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Information on EC 4.2.3.4 - 3-dehydroquinate synthase and Organism(s) Helicobacter pylori and UniProt Accession P56081

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.3 Acting on phosphates
                4.2.3.4 3-dehydroquinate synthase
IUBMB Comments
Requires Co2+ and bound NAD+. The hydrogen atoms on C-7 of the substrate are retained on C-2 of the product.
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This record set is specific for:
Helicobacter pylori
UNIPROT: P56081
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Word Map
The taxonomic range for the selected organisms is: Helicobacter pylori
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
3-dehydroquinate synthase, 5-dehydroquinate synthase, 3-dehydroquinate synthetase, hpdhqs, dehydroquinate synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dehydroquinate synthase
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3-dehydroquinate synthetase
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-
-
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3-dehydroquinic acid synthetase
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-
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5-dehydroquinate synthase
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-
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5-dehydroquinic acid synthetase
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dehydroquinate synthase
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-
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dehydroquinate synthetase
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-
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synthase, 5-dehydroquinate
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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.
CAS REGISTRY NUMBER
COMMENTARY hide
37211-77-1
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-deoxy-D-arabino-heptulosonate 7-phosphate
3-dehydroquinate + phosphate
show the reaction diagram
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
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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
3-deoxy-D-arabino-heptulosonate 7-phosphate
3-dehydroquinate + phosphate
show the reaction diagram
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
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000008
CBP
contains 5 functional groups (OH, COOH and phosphate)
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.061
HTS 11955
Helicobacter pylori
in 100 mM DMSO, compound carries N or O atoms and functional groups (CN, NH2 and NO2)
0.0845
RH 00573
Helicobacter pylori
in 100 mM DMSO, compound carries N or O atoms and functional groups (CN, NH2 and NO2)
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Uniprot
Manually annotated by BRENDA team
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
obtained in a solution containing 20 mM NAD+
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed HpDHQS protein is purified by immobilized nickel-ion chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
expression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
potential target for new antimicrobial agents, anti-parasitic agents and herbicides
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bereswill, S; Fassbinder, F.; Voelzing, C.; Haas, R.; Reuter, K.; Ficner, R.; Kist, M.
Cloning and functional characterization of the genes encoding 3-dehydroquinate synthase (aroB) and tRNA-guanine transglycosylase (tgt) from Helicobacter pylori
Med. Microbiol. Immunol.
186
125-134
1997
Helicobacter pylori
Manually annotated by BRENDA team
Liu, J.S.; Cheng, W.C.; Wang, H.J.; Chen, Y.C.; Wang, W.C.
Structure-based inhibitor discovery of Helicobacter pylori dehydroquinate synthase
Biochem. Biophys. Res. Commun.
373
1-7
2008
Helicobacter pylori (P56081), Helicobacter pylori
Manually annotated by BRENDA team