,5-trihydroxybenzaldehyde oxime]
-
-
-
(1E,7E)-1-(2,4,5-trihydroxyphenyl)-3,6-dioxa-2,7-diazanona-1,7-dien-9-oate
-
-
-
(E)-2,4,5-trihydroxybenzaldehyde O-benzyl oxime
-
-
-
(E)-2,4,5-trihydroxybenzaldehyde O-methyl oxime
-
-
-
(E)-2,4,5-trihydroxybenzaldehyde oxime
-
-
-
(E)-2,4-dihydroxybenzaldehyde O-methyl oxime
-
-
-
(E)-2,5-dihydroxybenzaldehyde O-methyl oxime
-
-
-
(E)-2-fluoro-4,5-dihydroxybenzaldehyde O-methyl oxime
-
-
-
(E)-2-fluoro-4,5-dimethoxybenzaldehyde O-methyl oxime
-
-
-
(E)-2-hydroxy-3-nitrobenzaldehyde O-methyl oxime
-
-
-
(E)-2-hydroxybenzaldehyde O-methyl oxime
-
-
-
(E)-3,4,5-trihydroxybenzaldehyde O-methyl oxime
-
-
-
(E)-3,4-dihydroxy-5-methoxybenzaldehyde O-methyl oxime
-
-
-
(E)-4,5-difluoro-2-hydroxybenzaldehyde O-methyl oxime
-
-
-
(E)-4-hydroxy-3-nitrobenzaldehyde O-methyl oxime
-
-
-
(E)-5-[(2-methylhydrazono)methyl]benzene-1,2,4-triol
-
-
-
(E)-uracil-6-carbaldehyde O-methyl oxime
-
-
-
(E,Z)-2,4,5-trimethoxybenzaldehyde O-methyl oxime
-
-
-
(E,Z)-3,4-dihydroxybenzaldehyde O-methyl oxime
-
-
-
1-methyl-2-nitrosobenzene
-
weak inhibitory activity
1-nitrosonaphthalen-2-ol
-
weak inhibitory activity
2,3-diphospho-D-glyceric acid
-
0.1 mM, 50% inhibition
2-fluoropyruvate
-
2-methyl-3,5-diphenyl-6-propylpyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
2-methyl-3,5-diphenylpyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
2-methyl-5-naphthalen-2-yl-3-phenylpyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
3,5-bis(4-methoxyphenyl)-2-methylpyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
3,5-dimethyl-4-nitroso-1-(propan-2-yl)-1H-pyrazole
-
weak inhibitory activity
3,5-diphenyl-2-(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
3-(4-bromophenyl)-5-(2-methoxyphenyl)-2-methylpyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
3-(4-bromophenyl)-5-methyl-2-(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
3-(4-chlorophenyl)-2-ethyl-5-(4-methoxyphenyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
3-(4-chlorophenyl)-2-methyl-5-phenylpyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
3-(4-chlorophenyl)-2-methyl-5-[[(1-phenyl-1H-tetrazol-5-yl)sulfanyl]methyl]pyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
3-(4-chlorophenyl)-5-(4-methoxyphenyl)-2-methylpyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
3-(4-chlorophenyl)-5-(methoxymethyl)-2-methylpyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
3-(4-chlorophenyl)-5-(methoxymethyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
3-(4-chlorophenyl)-5-methyl-2-(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
3-(4-chlorophenyl)-5-methylpyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
3-(4-chlorophenyl)-5-[[(4-chlorophenyl)sulfanyl]methyl]-2-methylpyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
3-(4-fluorophenyl)-5-(4-methoxyphenyl)-2-methylpyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
3-(4-methoxyphenyl)-2-methyl-5-phenylpyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
3-(4-methoxyphenyl)-5-phenyl-2-(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
3-Fluoropyruvate
competitive with respect to pyruvate
5-(chloromethyl)-3-phenylpyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
5-benzyl-3-(4-chlorophenyl)-2-(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
5-benzyl-3-(4-chlorophenyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
5-benzyl-3-phenyl-2-(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
5-[(methoxyamino)methyl]benzene-1,2,4-triol
-
-
-
5-[[(4-chlorophenyl)sulfanyl]methyl]-2-methyl-3-phenylpyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
6-benzyl-3-(4-chlorophenyl)-5-methyl-2-(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
6-bromo-1-nitrosonaphthalen-2-ol
-
weak inhibitory activity
6-hydroxy-5-nitrosonaphthalene-2-sulfonamide
-
weak inhibitory activity
7-methoxy-1-nitrosonaphthalen-2-ol
-
weak inhibitory activity
benzylacetylphosphonate
-
competitive inhibitor
-
beta-fluoropyruvate
-
dead-end inhibitor for pyruvate
beta-Glycerophosphate
-
0.3 mM, 40% inhibition
butyl acetyl phosphonate
-
-
-
D-3-Phosphoglyceric acid
-
0.16 mM, 23% inhibition
D-glyceraldehyde
-
competitive inhibition with respect to pyruvate
D-glyceraldehyde 3-phosphate
-
substrate inhibition
dimethylallyl diphosphate
-
competitive inhibitor
DL-alpha-glycerophosphate
-
0.29 mM, 50% inhibition
ethyl (5-methyl-7-oxo-3-phenyl-4,7-dihydropyrazolo[1,5-a]pyrimidin-6-yl)acetate
-
-
Fluoropyruvate
-
recombinant protein, 50% inhibition at 0.4 mM, fluoropyruvate is supposed to bind covalently to the active site
isopentenyl diphosphate
-
competitive inhibitor
ketoclomazone
-
-
-
methyl [3-(4-bromophenyl)-7-oxo-2-(trifluoromethyl)-4,7-dihydropyrazolo[1,5-a]pyrimidin-5-yl]acetate
-
-
Methylacetylphosphonate
N,N-dimethyl-4-nitrosoaniline
-
weak inhibitory activity
nitrosobenzene
-
weak inhibitory activity
phosphonoacetohydroxamate
-
0.1 mM, 25% inhibition
phosphonopropionohydroxamate
-
0.1 mM, 10% inhibition
pyruvate
-
substrate inhibition
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
helper component-proteinase
enhances the activity of 1-deoxy-D-xylulose-5-phosphate synthase
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.099
1-methyl-2-nitrosobenzene
-
at pH 8.0 and 37C
0.041
1-nitrosonaphthalen-2-ol
-
at pH 8.0 and 37C
0.512
2-hydroxy-4,6-dinitrobenzaldehyde
-
at pH 8.0 and 37C
-
0.387
3,5-dimethyl-4-nitroso-1-(propan-2-yl)-1H-pyrazole
-
at pH 8.0 and 37C
0.024
6-bromo-1-nitrosonaphthalen-2-ol
-
at pH 8.0 and 37C
0.018
6-hydroxy-5-nitrosonaphthalene-2-sulfonamide
-
at pH 8.0 and 37C
0.063
7-methoxy-1-nitrosonaphthalen-2-ol
-
at pH 8.0 and 37C
0.12
D-erythrose 4-phosphate
-
pH 7.9, 37C
5.6 - 38
D-glyceraldehyde
0.0016 - 1.78
D-glyceraldehyde 3-phosphate
4.5
L-Glyceraldehyde
-
pH 7.9, 37C
0.054
N,N-dimethyl-4-nitrosoaniline
-
at pH 8.0 and 37C
0.0011 - 14
pyruvate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6
1-methyl-2-nitrosobenzene
Escherichia coli
-
at pH 8.0 and 37C
0.018
1-nitrosonaphthalen-2-ol
Escherichia coli
-
at pH 8.0 and 37C
0.006
2-hydroxy-4,6-dinitrobenzaldehyde
Escherichia coli
-
at pH 8.0 and 37C
-
0.023
3,5-dimethyl-4-nitroso-1-(propan-2-yl)-1H-pyrazole
Escherichia coli
-
at pH 8.0 and 37C
0.033
6-bromo-1-nitrosonaphthalen-2-ol
Escherichia coli
-
at pH 8.0 and 37C
0.02
6-hydroxy-5-nitrosonaphthalene-2-sulfonamide
Escherichia coli
-
at pH 8.0 and 37C
0.022
7-methoxy-1-nitrosonaphthalen-2-ol
Escherichia coli
-
at pH 8.0 and 37C
1.7
D-glyceraldehyde
Rhodobacter capsulatus
-
pH 7.4, 37C
0.64 - 26.8
D-glyceraldehyde 3-phosphate
0.015
N,N-dimethyl-4-nitrosoaniline
Escherichia coli
-
at pH 8.0 and 37C
0.53 - 26.8
pyruvate
additional information
additional information
Escherichia coli
-
the most efficient turnover of substrates is observed in HEPES buffer, pH 8.0
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6
1-methyl-2-nitrosobenzene
Escherichia coli
-
at pH 8.0 and 37C
209765
0.045
1-nitrosonaphthalen-2-ol
Escherichia coli
-
at pH 8.0 and 37C
209766
0.06
3,5-dimethyl-4-nitroso-1-(propan-2-yl)-1H-pyrazole
Escherichia coli
-
at pH 8.0 and 37C
209770
1.3
6-bromo-1-nitrosonaphthalen-2-ol
Escherichia coli
-
at pH 8.0 and 37C
209767
1.1
6-hydroxy-5-nitrosonaphthalene-2-sulfonamide
Escherichia coli
-
at pH 8.0 and 37C
209768
0.35
7-methoxy-1-nitrosonaphthalen-2-ol
Escherichia coli
-
at pH 8.0 and 37C
209769
0.01167
acetaldehyde
Escherichia coli
-
-
90
0.006
Butanal
Escherichia coli
-
-
540
0.035
D-glyceraldehyde
Escherichia coli
-
-
639
0.03 - 570
D-glyceraldehyde 3-phosphate
147
0.28
N,N-dimethyl-4-nitrosoaniline
Escherichia coli
-
at pH 8.0 and 37C
7034
0.0035
propanal
Escherichia coli
-
-
328
6.5 - 250
pyruvate
31
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001
(1E,1'E)-O,O'-(ethane-1,2-diyl)bis[2,4,5-trihydroxybenzaldehyde oxime]
-
at pH 8.0 and 37C
-
0.0184
(1E,7E)-1-(2,4,5-trihydroxyphenyl)-3,6-dioxa-2,7-diazanona-1,7-dien-9-oate
-
at pH 8.0 and 37C
-
0.0091
(E)-2,4,5-trihydroxybenzaldehyde O-benzyl oxime
-
at pH 8.0 and 37C
-
0.0039
(E)-2,4,5-trihydroxybenzaldehyde O-methyl oxime
-
at pH 8.0 and 37C
-
0.0026
(E)-2,4,5-trihydroxybenzaldehyde oxime
-
at pH 8.0 and 37C
-
0.2
(E)-2,4-dihydroxybenzaldehyde O-methyl oxime, (E)-2,5-dihydroxybenzaldehyde O-methyl oxime
-
Ki above 0.2 mM, at pH 8.0 and 37C
-
0.0151
(E)-2-fluoro-4,5-dihydroxybenzaldehyde O-methyl oxime
-
at pH 8.0 and 37C
-
0.2
(E)-2-fluoro-4,5-dimethoxybenzaldehyde O-methyl oxime
-
Ki above 0.2 mM, at pH 8.0 and 37C
-
0.0478
(E)-2-hydroxy-3-nitrobenzaldehyde O-methyl oxime
-
at pH 8.0 and 37C
-
0.2
(E)-2-hydroxybenzaldehyde O-methyl oxime
-
Ki above 0.2 mM, at pH 8.0 and 37C
-
0.0294
(E)-3,4,5-trihydroxybenzaldehyde O-methyl oxime
-
at pH 8.0 and 37C
-
0.2
(E)-3,4-dihydroxy-5-methoxybenzaldehyde O-methyl oxime, (E)-4,5-difluoro-2-hydroxybenzaldehyde O-methyl oxime, (E)-4-hydroxy-3-nitrobenzaldehyde O-methyl oxime
-
Ki above 0.2 mM, at pH 8.0 and 37C
-
0.075
(E)-5-[(2-methylhydrazono)methyl]benzene-1,2,4-triol
-
Ki above 0.075 mM, at pH 8.0 and 37C
-
0.2
(E)-uracil-6-carbaldehyde O-methyl oxime
-
Ki above 0.2 mM, at pH 8.0 and 37C
-
0.1
(E,Z)-2,4,5-trimethoxybenzaldehyde O-methyl oxime
-
Ki above 0.1 mM, at pH 8.0 and 37C
-
0.2
(E,Z)-3,4-dihydroxybenzaldehyde O-methyl oxime
-
Ki above 0.2 mM, at pH 8.0 and 37C
-
0.035 - 0.043
2-fluoropyruvate
-
0.2
3-Fluoropyruvate
pH and temperature not specified in the publication
0.075
5-[(methoxyamino)methyl]benzene-1,2,4-triol
-
Ki above 0.075 mM, at pH 8.0 and 37C
-
0.0104
benzylacetylphosphonate
-
at pH 8.0 and 37C
-
0.0056
butyl acetyl phosphonate
-
at pH 8.0 and 37C
-
3.2
D-glyceraldehyde
-
pH 8.0, 37C
0.0813
dimethylallyl diphosphate
-
at pH 8.0 and 37C
0.0654
isopentenyl diphosphate
-
at pH 8.0 and 37C
0.075
ketoclomazone
-
at pH 8.0 and 37C
-
0.046 - 0.075
Methylacetylphosphonate
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.291
1-methyl-2-nitrosobenzene
Escherichia coli
-
at pH 8.0 and 37C
1.065
1-nitrosonaphthalen-2-ol
Escherichia coli
-
at pH 8.0 and 37C
0.0719
2-methyl-3,5-diphenyl-6-propylpyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
-
0.0306
2-methyl-3,5-diphenylpyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
-
0.0195
2-methyl-5-naphthalen-2-yl-3-phenylpyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
-
0.0424
3,5-bis(4-methoxyphenyl)-2-methylpyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
-
2
3,5-dimethyl-4-nitroso-1-(propan-2-yl)-1H-pyrazole
Escherichia coli
-
IC50 above 2.0 mM, at pH 8.0 and 37C
0.023
3,5-diphenyl-2-(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
-
0.0535
3-(4-bromophenyl)-5-(2-methoxyphenyl)-2-methylpyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
-
0.2
3-(4-bromophenyl)-5-methyl-2-(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
value above
0.0197
3-(4-chlorophenyl)-2-ethyl-5-(4-methoxyphenyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
-
0.0342
3-(4-chlorophenyl)-2-methyl-5-phenylpyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
-
0.0551
3-(4-chlorophenyl)-2-methyl-5-[[(1-phenyl-1H-tetrazol-5-yl)sulfanyl]methyl]pyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
-
0.0109
3-(4-chlorophenyl)-5-(4-methoxyphenyl)-2-methylpyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
-
0.2
3-(4-chlorophenyl)-5-(methoxymethyl)-2-methylpyrazolo[1,5-a]pyrimidin-7(4H)-one
0.0984
3-(4-chlorophenyl)-5-methyl-2-(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
-
0.2
3-(4-chlorophenyl)-5-methylpyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
value above
0.0411
3-(4-chlorophenyl)-5-[[(4-chlorophenyl)sulfanyl]methyl]-2-methylpyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
-
0.0106
3-(4-fluorophenyl)-5-(4-methoxyphenyl)-2-methylpyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
-
0.0907
3-(4-methoxyphenyl)-2-methyl-5-phenylpyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
-
0.0202 - 0.2
3-(4-methoxyphenyl)-5-phenyl-2-(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
0.2
5-(chloromethyl)-3-phenylpyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
value above
0.014
5-benzyl-3-(4-chlorophenyl)-2-(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
-
0.1141
5-benzyl-3-(4-chlorophenyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
-
0.0711
5-benzyl-3-phenyl-2-(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
-
0.0637
5-[[(4-chlorophenyl)sulfanyl]methyl]-2-methyl-3-phenylpyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
-
0.2
6-benzyl-3-(4-chlorophenyl)-5-methyl-2-(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
value above
0.522
6-bromo-1-nitrosonaphthalen-2-ol
Escherichia coli
-
at pH 8.0 and 37C
0.354
6-hydroxy-5-nitrosonaphthalene-2-sulfonamide
Escherichia coli
-
at pH 8.0 and 37C
2
7-methoxy-1-nitrosonaphthalen-2-ol
Escherichia coli
-
IC50 above 2.0 mM, at pH 8.0 and 37C
0.2
ethyl (5-methyl-7-oxo-3-phenyl-4,7-dihydropyrazolo[1,5-a]pyrimidin-6-yl)acetate
Mycobacterium tuberculosis
-
value above
0.073
methyl [3-(4-bromophenyl)-7-oxo-2-(trifluoromethyl)-4,7-dihydropyrazolo[1,5-a]pyrimidin-5-yl]acetate
Mycobacterium tuberculosis
-
-
0.844
N,N-dimethyl-4-nitrosoaniline
Escherichia coli
-
at pH 8.0 and 37C
0.208
nitrosobenzene
Escherichia coli
-
at pH 8.0 and 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.2
pH and temperature not specified in the publication
1.6
-
histidin-tagged DXP-synthase A, expressed in Escherichia coli
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 7.5
7.5 - 8
-
-
9
-
recombinant protein
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.5
-
the enzyme does not show substantial activity below pH 6.5 and above pH 8.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42 - 44
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
75% of the activity at 34C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.63
amino acid sequence calculation
6.3
calculated from amino acid sequence
7
amino acid sequence calculation of the enzyme encoded by dxs1
7.185
-
estimated
7.5
calculated
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
PaDXS2A is induced by treatment with chitosan, methyl salicylate, and Ceratocystis polonica (a bark beetle-associated, blue-staining fungal pathogen of Norway spruce); PaDXS2B is induced by treatment with methyl jasmonate and chitosan, but is not affected by methyl salicylate or Cochlearia polonica
Manually annotated by BRENDA team
high expression
Manually annotated by BRENDA team
-
RNA blot hybridization
Manually annotated by BRENDA team
yellow kernel
Manually annotated by BRENDA team
immature tassel
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65000 - 69000
-
SDS-PAGE
69000
-
predicted size from gene sequence
71000
-
predicted size from gene sequence, mature protein
76400
-
predicted
77600
-
predicted size from gene sequence
135000
native enzyme, gel filtration
260000
gel filtratiion
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant wild-type and selenomethionine-labeled enzyme in complex with cofactor thiamine diphosphate, mixing of protein solution with reservoir solution containing 150 mM NaCl, and 20% w/v PEG 6000 or PEG 8000, cryoprotection by 25% v/v ethylene glycol, X-ray diffraction structure determination and analysis at 2.9 A resolution
-
purified recombinant wild-type and selenomethionine-labeled enzyme in complex with cofactor thiamine diphosphate, protein solution is mixed with the reservoir solution containing 30% w/v PEG 3350 and 200 mM Na,K-tartrate and infected by a fungus, the enzyme crystallized only after in situ proteolysis by a fungal protease, cryoprotection by 25% v/v ethylene glycol, X-ray diffraction structure determination and analysis at 2.4 A resolution
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
sharp decrease in activity above
additional information
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 50 mM Tris-HCl pH 7.5, 5 mM beta-mercaptoethanol, 0.15 mM phenylmethysulfonyl fluoride, 30% glycerol, 4-6 weeks
-
-20C, elution buffer containing 30% glycerol, storage for around 10 days with no significant loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
95% pure by SDS-PAGE
-
ammonium sulfate precipitation and Ni-NTA column chromatography
-
Cosmogel His-Accept column chromatography
functional soluble, recombinant enzyme from Escherichia coli
histidine-tagged recombinant protein, expressed in Escherichia coli
-
histidine-tagged recombinant proteins DXP-synthase A and DXP-synthase B, expressed in Escherichia coli
-
Ni-NTA agarose column chromatography, amylose resin chromatography, and glutathione Sepharose column chromatography
Ni-NTA column chromatography and Superdex gel filtration
overexpression
-
recombinant His-tagged enzymes from Escherichia coli by nickel affinity and anion exchange chromatography, and gel filtration
recombinant protein, expressed in Escherichia coli
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned in Escherichia coli
complementation assay in Escherichia coli; isolation of cDNA, expression analysis indicates developmental and organ-specific regulation of mRNA accumulation
-
expressed in Arabidopsis thaliana protoplasts
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3)pLysS cells
-
expressed in Escherichia coli strain EcAB4-2
-
expressed in Escherichia coli; gene dxs11, DNA and amino acid sequence determination and analysis, functional overexpression of the soluble enzyme in Escherichia coli, functional overexpression in Agrobacterium tumefaciens strain KCCM 10413, the transformed strain shows increased enzyme activity
expressed in Saccharomyces cerevisiae AH109 and Escherichia coli BL21 cells
expression in Escherichia coli
expression in Escherichia coli strain DH5alpha
-
expression in Morinda citrifolia
-
expression in Nicotiana tabacum
-
expression of MtDXS1 and MtDXS2 in Escherichia coli
-
gene dxs, DNA and amino acid sequence determination and analysis, expression profile analysis, phylogenetic analysis, expression in Escherichia coli strain DH5alpha
gene dxs, overexpression in transgenic Solanum tuberosum tubers
-
gene dxs1, semiquantitative expression analysis, DNA and amino acid sequence determination and analysis, phylogenetic analysis; genes dxs1 and dxs2, semiquantitative expression analysis, DNA and amino acid sequence determination and analysis, phylogenetic analysis
gene dxs2, cloning from embryonic roots, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression in and complementation of an enzyme-deficient Escherichia coli mutant strain
genes dxs1, dxs2, and dxs3, DNA and amino acid sequence determination and analysis, phylogenetic tree
-
mutant enzymes are expressed in Escherichia coli BL21(DE3) cells
-
overexpression
-
overexpression in Nicotiana tabacum
-
overexpression in transgenic Lavandula latifolia plants using the Agrobacterium tumefaciens transfection method
-
overexpression of the His-tagged enzyme in Escherichia coli, production of the selenomethionine enzyme form in Escherichia coli strain B834
transfection to Arabidopsis thaliana, expression in Escherichia coli mutants; transfection to Arabidopsis thaliana, expression in Escherichia coli mutants
two genes dxsA and dxsB, dxsA is located in the photosynthesis cluster, both isoenzymes expressed in Escherichia coli
-
use of a step wise deletion approach for the successful production of a catalytically active and soluble form of Plasmodium vivax 1-deoxy-D-xylulose-5-phosphate synthase in Escherichia coli. Signal and transit peptide removed soluble and functionally active enzyme is expressed in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
3fold higher expression in seeds than in stems and flowers, 2fold higher expression in leaves than in stems and flowers
-
correlation exists between the transcript profile and the accumulation of free monoterpenol odorants. The modulation of enzyme gene expression during berry development appears to be independent of nucleotide variation in the coding sequence
-
decreasing transcript levels in leafs fully expanded, low expression level in nonphotosynthetic tissues like root
-
expression increases upon treatment with methyl jasmonate and salicylic acid
high transcript levels in the shoot, increasing transcript levels during leaf development, highest expression in young leaves prior to full
-
isoform DXS1 expression is stimulated by mechanical, chemical, and H2O2 treatment, while isoforms DXS2 and DXS3 only respond to chemical treatment and mechanical treatment, respectively. All isoforms are upregulated after methyl jasmonate treatment
-
light exposure results in a transient 2fold accumulation after 5 h of illumination; light induction, transcripts rapidly accumulate upon 1 h of illumination, and continue for up to 21 h with a final increase of 5fold above the initial level
mRNA accumulation patterns over time are almost identical among the three DXS isoforms reaching the highest expression levels on day 6 after inoculation into fresh medium; mRNA accumulation patterns over time are almost identical among the three DXS isoforms reaching the highest expression levels on day 6 after inoculation into fresh medium
transcript levels 2- or 3fold higher in wood than in other tissues and organs, 1300fold increase of transcript levels on the second day after treatment of trees with 1 mM methyl jasmonate, increase of transcript levels one day after mechanical wounding; transcript levels 2- or 6fold higher in wood than in other tissues and organs, 10fold increase of transcript levels on the second day after treatment of trees with 1 mM methyl jasmonate
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H48A
mutant protein with lost activity, below 0.1% of specific activity compared with that of the wild-type
R420A
-
thiamine diphosphate is significantly stabilized on the variant compared to the wild type enzyme in the absence of acceptor substrate. The substitution reduces affinity for D-glyceraldehyde 3-phosphate
R478A
-
thiamine diphosphate is significantly stabilized on the variant compared to the wild type enzyme in the absence of acceptor substrate. The substitution reduces affinity for D-glyceraldehyde 3-phosphate
Y392F
-
thiamine diphosphate is significantly stabilized on the variant compared to the wild type enzyme in the absence of acceptor substrate. The substitution reduces affinity for D-glyceraldehyde 3-phosphate
H49Q
-
mutant enzyme shows no detectable DXP-synthase activity, this demonstrates the key role of H49 for enzyme activity
R420A
-
the mutation has no apparent effect on the affinities of nitroso substrates in C-N bond formation
R478A
-
the mutation has no apparent effect on the affinities of nitroso substrates in C-N bond formation
K284N
-
single nucleotide polymorphism, significantly associated with Muscat-flavoured varieties. Substitution influences the enzyme kinetics by increasing the catalytic efficiency and also dramatically affects monoterpene levels upon heterologous expression
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
analysis
-
development of a sensitive assay suitable for plant extracts that is based on the decarboxylation of labeled pyruvate and detection of 13CO2 by isotope ratio mass spectrometry
biotechnology
increase production level of CoQ10 by coexpression of decaprenyl diphosphate synthase and 1-deoxy-D-xylulose 5-phosphate synthase isolated from Rhizobium radiobacter ATCC 4718 in recombinant Escherichia coli is shown
drug development
industry
medicine
development of 1-deoxy-D-xylulose-5-phosphate synthase inhibitors to treat Plasmodium vivax malaria
synthesis
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