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Information on EC 2.2.1.7 - 1-deoxy-D-xylulose-5-phosphate synthase and Organism(s) Escherichia coli and UniProt Accession P77488

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EC Tree
IUBMB Comments
Requires thiamine diphosphate. The enzyme forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis (for diagram, {terp/nonMVA}).
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Select one or more organisms in this record: ?
This record set is specific for:
Escherichia coli
UNIPROT: P77488
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
1-deoxy-d-xylulose 5-phosphate synthase, dxp synthase, 1-deoxy-d-xylulose-5-phosphate synthase, deoxyxylulose 5-phosphate synthase, dxs11, csdxs, 1-deoxyxylulose-5-phosphate synthase, pddxs2, gmdxs1, deoxyxylulose-5-phosphate synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1-deoxy-D-xylulose 5-phosphate synthase
-
DXP synthase
-
1-D-deoxy-D-threo-2-pentulose 5-phosphate synthetase
-
-
-
-
1-D-deoxyxylulose 5-phosphate synthase
-
-
-
-
1-deoxy-D-threo-pentulose synthase
-
-
-
-
1-deoxy-D-xylulose 5-phosphate synthase
-
-
1-deoxy-D-xylulose 5-phosphate synthetase
-
-
-
-
1-deoxy-D-xylulose-5-phosphate pyruvate lyase
-
-
-
-
1-deoxy-D-xylulose-5-phosphate synthase
-
-
1-desoxy-D-xylulose-5-phosphate synthase
-
-
-
-
D-1-deoxyxylulose 5-phosphate synthase
-
-
-
-
deoxyxylulose 5-phosphate synthase
-
-
-
-
deoxyxylulose-5-phosphate synthetase
-
-
-
-
DXP synthase
DXP-synthase
-
-
-
-
glyceraldehydes 3-phosphate-pyruvate ligase
-
-
-
-
synthase, 1-deoxy-D-xylulose 5-phosphate
-
-
-
-
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
-
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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-glyceraldehyde
1-deoxy-D-xylulose + CO2
show the reaction diagram
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
show the reaction diagram
pyruvate + DL-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + 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
-
-
-
?
hydroxypyruvate + D-glyceraldehyde 3-phosphate
D-xylulose 5-phosphate + CO2
show the reaction diagram
-
7.2% of the activity with pyruvate
-
-
?
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 + CO2
show the reaction diagram
pyruvate + D-ribose 5-phosphate
1-deoxy-D-sedoheptulose 7-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
-
-
?
additional information
?
-
-
no activity with D-glucose 6-phosphate, D-galactose 6-phosphate and free aldoses such as D-threose, D-xylose, D-arabinose or D-glucose
-
-
?
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
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
show the reaction diagram
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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thiamine diphosphate
thiamine diphosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
required
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-methyl-2-nitrosobenzene
weak inhibitory activity
1-nitrosonaphthalen-2-ol
weak inhibitory activity
3,5-dimethyl-4-nitroso-1-(propan-2-yl)-1H-pyrazole
weak inhibitory activity
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
N,N-dimethyl-4-nitrosoaniline
weak inhibitory activity
nitrosobenzene
weak inhibitory activity
(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
-
-
(2R)-2-(4-[2-[(acetylphosphinato)oxy]ethyl]-1H-1,2,3-triazol-1-yl)-3-(4-hydroxyphenyl)propanoate
-
-
(2R)-2-(4-[2-[(acetylphosphinato)oxy]ethyl]-1H-1,2,3-triazol-1-yl)-3-phenylpropanoate
-
most potent selective inhibitor
(2R)-2-(4-[2-[(acetylphosphinato)oxy]ethyl]-1H-1,2,3-triazol-1-yl)propanoate
-
-
(2S)-2-(4-[2-[(acetylphosphinato)oxy]ethyl]-1H-1,2,3-triazol-1-yl)-3-(4-hydroxyphenyl)propanoate
-
-
(2S)-2-(4-[2-[(acetylphosphinato)oxy]ethyl]-1H-1,2,3-triazol-1-yl)-3-phenylpropanoate
-
-
(2S)-2-(4-[2-[(acetylphosphinato)oxy]ethyl]-1H-1,2,3-triazol-1-yl)propanoate
-
-
(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
-
-
2-(1-benzyl-1H-1,2,3-triazol-4-yl)ethyl acetylphosphonate
-
-
2-(1-cyclohexyl-1H-1,2,3-triazol-4-yl)ethyl acetylphosphonate
-
-
2-(1-pentyl-1H-1,2,3-triazol-4-yl)ethyl acetylphosphonate
-
-
2-(1-[(2S)-1-[methyl(4-methylbenzene-1-sulfonyl)amino]-1-oxo-3-phenylpropan-2-yl]-1H-1,2,3-triazol-4-yl)ethyl acetylphosphonate
-
-
2-(1-[2-[methyl(methylsulfonyl)amino]-2-oxoethyl]-1H-1,2,3-triazol-4-yl)ethyl acetylphosphonate
-
-
2-[1-(2-hydroxyethyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
-
2-[1-(2-hydroxyphenyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
-
2-[1-(2-methoxy-2-oxoethyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
-
2-[1-(2-nitrobenzyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
-
2-[1-(2-phenylethyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
-
2-[1-(2-[methyl[(4-methylphenyl)sulfonyl]amino]-2-oxoethyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
-
2-[1-(3-hydroxyphenyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
-
2-[1-(4-hydroxyphenyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
-
2-[1-(4-nitrobenzyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
-
2-[1-(carboxymethyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
-
2-[1-(prop-2-en-1-yl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
-
2-[1-[4-(methoxycarbonyl)benzyl]-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
-
5-[(methoxyamino)methyl]benzene-1,2,4-triol
-
-
benzylacetylphosphonate
-
-
butyl acetyl phosphonate
-
-
butylacetylphosphonate
-
-
D-glyceraldehyde
-
competitive inhibition with respect to pyruvate
D-glyceraldehyde 3-phosphate
-
substrate inhibition
ethyl acetylphosphonate
-
-
hexyl acetylphosphonate
-
-
isopropylacetylphosphonate
-
weak inhibition
ketoclomazone
-
-
lithium but-3-yn-1-yl acetylphosphonate
-
-
methyl acetylphosphonate
-
-
Methylacetylphosphonate
-
-
octyl acetylphosphonate
-
-
pentyl acetylphosphonate
-
-
propyl acetylphosphonate
-
-
pyruvate
-
substrate inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.099
1-methyl-2-nitrosobenzene
at pH 8.0 and 37°C
0.041
1-nitrosonaphthalen-2-ol
at pH 8.0 and 37°C
0.512
2-hydroxy-4,6-dinitrobenzaldehyde
at pH 8.0 and 37°C
0.387
3,5-dimethyl-4-nitroso-1-(propan-2-yl)-1H-pyrazole
at pH 8.0 and 37°C
0.024
6-bromo-1-nitrosonaphthalen-2-ol
at pH 8.0 and 37°C
0.018
6-hydroxy-5-nitrosonaphthalene-2-sulfonamide
at pH 8.0 and 37°C
0.063
7-methoxy-1-nitrosonaphthalen-2-ol
at pH 8.0 and 37°C
38
D-glyceraldehyde
-
0.24
D-glyceraldehyde 3-phosphate
-
0.054
N,N-dimethyl-4-nitrosoaniline
at pH 8.0 and 37°C
0.096 - 0.123
pyruvate
0.0015 - 2.3
D-glyceraldehyde 3-phosphate
0.0011 - 1.61
pyruvate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6
1-methyl-2-nitrosobenzene
at pH 8.0 and 37°C
0.018
1-nitrosonaphthalen-2-ol
at pH 8.0 and 37°C
0.006
2-hydroxy-4,6-dinitrobenzaldehyde
at pH 8.0 and 37°C
0.023
3,5-dimethyl-4-nitroso-1-(propan-2-yl)-1H-pyrazole
at pH 8.0 and 37°C
0.033
6-bromo-1-nitrosonaphthalen-2-ol
at pH 8.0 and 37°C
0.02
6-hydroxy-5-nitrosonaphthalene-2-sulfonamide
at pH 8.0 and 37°C
0.022
7-methoxy-1-nitrosonaphthalen-2-ol
at pH 8.0 and 37°C
0.015
N,N-dimethyl-4-nitrosoaniline
at pH 8.0 and 37°C
0.045 - 1.38
D-glyceraldehyde 3-phosphate
2.6
pyruvate
-
pH 8.0, 37°C
additional information
additional information
-
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
at pH 8.0 and 37°C
0.045
1-nitrosonaphthalen-2-ol
at pH 8.0 and 37°C
0.06
3,5-dimethyl-4-nitroso-1-(propan-2-yl)-1H-pyrazole
at pH 8.0 and 37°C
1.3
6-bromo-1-nitrosonaphthalen-2-ol
at pH 8.0 and 37°C
1.1
6-hydroxy-5-nitrosonaphthalene-2-sulfonamide
at pH 8.0 and 37°C
0.35
7-methoxy-1-nitrosonaphthalen-2-ol
at pH 8.0 and 37°C
0.28
N,N-dimethyl-4-nitrosoaniline
at pH 8.0 and 37°C
0.01167
acetaldehyde
-
-
0.006
Butanal
-
-
0.035
D-glyceraldehyde
-
-
10.8 - 95
D-glyceraldehyde 3-phosphate
0.0035
propanal
-
-
0.037 - 32.2
pyruvate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0104
benzylacetylphosphonate
at pH 8.0 and 37°C
0.001
(1E,1'E)-O,O'-(ethane-1,2-diyl)bis[2,4,5-trihydroxybenzaldehyde oxime]
-
at pH 8.0 and 37°C
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 37°C
0.00033
(2R)-2-(4-[2-[(acetylphosphinato)oxy]ethyl]-1H-1,2,3-triazol-1-yl)-3-(4-hydroxyphenyl)propanoate
-
at pH 8.0 and 37°C
0.00009
(2R)-2-(4-[2-[(acetylphosphinato)oxy]ethyl]-1H-1,2,3-triazol-1-yl)-3-phenylpropanoate
-
at pH 8.0 and 37°C
0.0029
(2R)-2-(4-[2-[(acetylphosphinato)oxy]ethyl]-1H-1,2,3-triazol-1-yl)propanoate
-
at pH 8.0 and 37°C
0.001
(2S)-2-(4-[2-[(acetylphosphinato)oxy]ethyl]-1H-1,2,3-triazol-1-yl)-3-(4-hydroxyphenyl)propanoate
-
at pH 8.0 and 37°C
0.0021
(2S)-2-(4-[2-[(acetylphosphinato)oxy]ethyl]-1H-1,2,3-triazol-1-yl)-3-phenylpropanoate
-
at pH 8.0 and 37°C
0.0013
(2S)-2-(4-[2-[(acetylphosphinato)oxy]ethyl]-1H-1,2,3-triazol-1-yl)propanoate
-
at pH 8.0 and 37°C
0.0091
(E)-2,4,5-trihydroxybenzaldehyde O-benzyl oxime
-
at pH 8.0 and 37°C
0.0039
(E)-2,4,5-trihydroxybenzaldehyde O-methyl oxime
-
at pH 8.0 and 37°C
0.0026
(E)-2,4,5-trihydroxybenzaldehyde oxime
-
at pH 8.0 and 37°C
0.2
(E)-2,4-dihydroxybenzaldehyde O-methyl oxime
-
Ki above 0.2 mM, at pH 8.0 and 37°C
0.2
(E)-2,5-dihydroxybenzaldehyde O-methyl oxime
-
Ki above 0.2 mM, at pH 8.0 and 37°C
0.0151
(E)-2-fluoro-4,5-dihydroxybenzaldehyde O-methyl oxime
-
at pH 8.0 and 37°C
0.2
(E)-2-fluoro-4,5-dimethoxybenzaldehyde O-methyl oxime
-
Ki above 0.2 mM, at pH 8.0 and 37°C
0.0478
(E)-2-hydroxy-3-nitrobenzaldehyde O-methyl oxime
-
at pH 8.0 and 37°C
0.2
(E)-2-hydroxybenzaldehyde O-methyl oxime
-
Ki above 0.2 mM, at pH 8.0 and 37°C
0.0294
(E)-3,4,5-trihydroxybenzaldehyde O-methyl oxime
-
at pH 8.0 and 37°C
0.2
(E)-3,4-dihydroxy-5-methoxybenzaldehyde O-methyl oxime
-
Ki above 0.2 mM, at pH 8.0 and 37°C
0.2
(E)-4,5-difluoro-2-hydroxybenzaldehyde O-methyl oxime
-
Ki above 0.2 mM, at pH 8.0 and 37°C
0.2
(E)-4-hydroxy-3-nitrobenzaldehyde O-methyl oxime
-
Ki above 0.2 mM, at pH 8.0 and 37°C
0.075
(E)-5-[(2-methylhydrazono)methyl]benzene-1,2,4-triol
-
Ki above 0.075 mM, at pH 8.0 and 37°C
0.2
(E)-uracil-6-carbaldehyde O-methyl oxime
-
Ki above 0.2 mM, at pH 8.0 and 37°C
0.1
(E,Z)-2,4,5-trimethoxybenzaldehyde O-methyl oxime
-
Ki above 0.1 mM, at pH 8.0 and 37°C
0.2
(E,Z)-3,4-dihydroxybenzaldehyde O-methyl oxime
-
Ki above 0.2 mM, at pH 8.0 and 37°C
0.008
2-(1-benzyl-1H-1,2,3-triazol-4-yl)ethyl acetylphosphonate
-
at pH 8.0 and 37°C
0.00044
2-(1-cyclohexyl-1H-1,2,3-triazol-4-yl)ethyl acetylphosphonate
-
at pH 8.0 and 37°C
0.003
2-(1-pentyl-1H-1,2,3-triazol-4-yl)ethyl acetylphosphonate
-
at pH 8.0 and 37°C
0.00083
2-(1-[(2S)-1-[methyl(4-methylbenzene-1-sulfonyl)amino]-1-oxo-3-phenylpropan-2-yl]-1H-1,2,3-triazol-4-yl)ethyl acetylphosphonate
-
at pH 8.0 and 37°C
0.00052
2-(1-[2-[methyl(methylsulfonyl)amino]-2-oxoethyl]-1H-1,2,3-triazol-4-yl)ethyl acetylphosphonate
-
at pH 8.0 and 37°C
0.001
2-[1-(2-hydroxyethyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
at pH 8.0 and 37°C
0.00011
2-[1-(2-hydroxyphenyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
at pH 8.0 and 37°C
0.0013
2-[1-(2-methoxy-2-oxoethyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
at pH 8.0 and 37°C
0.0054
2-[1-(2-nitrobenzyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
at pH 8.0 and 37°C
0.008
2-[1-(2-phenylethyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
at pH 8.0 and 37°C
0.00047
2-[1-(2-[methyl[(4-methylphenyl)sulfonyl]amino]-2-oxoethyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
at pH 8.0 and 37°C
0.00032
2-[1-(3-hydroxyphenyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
at pH 8.0 and 37°C
0.006
2-[1-(4-hydroxyphenyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
at pH 8.0 and 37°C
0.0027
2-[1-(4-nitrobenzyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
at pH 8.0 and 37°C
0.00084
2-[1-(carboxymethyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
at pH 8.0 and 37°C
0.006
2-[1-(prop-2-en-1-yl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
at pH 8.0 and 37°C
0.008
2-[1-[4-(methoxycarbonyl)benzyl]-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
at pH 8.0 and 37°C
0.075
5-[(methoxyamino)methyl]benzene-1,2,4-triol
-
Ki above 0.075 mM, at pH 8.0 and 37°C
0.0056
butyl acetyl phosphonate
-
at pH 8.0 and 37°C
0.0026 - 0.0056
butylacetylphosphonate
3.2
D-glyceraldehyde
-
pH 8.0, 37°C
0.00671
ethyl acetylphosphonate
-
at pH 8.0 and 37°C
0.0089
hexyl acetylphosphonate
-
at pH 8.0 and 37°C
0.075
ketoclomazone
-
at pH 8.0 and 37°C
0.00047
lithium but-3-yn-1-yl acetylphosphonate
-
at pH 8.0 and 37°C
0.001
methyl acetylphosphonate
-
at pH 8.0 and 37°C
0.00324 - 1.08
Methylacetylphosphonate
0.0014
octyl acetylphosphonate
-
at pH 8.0 and 37°C
0.0017
pentyl acetylphosphonate
-
at pH 8.0 and 37°C
0.0071
propyl acetylphosphonate
-
at pH 8.0 and 37°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.291
1-methyl-2-nitrosobenzene
Escherichia coli
at pH 8.0 and 37°C
1.065
1-nitrosonaphthalen-2-ol
Escherichia coli
at pH 8.0 and 37°C
2
3,5-dimethyl-4-nitroso-1-(propan-2-yl)-1H-pyrazole
Escherichia coli
IC50 above 2.0 mM, at pH 8.0 and 37°C
0.522
6-bromo-1-nitrosonaphthalen-2-ol
Escherichia coli
at pH 8.0 and 37°C
0.354
6-hydroxy-5-nitrosonaphthalene-2-sulfonamide
Escherichia coli
at pH 8.0 and 37°C
2
7-methoxy-1-nitrosonaphthalen-2-ol
Escherichia coli
IC50 above 2.0 mM, at pH 8.0 and 37°C
0.844
N,N-dimethyl-4-nitrosoaniline
Escherichia coli
at pH 8.0 and 37°C
0.208
nitrosobenzene
Escherichia coli
at pH 8.0 and 37°C
0.0018 - 10
Methylacetylphosphonate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1167
HPLC method, at pH 8.0 and 37°C
1233
coupled assay, at pH 8.0 and 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000
2 * 60000, gel filtration
65000 - 69000
SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 60000, gel filtration
additional information
-
secondary structure analysis, the enzyme possesses a three domain structure, the active site of DXS is located at the interface of domains I and II in the same monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
H299A
-
the mutant shows reduced activity compared to the wild type enzyme
H299N
-
the mutant shows reduced activity compared to the wild type enzyme
H49A
-
the mutant shows reduced activity compared to the wild type enzyme
R478A
-
the mutant shows reduced affinity for D-glyceraldehyde 3-phosphate compared to the wild type enzyme
additional information
-
overexpression of the bacterial dxs gene in Solanum tuberosum tubers perturbs the isoprenoid metabolic network, expression analysis of the nine transgenic lines shows that four exhibit the altered regulation phenotype and five show a wild-type phenotype, the tubers with altered regulation phenotype e.g. show earlier apical bud growth with an 56-day-lag period before sprouting with altered phytohormone levels, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression
recombinant His-tagged enzymes from Escherichia coli by nickel affinity and anion exchange chromatography, and gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression
expressed in Escherichia coli BL21(DE3) cells
-
gene dxs, overexpression in transgenic Solanum tuberosum tubers
-
overexpression of the His-tagged enzyme in Escherichia coli, production of the selenomethionine enzyme form in Escherichia coli strain B834
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
-
DXS is an attractive target for the development of antibiotics, antimalarials, and herbicides
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kuzuyama, T.; Takagi, M.; Takahashi, S.; Seto, H.
Cloning and characterization of 1-deoxy-D-xylulose 5-phosphate synthase from Streptomyces sp. strain CL190, which uses both the mevalonate and nonmevalonate pathways for isopentenyl diphosphate biosynthesis
J. Bacteriol.
182
891-897
2000
Streptomyces sp., Escherichia coli (P77488), Escherichia coli
Manually annotated by BRENDA team
Lois, L.M.; Campos, N.; Putra, S.R.; Danielsen, K.; Rohmer, M.; Boronat, A.
Cloning and characterization of a gene from Escherichia coli encoding a transketolase-like enzyme that catalyzes the synthesis of D-1-deoxyxylulose 5-phosphate, a common precursor for isoprenoid, thiamin, and pyridoxol biosynthesis
Proc. Natl. Acad. Sci. USA
95
2105-2110
1998
Escherichia coli (P77488)
Manually annotated by BRENDA team
Querol, J.; Rodriguez-Concepcion, M.; Boronat, A.; Imperial, S.
Essential role of residue H49 for activity of Escherichia coli 1-deoxy-D-xylulose 5-phosphate synthase, the enzyme catalyzing the first step of the 2-C-methyl-D-erythritol 4-phosphate pathway for isoprenoid synthesis
Biochem. Biophys. Res. Commun.
289
155-160
2001
Escherichia coli (P77488), Escherichia coli
Manually annotated by BRENDA team
Schrmann, M.; Schrmann, M.; Sprenger, G.A.
Fructose 6-phosphate aldolase and 1-deoxy-D-xylulose 5-phosphate synthase from Escherichia coli as tools in enzymatic synthesis of 1-deoxysugars
J. Mol. Catal. B
19-20
247-252
2002
Escherichia coli
-
Manually annotated by BRENDA team
Querol, J.; Grosdemange-Billiard, C.; Rohmer, M.; Boronat, A.; Imperial, S.
Enzymatic synthesis of 1-deoxysugar-phosphates using E. coli 1-deoxy-D-xylulose 5-phosphate synthase
Tetrahedron Lett.
43
8265-8268
2002
Escherichia coli
-
Manually annotated by BRENDA team
Xiang, S.; Usunow, G.; Lange, G.; Busch, M.; Tong, L.
Crystal structure of 1-deoxy-D-xylulose 5-phosphate synthase, a crucial enzyme for isoprenoids biosynthesis
J. Biol. Chem.
282
2676-2682
2007
Deinococcus radiodurans, Escherichia coli
Manually annotated by BRENDA team
Morris, W.L.; Ducreux, L.J.; Hedden, P.; Millam, S.; Taylor, M.A.
Overexpression of a bacterial 1-deoxy-D-xylulose 5-phosphate synthase gene in potato tubers perturbs the isoprenoid metabolic network: implications for the control of the tuber life cycle
J. Exp. Bot.
57
3007-3018
2006
Escherichia coli
Manually annotated by BRENDA team
Cordoba, E.; Salmi, M.; Leon, P.
Unravelling the regulatory mechanisms that modulate the MEP pathway in higher plants
J. Exp. Bot.
60
2933-2943
2009
Arabidopsis thaliana (Q38854), Escherichia coli, Ginkgo biloba, Medicago truncatula (Q8L692), Medicago truncatula (Q8L693), Oryza sativa, Picea abies (A7LA00), Picea abies (A7LA01), Picea abies (A7LA02), Solanum lycopersicum, Solanum tuberosum, Zea mays
Manually annotated by BRENDA team
Brammer, L.A.; Meyers, C.F.
Revealing substrate promiscuity of 1-deoxy-D-xylulose 5-phosphate synthase
Org. Lett.
11
4748-4751
2009
Escherichia coli
Manually annotated by BRENDA team
Brammer, L.A.; Smith, J.M.; Wade, H.; Meyers, C.F.
1-Deoxy-D-xylulose 5-phosphate synthase catalyzes a novel random sequential mechanism
J. Biol. Chem.
286
36522-36531
2011
Escherichia coli
Manually annotated by BRENDA team
Kirby, J.; Nishimoto, M.; Chow, R.W.; Baidoo, E.E.; Wang, G.; Martin, J.; Schackwitz, W.; Chan, R.; Fortman, J.L.; Keasling, J.D.
Enhancing terpene yield from sugars via novel routes to 1-deoxy-D-xylulose 5-phosphate
Appl. Environ. Microbiol.
81
130-138
2015
Escherichia coli (P77735), Escherichia coli, Escherichia coli MG1655 (P77735)
Manually annotated by BRENDA team
Morris, F.; Vierling, R.; Boucher, L.; Bosch, J.; Freel Meyers, C.L.
DXP synthase-catalyzed C-N bond formation: nitroso substrate specificity studies guide selective inhibitor design
ChemBioChem
14
1309-1315
2013
Escherichia coli (P77488), Escherichia coli
Manually annotated by BRENDA team
Bartee, D.; Morris, F.; Al-Khouja, A.; Freel Meyers, C.L.
Hydroxybenzaldoximes are D-GAP-competitive inhibitors of E. coli 1-deoxy-D-xylulose-5-phosphate synthase
ChemBioChem
16
1771-1781
2015
Escherichia coli
Manually annotated by BRENDA team
Sanders, S.; Vierling, R.J.; Bartee, D.; DeColli, A.A.; Harrison, M.J.; Aklinski, J.L.; Koppisch, A.T.; Freel Meyers, C.L.
Challenges and hallmarks of establishing alkylacetylphosphonates as probes of bacterial 1-deoxy-D-xylulose 5-phosphate synthase
ACS Infect. Dis.
3
467-478
2017
Escherichia coli, Escherichia coli MG1655
Manually annotated by BRENDA team
Bartee, D.; Freel Meyers, C.L.
Targeting the unique mechanism of bacterial 1-deoxy-D-xylulose-5-phosphate synthase
Biochemistry
57
4349-4356
2018
Escherichia coli
Manually annotated by BRENDA team
DeColli, A.A.; Zhang, X.; Heflin, K.L.; Jordan, F.; Freel Meyers, C.L.
Active site histidines link conformational dynamics with catalysis on anti-infective target 1-deoxy-D-xylulose 5-phosphate synthase
Biochemistry
58
4970-4982
2019
Escherichia coli
Manually annotated by BRENDA team
Zhou, J.; Yang, L.; DeColli, A.; Freel Meyers, C.; Nemeria, N.S.; Jordan, F.
Conformational dynamics of 1-deoxy-D-xylulose 5-phosphate synthase on ligand binding revealed by H/D exchange MS
Proc. Natl. Acad. Sci. USA
114
9355-9360
2017
Escherichia coli (P77488), Escherichia coli
Manually annotated by BRENDA team
Liang, Y.F.; Liu, H.; Li, H.; Gao, W.Y.
Determination of the activity of 1-deoxy-D-xylulose 5-phosphate synthase by pre-column derivatization-HPLC using 1,2-diamino-4,5-methylenedioxybenzene as a derivatizing reagent
Protein J.
38
160-166
2019
Escherichia coli (P77488)
Manually annotated by BRENDA team