Information on EC 4.2.3.4 - 3-dehydroquinate synthase

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

EC NUMBER
COMMENTARY
4.2.3.4
-
RECOMMENDED NAME
GeneOntology No.
3-dehydroquinate synthase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate = 3-dehydroquinate + phosphate
show the reaction diagram
requires Co2+. The hydrogen atoms on C-7 of the substrate are retained on C-2 of the product
-
-
-
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate = 3-dehydroquinate + phosphate
show the reaction diagram
reaction follows a rapid-equilibrium random mechanism
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
aldol condensation
-
intramolecular
cyclization
P07639
-
cyclization
-
-
cyclization
-, P56081
-
oxidation
-
alcohol oxidation
reduction
-
carbonyl reduction
elimination
-
-
P-O bond cleavage
-
additional information
-
DHQS itself is of interest because it apparently catalyzes five individual reactions, alcohol oxidation, phosphate omega-elimination, carbonyl reduction, ring opening and intramolecular aldol condensation, in a single active site as well as being a drug target
PATHWAY
KEGG Link
MetaCyc Link
3-dehydroquinate biosynthesis I
-
Biosynthesis of secondary metabolites
-
Metabolic pathways
-
Phenylalanine, tyrosine and tryptophan biosynthesis
-
SYSTEMATIC NAME
IUBMB Comments
3-deoxy-D-arabino-hept-2-ulosonate-7-phosphate phosphate-lyase (cyclizing; 3-dehydroquinate-forming)
Requires Co2+ and bound NAD+. The hydrogen atoms on C-7 of the substrate are retained on C-2 of the product.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3-dehydroquinate synthase
E6Y3G5
-
3-dehydroquinate synthase
P07639
-
3-dehydroquinate synthase
P0A4Z4
-
3-dehydroquinate synthase
-
-
3-dehydroquinate synthetase
-
-
-
-
3-dehydroquinic acid synthetase
-
-
-
-
5-dehydroquinate synthase
-
-
-
-
5-dehydroquinic acid synthetase
-
-
-
-
dehydroquinate synthase
-
-
-
-
dehydroquinate synthase
-
-
dehydroquinate synthase
-
-
dehydroquinate synthase
Escherichia coli RB791
-
;
-
dehydroquinate synthase
-
-
dehydroquinate synthase
P0A4Z4
-
dehydroquinate synthase
-
-
dehydroquinate synthase
-
-
dehydroquinate synthetase
-
-
-
-
DHQ synthase
P07639
-
DHQ synthase
P0A4Z4
-
DHQS
Q8U0A8
-
EC 4.6.1.3
-
-
formerly
-
synthase, 5-dehydroquinate
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
37211-77-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
overview
-
-
Manually annotated by BRENDA team
Escherichia coli RB791
-
-
-
Manually annotated by BRENDA team
Hansenula henricii
-
-
-
Manually annotated by BRENDA team
overview
-
-
Manually annotated by BRENDA team
Saccharomycopsis lipolytica
-
-
-
Manually annotated by BRENDA team
Sorghum sp.
-
-
-
Manually annotated by BRENDA team
strain HB8
Uniprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
Q8U0A8
the enzyme catalyses the second step of the shikimate pathway to aromatic compounds
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(3R)-3-fluoro-3-deoxy-D-arabino-heptulosonate 7-phosphate
(6R)-6-fluoro-dehydroquinate
show the reaction diagram
-
-
-
-
?
(3S)-3-fluoro-3-deoxy-D-arabino-heptulosonate 7-phosphate
(6S)-6-fluoro-dehydroquinate + 1-epi-(6S)-6-fluoro-dehydroquinate
show the reaction diagram
-
-
1-epi-(6S)-6-fluoro-dehydroquinate formation occurs by an unusual partial leakage of a reaction intermediate from the enzyme
-
?
3-deoxy-arabino-heptulonate 7-phosphate
3-dehydroquinate + phosphate
show the reaction diagram
-
-
-
-
?
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate
3-dehydroquinate + phosphate
show the reaction diagram
-
-
-
-
?
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate
3-dehydroquinate + phosphate
show the reaction diagram
-
-
-
-
?
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate
3-dehydroquinate + phosphate
show the reaction diagram
P07639
-
-
-
ir
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate
3-dehydroquinate + phosphate
show the reaction diagram
P0A4Z4
-
-
-
ir
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate
3-dehydroquinate + phosphate
show the reaction diagram
Q8U0A8
-, the enzyme catalyses the second step of the shikimate pathway to aromatic compounds
-
-
?
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate
3-dehydroquinate + phosphate
show the reaction diagram
Escherichia coli RB791
-
-
-
-
?
3-deoxy-D-arabino-heptulosonate 7-phosphate
3-dehydroquinate + phosphate
show the reaction diagram
-
-
-
-
-
3-deoxy-D-arabino-heptulosonate 7-phosphate
3-dehydroquinate + phosphate
show the reaction diagram
-, P56081
second key step in the shikimate pathway which is crucial for the aromatic amino acid metabolism in bacteria, fungi, and plants, but not in mammals
-
-
?
3-deoxy-D-arabino-heptulosonic acid 7-phosphate
3-dehydroquinate + phosphate
show the reaction diagram
-
-
-
ir
3-deoxy-D-arabino-heptulosonic acid 7-phosphate
3-dehydroquinate + phosphate
show the reaction diagram
-
-
-
ir
3-deoxy-D-arabino-heptulosonic acid 7-phosphate
3-dehydroquinate + phosphate
show the reaction diagram
-
-
-
ir
3-deoxy-D-arabino-heptulosonic acid 7-phosphate
3-dehydroquinate + phosphate
show the reaction diagram
-
-
-
-
3-deoxy-D-arabino-heptulosonic acid 7-phosphate
3-dehydroquinate + phosphate
show the reaction diagram
Neurospora crassa, Neurospora crassa 74-OR23-1A
-
-
-
-
3-deoxy-D-arabino-heptulosonic acid 7-phosphate
?
show the reaction diagram
-
-
-
-
-
3-deoxy-D-arabino-heptulosonic acid 7-phosphate
?
show the reaction diagram
-
-
-
-
-
3-deoxy-D-arabino-heptulosonic acid 7-phosphate
?
show the reaction diagram
-
-
-
-
-
3-deoxy-D-arabinoheptulosonate 7-phosphate
3-dehydroquinate + phosphate
show the reaction diagram
-
shikimate pathway is present in all organisms except mammals
-
-
?
additional information
?
-
-
enzyme plays an essential role in the synthesis of aromatic compounds in the shikimate pathway
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate
3-dehydroquinate + phosphate
show the reaction diagram
P07639
-
-
-
ir
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate
3-dehydroquinate + phosphate
show the reaction diagram
P0A4Z4
-
-
-
ir
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate
3-dehydroquinate + phosphate
show the reaction diagram
Q8U0A8
the enzyme catalyses the second step of the shikimate pathway to aromatic compounds
-
-
?
3-deoxy-D-arabino-heptulosonate 7-phosphate
3-dehydroquinate + phosphate
show the reaction diagram
-, P56081
second key step in the shikimate pathway which is crucial for the aromatic amino acid metabolism in bacteria, fungi, and plants, but not in mammals
-
-
?
3-deoxy-D-arabino-heptulosonic acid 7-phosphate
?
show the reaction diagram
-
-
-
-
-
3-deoxy-D-arabino-heptulosonic acid 7-phosphate
?
show the reaction diagram
-
-
-
-
-
3-deoxy-D-arabino-heptulosonic acid 7-phosphate
?
show the reaction diagram
-
-
-
-
-
3-deoxy-D-arabinoheptulosonate 7-phosphate
3-dehydroquinate + phosphate
show the reaction diagram
-
shikimate pathway is present in all organisms except mammals
-
-
?
additional information
?
-
-
enzyme plays an essential role in the synthesis of aromatic compounds in the shikimate pathway
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NAD+
-
1 mol of NAD+ per mol of protein
NAD+
Sorghum sp.
-
-
NAD+
-
determination of constants of the cyclic reduction and oxidation of NAD+ and NADH. There is a transient increase in absorbance at 340 nm associated with NADH formation followed by its oxidation. The rates of NAD+ to NADH to NAD+ conversions are not rate limiting because they are larger than the kcat value
NAD+
-
required for activity
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Cd2+
-
reconstitution of the apoenzyme with Cd2+ restores activity to12% of the level observed with the Co2+-holoenzyme
Cd2+
Q8U0A8
activates
Co2+
Sorghum sp.
-
-
Co2+
-
contains 1 mol of Co2+, required for 100% activity
Co2+
-
required
Co2+
Q8U0A8
activates
Cu2+
-
-
Cu2+
-
reconstitution of the apoenzyme with Zn2+ restores activity to 9% of the level observed with the Co2+-holoenzyme
Mn2+
-
reconstitution of the apoenzyme with Mn2+ restores activity to 10% of the level observed with the Co2+-holoenzyme
Ni2+
-
reconstitution of the apoenzyme with Ni2+ restores activity to 23% of the level observed with the Co2+-holoenzyme
Zn2+
P83703
binding on the C-terminal alpha-helical domain
Zn2+
-, P56081
-
Zn2+
-
reconstitution of the apoenzyme with Zn2+ restores activity to 53% of the level observed with the Co2+-holoenzyme
Zn2+
Q8U0A8
activates
Mn2+
Q8U0A8
activates
additional information
-
no activity in the presence of Mg2+, Ca2+, Sr2+, and Ba2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(-)-epicatechin gallate
-
-
(-)-epigallocatechin gallate
-
-
1,10-phenanthroline
-
-
3-deoxy-D-arabino-heoptulosonic acid
-
-
3-deoxy-D-arabino-heptulosonic acid 7-homophosphate
-
-
-
3-deoxy-D-arabino-heptulosonic acid 7-phosphonate
-
-
3-deoxy-D-arabino-heptulosonic acid 7-phosphonate
-
-
3-deoxy-D-arabino-heptulosonic acid-2-O-methylglycoside 7-phosphate
-
-
-
alpha-(2,6-anhydro-3-deoxy-D-arabino-heptulopyranosid)onate 7-phosphate
-
-
alpha-(2,6-anhydro-3-deoxy-D-arabino-heptulopyranosid)onate 7-phosphate
-
-
alpha-(2,6-anhydro-3-deoxy-D-arabino-heptulopyranosid)onate 7-phosphonate
-
-
beta-(2,6-anhydro-3-deoxy-D-arabino-heptulopyranosid)onate 7-phosphate
-
-
bistrispropane
-
-
carabaphosphonate
-
-
D-2-cis-hydroquinic acid
-
-
D-gluco-3-heptulosonate 7-phosphate
-
-
D-gluco-heptulosonate 7-homophosphonate
-
-
D-gluco-heptulosonate 7-phosphonate
-
-
diethyl dicarbonate
-
-
dithiothreitol
-
-
EDTA
Sorghum sp.
-
-
EDTA
-
0.1 mM, complete loss of activity. Addition of Co2+, Zn2+ and Ca2+ leads to, respectively, full, 43% and 38% recovery of the enzyme activity
EDTA
-
treatment of the Co2+-holoenzyme with EDTA in the absence of substrate results in the rapid loss of catalytic activity
EDTA
Q8U0A8
inactivates the enzyme, and enzyme activity is restored by several divalent metal ions including (in order of decreasing effectiveness) Cd2+, Co2+, Zn2+, and Mn2+
epoxyshikimic acid
-
-
Gallic acid
-
-
HTS 11955
-, P56081
-
NADH
Sorghum sp.
-
-
RH00573
-, P56081
-
[(1R)-(1alpha,3beta,4alpha ,5beta)]-5-(2-phosphonoethyl)-1,3,4-trihydroxycyclohexane-1-carboxylic acid
-
-
-
[(1R)-(1alpha,3beta,4alpha,5beta)]-1,4,5-trihydroxy-3-(phosphonooxy)-cyclohexane-1-carboxylate
-
-
-
[(1R)-(1alpha,3beta,4alpha,5beta)]-5-(E)-(2-phosphonoethenyl)-1,3,4-trihydroxycyclohexane-1-carboxylic acid
-
-
-
[(1R)-(1alpha,3beta,4alpha,5beta)]-5-(phosphonomethyl)-l,3,4-trihydroxycyclohexane-1-carboxylic acid
-
slow binding inhibitor
-
[(1R)-(1alpha,3beta,4alpha,5beta)]-5-(Z)-(2-phosphonoethenyl)-1,3,4-trihydroxycyclohexane-1-carboxylic acid
-
-
-
[(2R)-(2alpha,4beta,5alpha,6beta)]-6-(2-phosphonoethyl)-2,4,5-trihydroxytetrahydropyran-2-carboxylate
-
-
-
[(2R)-(2alpha,4beta,5alpha,6beta)]-6-(phosphonomethyl)-2,4,5-trihydroxytetrahydropyran-2-carboxylate
-
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NAD+
P83703
binding on the N-terminal alpha/beta domain
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0016
-
(3R)-3-fluoro-3-deoxy-D-arabino-heptulosonate 7-phosphate
-
pH 6.8, 25C
0.002
-
(3R)-3-fluoro-3-deoxy-D-arabino-heptulosonate 7-phosphate
-
pH 6.8, 25C
0.0087
-
(3R)-3-fluoro-3-deoxy-D-arabino-heptulosonate 7-phosphate
-
pH 6.8, 25C
0.021
-
(3S)-3-fluoro-3-deoxy-D-arabino-heptulosonate 7-phosphate
-
pH 6.8, 25C
0.029
-
(3S)-3-fluoro-3-deoxy-D-arabino-heptulosonate 7-phosphate
-
pH 6.8, 25C
0.064
-
(3S)-3-fluoro-3-deoxy-D-arabino-heptulosonate 7-phosphate
-
pH 6.8, 25C
0.00055
-
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate
-
at 20C and pH 8.5
0.0006
-
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate
-
at 20C and pH 6.5
0.0032
-
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate
-
pH 6.8, 25C
0.0037
-
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate
-
pH 6.8, 25C
0.0037
-
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate
Q8U0A8
pH 6.8, 60C
0.0057
-
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate
-
pH 6.8, 25C
0.021
-
3-deoxy-D-arabino-heptulosonate 7-phosphate
-
-
0.228
-
3-deoxy-D-arabino-heptulosonate 7-phosphate
-
mutant R130K
0.0022
-
3-deoxy-D-arabino-heptulosonate phosphate
-
-
0.0014
-
3-deoxy-D-arabino-heptulosonic acid 7-phosphate
-
-
0.033
0.055
3-deoxy-D-arabino-heptulosonic acid 7-phosphate
-
-
0.033
0.055
3-deoxy-D-arabino-heptulosonic acid 7-phosphate
-
-
0.0019
-
NAD+
-
-
0.014
-
NAD+
-
mutant R130K
0.055
-
NAD+
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.3
-
(3R)-3-fluoro-3-deoxy-D-arabino-heptulosonate 7-phosphate
-
pH 6.8, 25C
2.5
-
(3R)-3-fluoro-3-deoxy-D-arabino-heptulosonate 7-phosphate
-
pH 6.8, 25C
3.3
-
(3R)-3-fluoro-3-deoxy-D-arabino-heptulosonate 7-phosphate
-
pH 6.8, 25C
0.3
-
(3S)-3-fluoro-3-deoxy-D-arabino-heptulosonate 7-phosphate
-
pH 6.8, 25C
0.9
-
(3S)-3-fluoro-3-deoxy-D-arabino-heptulosonate 7-phosphate
-
pH 6.8, 25C
1.3
-
(3S)-3-fluoro-3-deoxy-D-arabino-heptulosonate 7-phosphate
-
pH 6.8, 25C
0.5
-
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate
-
pH 6.8, 25C
3
-
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate
-
pH 6.8, 25C
3
-
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate
Q8U0A8
pH 6.8, 60C
16
-
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate
-
pH 6.8, 25C
25000
-
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate
-
at 20C and pH 7.8
6.8
-
3-deoxy-D-arabino-heptulosonate 7-phosphate
-
-
19
-
3-deoxy-D-arabino-heptulosonic acid 7-phosphate
-
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
34.5
-
(3R)-3-fluoro-3-deoxy-D-arabino-heptulosonate 7-phosphate
-
pH 6.8, 25C
313551
1562
-
(3R)-3-fluoro-3-deoxy-D-arabino-heptulosonate 7-phosphate
-
pH 6.8, 25C
313551
1650
-
(3R)-3-fluoro-3-deoxy-D-arabino-heptulosonate 7-phosphate
-
pH 6.8, 25C
313551
14
-
(3S)-3-fluoro-3-deoxy-D-arabino-heptulosonate 7-phosphate
-
pH 6.8, 25C
313548
14.3
-
(3S)-3-fluoro-3-deoxy-D-arabino-heptulosonate 7-phosphate
-
pH 6.8, 25C
313548
44.8
-
(3S)-3-fluoro-3-deoxy-D-arabino-heptulosonate 7-phosphate
-
pH 6.8, 25C
313548
156
-
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate
-
pH 6.8, 25C
218525
811
-
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate
-
pH 6.8, 25C
218525
811
-
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate
Q8U0A8
pH 6.8, 60C
218525
2807
-
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate
-
pH 6.8, 25C
218525
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0000008
-
CBP
-, P56081
contains 5 functional groups (OH, COOH and phosphate)
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.061
-
HTS 11955
-, P56081
in 100 mM DMSO, compound carries N or O atoms and functional groups (CN, NH2 and NO2)
0.0845
-
RH 00573
-, P56081
in 100 mM DMSO, compound carries N or O atoms and functional groups (CN, NH2 and NO2)
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.009
-
P07639
strain NR7, plasmid pKL4.79, activity is measured for cells removed from the fermentor 24 h after inoculation
0.01
-
P07639
strain NR7, plasmid pKL4.79, activity is measured for cells removed from the fermentor 36 h after inoculation
0.011
-
P07639
strain NR7, plasmid pKL4.79, activity is measured for cells removed from the fermentor 48 h after inoculation
0.015
-
P07639
strain NR7, plasmid pNR8.075, activity is measured for cells removed from the fermentor 24 h after inoculation
0.016
-
P07639
strain NR7, plasmid pNR8.075, activity is measured for cells removed from the fermentor 36 h after inoculation; strain NR7, plasmid pNR8.075, activity is measured for cells removed from the fermentor 48 h after inoculation; strain NR7, plasmid pNR8.288, activity is measured for cells removed from the fermentor 48 h after inoculation
0.017
-
P07639
strain NR7, plasmid pNR8.288, activity is measured for cells removed from the fermentor 24 h after inoculation; strain NR7, plasmid pNR8.288, activity is measured for cells removed from the fermentor 36 h after inoculation
0.022
-
P07639
strain NR7, plasmid pNR9.127, activity is measured for cells removed from the fermentor 36 h after inoculation
0.023
-
P07639
strain NR7, plasmid pNR8.294, activity is measured for cells removed from the fermentor 48 h after inoculation
0.024
-
P07639
strain NR7, plasmid pNR9.127, activity is measured for cells removed from the fermentor 48 h after inoculation
0.027
-
P07639
strain NR7, plasmid pNR9.127, activity is measured for cells removed from the fermentor 24 h after inoculation
0.039
-
P07639
strain NR7, plasmid pNR8.294, activity is measured for cells removed from the fermentor 36 h after inoculation
0.043
-
P07639
strain NR7, plasmid pNR8.294, activity is measured for cells removed from the fermentor 24 h after inoculation
0.07
-
-
mutant R130K
0.53
-
P07639
strain NR7, plasmid pNR9.056, activity is measured for cells removed from the fermentor 24 h after inoculation
0.59
-
-
-
0.92
-
P07639
strain NR7, plasmid pNR9.056, activity is measured for cells removed from the fermentor 36 h after inoculation
1.17
-
P07639
strain NR7, plasmid pNR9.056, activity is measured for cells removed from the fermentor 48 h after inoculation
additional information
-
-
-
additional information
-
-
-
additional information
-
Sorghum sp.
-
-
additional information
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additional information
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additional information
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additional information
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additional information
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Inactivation of enzymes in the shikimate pathway results in attenuation of virulence and loss of viability in a large number of bacterial species
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.8
-
Q8U0A8
-
7
7.5
Sorghum sp.
-
-
7
-
-, P56081
assay at
7.4
8.4
-
-
7.5
-
P07639
activity assay
7.6
-
-
activity assay
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.3
9.5
Q8U0A8
pH 6.3: 65% of maximal activity, pH 9.5: about 65% of maximal activity
6.8
8
Sorghum sp.
-
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
activity assay
37
-
-, P56081
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
90
-
Q8U0A8
active up to
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Sorghum sp.
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
Helicobacter pylori (strain ATCC 700392 / 26695)
Staphylococcus aureus (strain MRSA252)
Staphylococcus aureus (strain MRSA252)
Staphylococcus aureus (strain MRSA252)
Staphylococcus aureus (strain MRSA252)
Staphylococcus aureus (strain MRSA252)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
24000
-
-
enzyme complex with chorismate synthase, SDS-PAGE
38100
-
-
determined by SDS-PAGE
38140
-
-
determined by ESI-MS
38880
-
-
denaturing gel electrophoresis; HPLC
38880
-
-
comparison of values from bacteria + yeasts
38880
-
-
amino acid sequence
40000
44000
-
HPLC
43000
-
-
SDS-PAGE
43000
-
-
gel filtration
44000
-
-
HPLC
57000
-
-
gel filtration
66000
-
-
gel filtration
67000
-
-
gel filtration
72000
-
Q8U0A8
gel filtration
78400
-
P83703
dynamic light scattering method, bimodal analysis
290000
330000
Sorghum sp.
-
-
290000
330000
-
gel electrophoresis after cross-linkage with dimethyl suberimidate
290000
330000
-
sedimentation equilibrum centrifugation
290000
330000
-
-
290000
330000
-
gel filtration
290000
330000
-
-
290000
330000
-
arom-multienzyme complex, gel filtration
290000
330000
Saccharomycopsis lipolytica, Wickerhamomyces anomalus
-
-
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 45189, electrospray ionisation mass spectrometry, His-tagged protein
?
-
x * 38888, electrospray ionisation mass spectrometry
?
-
x * 37397, electrospray ionisation mass spectrometry
dimer
-
2 * 165000, SDS-electrophoresis
dimer
-, P56081
electron density map reveals 2 molecules (AB) per asymmetric unit. Disordered regions include the N-terminal 1-3 segment and 2 loop regions. The electron density map shows the presence of a piece of density in each subunit, which could be modeled as a zinc ion in each subunit. Subunits A and B associate into an AB dimer related by a non-crystallographic two-fold axis, and three AB dimers assemble into a hexamer along the 3-fold axis
homodimer
P83703
dynamic light scattering with 1 mg/ml protein at pH 8.0, 18C in 20 mM Tris-HCl buffer
homodimer
Q8U0A8
2 * 37397, electrospray ionisation mass spectrometry
monomer
-
1 * 40000-44000, HPLC
monomer
-
1 * 57000, gel filtration
monomer
-
1 * 43000, gel filtration
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
sitting-drop vapour-diffusion crystallisation at 4C utilising microbridges, crystals of unliganded enzyme as well as in complexes with NAD+, the substrate analogue [1R-(1alpha,3beta,4alpha,5beta)]-5-phosphonomethyl-1,3,4-trihydroxycyclohexane-1-carboxylic acid and together with both, NAD+ and [1R-(1alpha,3beta,4alpha,5beta)]-5-phosphonomethyl-1,3,4-trihydroxycyclohexane-1-carboxylic acid
-
sitting-drop vapour-diffusion, crystals of unliganded enzyme, binary complexes with either the substrate analogue, carbaphosphonate or the cofactor NADH, as well as the ternary enzyme-carbaphosphonate-cofactor complex
-
sitting-drop vapour-diffusion, structure at 1.7 A resolution
-
obtained in a solution containing 20 mM NAD+
-, P56081
sitting-drop vapour-diffusion crystallisation at 4C utilising microbridges, crystals of unliganded enzyme as well as in complexes with NAD, the substrate analogue [1R-(1alpha,3beta,4alpha,5beta)]-5-phosphonomethyl-1,3,4-trihydroxycyclohexane-1-carboxylic acid and together with both, NAD and [1R-(1alpha,3beta,4alpha,5beta)]-5-phosphonomethyl-1,3,4-trihydroxycyclohexane-1-carboxylic acid
Q6GGU4
oil microbatch method, homodimer 1.8 A resolution
P83703
by using the hanging-drop vapour-diffusion method with different screening kits, yields crystals belonging to the tetragonal space group, crystals of DHQS obtained in sitting-drop setups using a hydra automated high-throughput crystal screening machine with different screening kits: (a) 0.1 M sodium malonate pH 4.0, 12% PEG 3350, (b) 0.2 M sodium malonate pH 6.0, 20% PEG 3350, (c) 0.1 M Tris pH 8.5, 2.0 M ammonium sulfate, (d) 0.15 M caesium chloride, 15% PEG 3350, (e) 1.0 M sodium citrate, 0.1 M CHES pH 9.5, (f) 0.2 M ammonium sulfate, 0.1 M bis-Tris pH 5.5, 25% PEG 3350, (g) 0.2 M ammonium sulfate, 0.1 M MES pH 6.5, 30% PEG MME 5000, (h) 0.02 M zinc chloride, 20% PEG 3350. Best crystals are obtained after two weeks from a reservoir containing 0.2 M ammonium sulfate, 0.1 M MES monohydrate pH 6.0 and 31%PEG MME 5000
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
-20
-
-
inactivation
4
-
-
48 h, 65% activity
45
-
-
3-deoxy-D-arabino-heptulosonate protects against inactivation
55
-
-
inactivation
90
-
Q8U0A8
Tm-value
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
freezing and thawing , inactivation
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-70C, more than 1 year
-
4C, free enzyme in the presence of Co2+ and NAD+, at pH 7.5 in 100 mM MOPS buffer, several months, the enzyme remains stable
-
-20C, more than 1 year
-
50% glycerol
-
1 month
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
together with chorismate synthase
-
expressed HpDHQS protein is purified by immobilized nickel-ion chromatography
-, P56081
using a Q-Sepharose Fast Flow, a HiLoad 16/10 phenyl-Sepharose, and a Sephacryl S-200 HR column
-
arom-multienzyme complex
-
partial
Sorghum sp.
-
by Ni2+-NTA affinity chromatography, enzyme is subjected to a TEV protease cleavage reaction to cleave the six His-tag residues at the N-terminus, further purification by ion-exchange chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-
overexpression of the dehydroquinate synthase domain of the pentafunctional AROM protein in Escherichia coli
-
overexpression in Escherichia coli
-
expression in Escherichia coli
-
The aroB gene encoding HpDHQS is amplified from genomic DNA by PCR and inserted into the pQE30 expression vector. The HpDHQS protein is expressed from Escherichia coli JM109 cells transformed with pQE30-HpDHQS
-, P56081
into the pET23a+ vector for expression in Escherichia coli BL21DE3 cells
-
overexpressed in Escherichia coli Rosetta DE3. The enzyme is insoluble when expressed in Escherichia coli but is partially solubilised when KCl is included in the cell lysis buffer
Q8U0A8
expression in Escherichia coli BL21
P83703
The aroB gene cloned from Xoo and the corresponding DHQS protein is subsequently overexpressed in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
drug development
-, P56081
potential target for new antimicrobial agents, anti-parasitic agents and herbicides
medicine
-
the enzymes of the shikimate pathway are attractive drug targets for the treatment of tuberculosis
drug development
-
potential antibiotic target