Information on EC 4.2.1.10 - 3-dehydroquinate dehydratase

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

EC NUMBER
COMMENTARY
4.2.1.10
-
RECOMMENDED NAME
GeneOntology No.
3-dehydroquinate dehydratase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
3-dehydroquinate = 3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
3-dehydroquinate = 3-dehydroshikimate + H2O
show the reaction diagram
the first step of the reaction involves the formation of an imine intermediate between the oxo group of the 3-dehydroquinate and the enzyme
-
3-dehydroquinate = 3-dehydroshikimate + H2O
show the reaction diagram
type II dehydroquinase catalyzes a trans-dehydration via an enolate intermediate
-
3-dehydroquinate = 3-dehydroshikimate + H2O
show the reaction diagram
type II dehydroquinase catalyzes a trans-dehydration via an enolate intermediate
P0A4Z6
3-dehydroquinate = 3-dehydroshikimate + H2O
show the reaction diagram
type I dehydroquinase catalyzes cis-dehydration of 3-dehydroquinate via a covalent imine intermediate
-
3-dehydroquinate = 3-dehydroshikimate + H2O
show the reaction diagram
type II dehydroquinase catalyzes a trans-dehydration via an enolate intermediate
-
3-dehydroquinate = 3-dehydroshikimate + H2O
show the reaction diagram
type I and type II DHQases are quite distinct from one another in terms of amino acid sequences and three-dimensional structures. Type I enzymes involve a syn elimination and catalyse the biosynthetic reaction. By contrast type II enzymes, which can catalyse either the biosynthetic or catabolic reactions, involve and anti elimination reaction
-
3-dehydroquinate = 3-dehydroshikimate + H2O
show the reaction diagram
type I and type II DHQases have different biochemical and biophysical properties, and no sequence similarity exists between them
-
3-dehydroquinate = 3-dehydroshikimate + H2O
show the reaction diagram
mechanism
-
3-dehydroquinate = 3-dehydroshikimate + H2O
show the reaction diagram
DHQ2 catalyzes the reversible dehydration of 3-dehydroquinic acid to form 3-dehydroshikimic acid through anti elimination of water, with the loss of the more acidic pro-S hydrogen from C-2 of 3-dehydroquinate. The elimination proceeds by a stepwise E1CB mechanism involving an enol intermediate. In the first step, an essential tyrosine in the active site removes the pro-S hydrogen from C-2 of 1. The final step is the acid-catalyzed elimination of the C-1 hydroxy group, a reaction catalyzed by a histidine, which acts as a proton donor, reaction mechanism, overview
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dehydration
-, O30011
-
dehydration
-
-
dehydration
-
-
dehydration
Gluconobacter oxydans IFO 3244
-
-
-
elimination
-
-
-
-
elimination
-, O30011
-
elimination
-
-
elimination
Gluconobacter oxydans IFO 3244
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
chorismate biosynthesis from 3-dehydroquinate
-
gallate biosynthesis
-
Metabolic pathways
-
Phenylalanine, tyrosine and tryptophan biosynthesis
-
quinate degradation I
-
quinate degradation II
-
SYSTEMATIC NAME
IUBMB Comments
3-dehydroquinate hydro-lyase (3-dehydroshikimate-forming)
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3-dehydroquinase
-
-
-
-
3-dehydroquinate dehydratase
-
-
-
-
3-dehydroquinate dehydratase
O30011
-
3-dehydroquinate dehydratase
-
-
3-dehydroquinate dehydratase
Gluconobacter oxydans IFO 3244
-
;
-
3-dehydroquinate dehydratase /shikimate dehydrogenase isoform 1
Q6PUF9
-
3-dehydroquinate dehydratase /shikimate dehydrogenase isoform 2
Q6PUG0
-
3-dehydroquinate dehydratase/shikimate dehydrogenase
Q6PUF9, Q6PUG0
-
3-dehydroquinate dehydratase/shikimate dehydrogenase
-
-
5-dehydroquinase
-
-
-
-
5-dehydroquinate dehydratase
-
-
-
-
5-dehydroquinate hydro-lyase
-
-
-
-
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase, chloroplast
Q9SQT8
-
dehydratase, 3-dehydroquinate
-
-
-
-
dehydroquinase
-
-
-
-
dehydroquinase
O30011
-
dehydroquinase
-
-
dehydroquinase
Q48255
-
dehydroquinase
-
-
dehydroquinase
P0A4Z6
-
dehydroquinase
-
-
dehydroquinase
P15474
-
dehydroquinate dehydratase
-
-
-
-
dehydroquinate dehydratase
Clostridium difficile
-
-
dehydroquinate dehydratase
P58687
-
dehydroquinate dehydratase
Salmonella enterica LT2
P58687
-
-
dehydroquinate dehydratase-shikimate dehydrogenase
Q9SQT8
-
dehydroquinate synthase
-
-
DHD/SHD
Q6PUF9, Q6PUG0
-
DHQ synthase
-
-
-
-
DHQ-SDH
Q9SQT8
-
DHQ-SDH protein
Q9SQT8
-
DHQ/SDH
-
bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase
DHQ2
Q48255
-
DHQase
-
-
-
-
DHQase
Q48255
-
DHQase I
-
-
DHQase-SORase
Q9SQT8
-
DHQD
Clostridium difficile
-
-
DHQD
Salmonella enterica LT2
P58687
-
-
DQD
Gluconobacter oxydans IFO 3244
-
;
-
mDQD
Gluconobacter oxydans IFO 3244
-
-
-
membrane-bound 3-dehydroquinate dehydratase
-
-
NtDHD/SHD-1
Q6PUF9
-
NtDHD/SHD-2
Q6PUG0
cytosolic isoenzyme
pDQD
-
periplasmic 3-dehydroquinate dehydratase
pDQD
Gluconobacter oxydans IFO 3244
-
periplasmic 3-dehydroquinate dehydratase
-
sDQD
-
soluble, cytoplasmic 3-dehydroquinate dehydratase
sDQD
Gluconobacter oxydans IFO 3244
-
soluble, cytoplasmic 3-dehydroquinate dehydratase
-
Type I dehydroquinase
-
-
-
-
type I dehydroquinate dehydratase
Clostridium difficile
-
-
type I dehydroquinate dehydratase
P58687
-
type I dehydroquinate dehydratase
Salmonella enterica LT2
P58687
-
-
Type I DHQase
-
-
-
-
type I DHQD
Clostridium difficile
-
-
type I DHQD
P58687
-
type I DHQD
Salmonella enterica LT2
P58687
-
-
Type II dehydroquinase
-
-
-
-
Type II dehydroquinase
-
-
Type II dehydroquinase
Q48255
-
Type II DHQase
-
-
-
-
membrane-bound 3-dehydroquinate dehydratase
Gluconobacter oxydans IFO 3244
-
-
-
additional information
Q6PUG0
cf. EC 1.1.1.25
CAS REGISTRY NUMBER
COMMENTARY
9012-66-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
formerly Haemophilus pleuropneumoniae
-
-
Manually annotated by BRENDA team
Bacillus subtilis 168
168
-
-
Manually annotated by BRENDA team
cultivar: Yabukia, Sayamamidor, Hatsumomiji, Boh
-
-
Manually annotated by BRENDA team
Clostridium difficile
-
-
-
Manually annotated by BRENDA team
pentafunctional AROM protein with activities of EC 1.1.1.25, EC 4.2.1.10, 5-dehydroquinate synthetase, 3-enolpyruvylshikimic acid 5-phosphate synthetase and shikimic acid kinase
-
-
Manually annotated by BRENDA team
strain WA53
-
-
Manually annotated by BRENDA team
type II dehydroquinase
-
-
Manually annotated by BRENDA team
Emericella nidulans WA53
strain WA53
-
-
Manually annotated by BRENDA team
mutant strain 170-27
-
-
Manually annotated by BRENDA team
strain AB2848/pKS201
-
-
Manually annotated by BRENDA team
type I dehydroquinase
-
-
Manually annotated by BRENDA team
Escherichia coli AB2848/pKS201
strain AB2848/pKS201
-
-
Manually annotated by BRENDA team
strain IFO 3244
-
-
Manually annotated by BRENDA team
Gluconobacter oxydans IFO 3244
-
-
-
Manually annotated by BRENDA team
Gluconobacter oxydans IFO 3244
strain IFO 3244
-
-
Manually annotated by BRENDA team
Hansenula henricii
-
-
-
Manually annotated by BRENDA team
dehydroquinase type II
-
-
Manually annotated by BRENDA team
dehydroquinase type II
-
-
Manually annotated by BRENDA team
dehydroquinase type II
UniProt
Manually annotated by BRENDA team
gene Rv2537c or aroD
UniProt
Manually annotated by BRENDA team
2 isoenzymes: the catabolic dehydroquinase is produced by the qa-2 gene and the biosynthetic dehydroquinase is produced by the constitutive aro cluster
-
-
Manually annotated by BRENDA team
type II dehydroquinase
-
-
Manually annotated by BRENDA team
wild type strain 74A, multienzyme complex with the activities of ec 1.1.1.25, ec 4.2.1.10, 5-dehydroquinate synthetase, 3-enolpyruvylshikimic acid 5-phosphate synthetase and shikimic acid kinase
-
-
Manually annotated by BRENDA team
cv. Samsun NN
Q6PUF9
SwissProt
Manually annotated by BRENDA team
cv. Samsun NN; DHD/SHD-2; cytosolic isozyme
SwissProt
Manually annotated by BRENDA team
no activity in Homo sapiens
-
-
-
Manually annotated by BRENDA team
bifunctional enzyme with activities of ec 1.1.1.25 and ec 4.2.1.10
-
-
Manually annotated by BRENDA team
bifunctional enzyme ec 4.2.1.10/ec 1.1.1.25
-
-
Manually annotated by BRENDA team
Saccharomycopsis lipolytica
-
-
-
Manually annotated by BRENDA team
Salmonella enterica LT2
-
UniProt
Manually annotated by BRENDA team
bifunctional enzyme ec 4.2.1.10/ec 1.1.1.25
-
-
Manually annotated by BRENDA team
dehydroquinase type II
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
evolution
-
There are two distinct dehydroquinases, designated as type I DHQ1, and type II DHQ2, which have different biochemical and biophysical properties and exhibit little sequence similarity. Both subtypes catalyze the same overall reaction through independent mechanisms and with opposite stereochemistry. Type I DHQ occurs in Escherichia coli and Salmonella typhimurium, type II DHQ in Mycobacterium tuberculosis, Streptomyces coelicolor and Helicobacter pylori
metabolism
P0A4Z6
the enzyme is the third enzyme of the shikimate pathway, which is essential in Mycobacterium tuberculosis
metabolism
-
dehydroquinase is the third enzyme in the shikimic acid pathway and catalyzes the reversible dehydration of 3-dehydroquinic acid to form 3-dehydroshikimic acid
metabolism
-
dehydroquinase catalyzes the third step in the shikimate pathway, the reversible dehydration of 3-dehydroquinate to 3-dehydroshikimate
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
-
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
-
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
-
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
P0A4Z6
-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
r
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
-
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
r
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
-
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
r
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
-
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
-
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
Clostridium difficile
-
-
-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
P15474
-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
r
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-, O30011
-
-
-
-
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
r
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
P58687, -
-
-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
Escherichia coli AB2848/pKS201
-
-
-
-
-
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
Emericella nidulans WA53
-
-
-
-
-
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
Salmonella enterica LT2
P58687
-
-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
Gluconobacter oxydans IFO 3244
-
-
-
-
?
3-dehydroquinate
?
show the reaction diagram
-
-
-
-
-
3-dehydroquinate
?
show the reaction diagram
-
type II dehydroquinase is involved in the quinate pathway
-
-
-
3-dehydroquinate
?
show the reaction diagram
-
the enzyme is involved in both the catabolism of quinate and the biosynthesis of aromatic amino acids
-
-
-
3-dehydroquinate
?
show the reaction diagram
-
type I dehydroquinase is involved in the biosynthetic shikimate pathway
-
-
-
3-dehydroquinate
?
show the reaction diagram
-
enzyme of the shikimate pathway
-
-
-
3-dehydroquinate
?
show the reaction diagram
-
the enzyme catalyzes the third of the seven step shikimate pathway
-
-
-
3-dehydroquinate
?
show the reaction diagram
-
the enzyme is likely to function in the shikimate pathway
-
-
-
3-dehydroquinate
?
show the reaction diagram
Escherichia coli AB2848/pKS201
-
the enzyme catalyzes the third of the seven step shikimate pathway
-
-
-
3-dehydroquinate
3-dehydroshikimate
show the reaction diagram
-
-
-
-
?
3-deoxy-D-arabino-heptulosonate 7-phosphate
3-dehydroquinate + phosphate
show the reaction diagram
-
-
-
-
?
5-dehydroquinate
dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
-
5-dehydroquinate
dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
5-dehydroquinate
dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
-
5-dehydroquinate
dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
-
5-dehydroquinate
dehydroshikimate + H2O
show the reaction diagram
-
-
5-dehydroshikimate
-
5-dehydroquinate
?
show the reaction diagram
-
-
-
-
-
5-dehydroquinate
?
show the reaction diagram
-
enzyme is involved in the biosynthesis of aromatic amino acids
-
-
-
5-dehydroquinate
?
show the reaction diagram
-
enzyme catalyzes the third step in the biosynthesis of chorismate
-
-
-
5-dehydroquinate
?
show the reaction diagram
-
2 isoenzymes: the catabolic dehydroquinase is produced by the qa-2 gene and the biosynthetic dehydroquinase is produced by the constitutive aro cluster
-
-
-
dehydroquinate
dehydroshikimate + H2O
show the reaction diagram
-, Q6PUF9, Q6PUG0
-
-
-
r
additional information
?
-
P15474
role in shikimate pathway
-
?
additional information
?
-
-
role in shikimate pathway for the biosynthesis of aromatic compounds
-
?
additional information
?
-
-, Q6PUF9, Q6PUG0
the enzyme also shows shikimate dehydrogenase activity, EC 1.1.1.25
-
-
-
additional information
?
-
P0A4Z6
active-site binding of 3-dehydroshikimate, catalytic loop in the MtDHQase-1 structure, comparison with the incomplete structure of apo-MtDHQase, PDB code 2DHQ, overview
-
-
-
additional information
?
-
P58687, -
functionality of a surface loop that closes over the active site following substrate binding, both direct and indirect mechanisms of involvement of the loop in substrate binding exist, overview. To establish a direct interaction with the substrate, closure of the loop necessitates a conformational change of a key active site arginine, which in turn positions the substrate productively. Loop closure induces a conformational change in Arg213. Specifically the side chain of Gln236, may be critical for inducing the change in the conformation of Arg213
-
-
-
additional information
?
-
Clostridium difficile, Salmonella enterica
-
the intermediate state structures reveal a reaction state-dependent behavior of His143 in which the residue adopts a conformation proximal to the site of catalytic dehydration only when the leaving group is present. His143 is likely to assume differing catalytic roles in each of its observed conformations. One conformation of His143 positions the residue for the formation/hydrolysis of the covalent Schiff base intermediates, whereas the other conformation positions the residue for a role in the catalytic dehydration event, role of His143 in type I DHQD-catalyzed reaction, reaction mechanism, overview
-
-
-
additional information
?
-
Salmonella enterica LT2
P58687
the intermediate state structures reveal a reaction state-dependent behavior of His143 in which the residue adopts a conformation proximal to the site of catalytic dehydration only when the leaving group is present. His143 is likely to assume differing catalytic roles in each of its observed conformations. One conformation of His143 positions the residue for the formation/hydrolysis of the covalent Schiff base intermediates, whereas the other conformation positions the residue for a role in the catalytic dehydration event, role of His143 in type I DHQD-catalyzed reaction, reaction mechanism, overview
-
-
-
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-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
r
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
r
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
r
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
Clostridium difficile
-
-
-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
r
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-, O30011
-
-
-
-
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
r
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
P58687, -
-
-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
-
-
-
-
?
3-dehydroquinate
?
show the reaction diagram
-
-
-
-
-
3-dehydroquinate
?
show the reaction diagram
-
type II dehydroquinase is involved in the quinate pathway
-
-
-
3-dehydroquinate
?
show the reaction diagram
-
the enzyme is involved in both the catabolism of quinate and the biosynthesis of aromatic amino acids
-
-
-
3-dehydroquinate
?
show the reaction diagram
-
type I dehydroquinase is involved in the biosynthetic shikimate pathway
-
-
-
3-dehydroquinate
?
show the reaction diagram
-
enzyme of the shikimate pathway
-
-
-
3-dehydroquinate
?
show the reaction diagram
-
the enzyme catalyzes the third of the seven step shikimate pathway
-
-
-
3-dehydroquinate
?
show the reaction diagram
-
the enzyme is likely to function in the shikimate pathway
-
-
-
3-dehydroquinate
?
show the reaction diagram
Escherichia coli AB2848/pKS201
-
the enzyme catalyzes the third of the seven step shikimate pathway
-
-
-
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
Salmonella enterica LT2
P58687
-
-
-
?
3-dehydroquinate
3-dehydroshikimate + H2O
show the reaction diagram
Gluconobacter oxydans IFO 3244
-
-
-
-
?
3-deoxy-D-arabino-heptulosonate 7-phosphate
3-dehydroquinate + phosphate
show the reaction diagram
-
-
-
-
?
5-dehydroquinate
?
show the reaction diagram
-
-
-
-
-
5-dehydroquinate
?
show the reaction diagram
-
enzyme is involved in the biosynthesis of aromatic amino acids
-
-
-
5-dehydroquinate
?
show the reaction diagram
-
enzyme catalyzes the third step in the biosynthesis of chorismate
-
-
-
5-dehydroquinate
?
show the reaction diagram
-
2 isoenzymes: the catabolic dehydroquinase is produced by the qa-2 gene and the biosynthetic dehydroquinase is produced by the constitutive aro cluster
-
-
-
dehydroquinate
dehydroshikimate + H2O
show the reaction diagram
-, Q6PUF9, Q6PUG0
-
-
-
r
additional information
?
-
P15474
role in shikimate pathway
-
?
additional information
?
-
-
role in shikimate pathway for the biosynthesis of aromatic compounds
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NAD+
-, Q6PUF9, Q6PUG0
-
NADH
-, Q6PUF9, Q6PUG0
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
KCl
-
facilitates mDQD enzyme purification/solubilization by detergents n-dodecyl-beta-D-maltoside and n-octyl-beta-D-glucoside as a chaotropic agent
Mg2+
-
required
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(1R,2R,4S,5R)-1,4,5-trihydroxy-2-(4-methoxybenzyl)-3-oxocyclohexanecarboxylic acid
-
-
(1R,2R,4S,5R)-1,4,5-trihydroxy-2-(4-methylbenzyl)-3-oxocyclohexanecarboxylic acid
-
-
(1R,2R,4S,5R)-1,4,5-trihydroxy-3-oxo-2-(prop-2-en-1-yl)cyclohexanecarboxylic acid
-
-
(1R,2R,4S,5R)-1,4,5-trihydroxy-3-oxo-2-propylcyclohexanecarboxylic acid
-
-
(1R,2R,4S,5R)-2-(1-benzothiophen-5-yl)-1,4,5-trihydroxy-3-oxocyclohexanecarboxylic acid
-
-
(1R,2R,4S,5R)-2-benzyl-1,4,5-trihydroxy-3-oxocyclohexanecarboxylic acid
-
-
(1R,2R,4S,5R)-2-[difluoro(pentafluorophenyl)methyl]-1,4,5-trihydroxy-3-oxocyclohexanecarboxylic acid
-
-
(1R,2S,4S,5R)-1,4,5-trihydroxy-2-(4-methoxybenzyl)-3-oxocyclohexanecarboxylic acid
-
-
(1R,2S,4S,5R)-1,4,5-trihydroxy-2-(4-methylbenzyl)-3-oxocyclohexanecarboxylic acid
-
-
(1R,2S,4S,5R)-1,4,5-trihydroxy-3-oxo-2-(prop-2-en-1-yl)cyclohexanecarboxylic acid
-
-
(1R,2S,4S,5R)-2-(1-benzothiophen-5-yl)-1,4,5-trihydroxy-3-oxocyclohexanecarboxylic acid
-
-
(1R,2S,4S,5R)-2-benzyl-1,4,5-trihydroxy-3-oxocyclohexanecarboxylic acid
-
-
(1R,2S,4S,5R)-2-[difluoro(pentafluorophenyl)methyl]-1,4,5-trihydroxy-3-oxocyclohexanecarboxylic acid
-
-
(1R,3R,4R)-1,3,4-trihydroxy-5-(3,5-difluoro)phenylcyclohex-5-en-1-carboxylic acid
-
-
(1R,3R,4R)-1,3,4-trihydroxy-5-(3-carboxylic)phenylcyclohex-5-en-1-carboxylic acid
-
-
(1R,3R,4R)-1,3,4-trihydroxy-5-(3-fluoro)phenylcyclo-hex-5-en-1-carboxylic acid
-
-
(1R,3R,4R)-1,3,4-trihydroxy-5-(3-hydroxy)phenylcyclohex-5-en-1-carboxylic acid
-
-
(1R,3R,4R)-1,3,4-trihydroxy-5-(3-nitro)phenylcyclohex-5-en-1-carboxylic acid
-
-
(1R,3R,4R)-1,3,4-trihydroxy-5-(3-trifluoromethyl)phenylcyclohex-5-en-1-carboxylic acid
-
-
(1R,3R,4R)-1,3,4-trihydroxy-5-(4-fluoro)phenylcyclo-hex-5-en-1-carboxylic acid
-
-
(1R,3R,4R)-1,3,4-trihydroxy-5-(4-trifluoromethyl)phenylcyclohex-5-en-1-carboxylic acid
-
-
(1R,3R,4R)-1,3,4-trihydroxy-5-(furan-3-yl)phenylcyclohex-5-en-1-carboxylic acid
-
-
(1R,3R,4R)-1,3,4-trihydroxy-5-(pyridine-3-yl)cyclohex-5-en-1-carboxylic acid
-
-
(1R,3R,4R)-1,3,4-trihydroxy-5-(thiophen-3-yl)phenyl-cyclohex-5-en-1-carboxylic acid
-
-
(1R,3R,4R)-1,3,4-trihydroxy-5-phenylcyclohex-5-en-1-carboxylic acid
-
-
(1R,4R,5R)-1,4,5-trihydroxy-2-cyclohexene-1-carboxylic acid
-
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(1-phenyl-1H-1,2,3-triazol-4-yl)cyclohex-2-ene-1-carboxylic acid
-
competitive inhibitor
(1R,4R,5R)-1,4,5-trihydroxy-3-(1H-1,2,3-triazol-4-yl)cyclohex-2-en-1-carboxylic acid
-
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(2-nitrophenyl)cyclohex-2-ene-1-carboxylic acid
-
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(2-nitrothien-3-yl)cyclohex-2-en-1-carboxylic acid
-
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(3-bromothien-2-yl)cyclohex-2-en-1-carboxylic acid
-
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(3-hydroxyphenyl)cyclohex-2-ene-1-carboxylic acid
-
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(3-nitrophenyl)cyclohex-2-ene-1-carboxylic acid
-
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(3-nitrophenyl)cyclohex-2-ene-1-carboxylic acid
-
a competitive inhibitor
(1R,4R,5R)-1,4,5-trihydroxy-3-(3-nitrothien-2-yl)cyclohex-2-en-1-carboxylic acid
-
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(3-phenoxyphenyl)cyclohex-2-ene-1-carboxylic acid
-
competitive inhibitor
(1R,4R,5R)-1,4,5-trihydroxy-3-(3-phenoxyphenyl)cyclohex-2-ene-1-carboxylic acid
-
a competitive inhibitor
(1R,4R,5R)-1,4,5-trihydroxy-3-(4-nitrophenyl)cyclohex-2-ene-1-carboxylic acid
-
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(phenylethynyl)cyclohex-2-ene-1-carboxylic acid
-
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(pyridin-3-ylethynyl)cyclohex-2-ene-1-carboxylic acid
-
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(quinolin-3-ylethynyl)cyclohex-2-ene-1-carboxylic acid
-
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(thien-2-yl)cyclohex-2-en-1-carboxylic acid
-
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(thiophen-2-yl)cyclohex-2-ene-1-carboxylic acid
-
competitive inhibitor
(1R,4R,5R)-1,4,5-trihydroxy-3-(thiophen-2-yl)cyclohex-2-ene-1-carboxylic acid
-
a competitive inhibitor
(1R,4R,5R)-1,4,5-trihydroxy-3-(thiophen-2-ylethynyl)cyclohex-2-ene-1-carboxylic acid
-
-
(1R,4R,5R)-1,4,5-trihydroxy-3-naphthalen-2-ylcyclohex-2-ene-1-carboxylic acid
-
-
(1R,4R,5R)-1,4,5-trihydroxy-3-phenylcyclohex-2-ene-1-carboxylic acid
-
-
(1R,4R,5R)-1,4,5-trihydroxy-3-pyridin-3-ylcyclohex-2-ene-1-carboxylic acid
-
-
(1R,4R,5R)-1,4,5-trihydroxy-3-thiophen-3-ylcyclohex-2-ene-1-carboxylic acid
-
-
(1R,4R,5R)-1,4,5-trihydroxy-3-[(1E)-3-phenoxyprop-1-en-1-yl]cyclohex-2-ene-1-carboxylic acid
-
a competitive inhibitor
(1R,4R,5R)-1,4,5-trihydroxy-3-[(3-nitrophenyl)ethynyl]cyclohex-2-ene-1-carboxylic acid
-
-
(1R,4R,5R)-1,4,5-trihydroxy-3-[1-(2-hydroxyphenyl)-1H-1,2,3-triazol-4-yl]cyclohex-2-ene-1-carboxylic acid
-
competitive inhibitor
(1R,4R,5R)-1,4,5-trihydroxy-3-[1-(3-nitrophenyl)-1H-1,2,3-triazol-4-yl]cyclohex-2-ene-1-carboxylic acid
-
competitive inhibitor
(1R,4R,5R)-1,4,5-trihydroxy-3-[1-(pyridin-3-yl)-1H-1,2,3-triazol-4-yl]cyclohex-2-ene-1-carboxylic acid
-
competitive inhibitor
(1R,4R,5R)-1,4,5-trihydroxy-3-[1-(thiophen-2-ylmethyl)-1H-1,2,3-triazol-4-yl]cyclohex-2-ene-1-carboxylic acid
-
competitive inhibitor
(1R,4R,5R)-1,4,5-trihydroxy-3-[3-(phenylsulfanyl)phenyl]cyclohex-2-ene-1-carboxylic acid
-
a competitive inhibitor
(1R,4R,5R)-1,4,5-trihydroxy-3-[3-(trifluoromethyl)phenyl]cyclohex-2-ene-1-carboxylic acid
-
-
(1R,4R,5R)-1,4,5-trihydroxy-3-[3-phenoxy-prop-(E)-enyl]-cyclohex-2-enecarboxylic acid
P0A4Z6
-
-
(1R,4R,5R)-1,4,5-trihydroxy-3-[4-(trifluoromethyl)phenyl]cyclohex-2-ene-1-carboxylic acid
-
-
(1R,4R,5R)-1,4,5-trihydroxy-3-[[3-(trifluoromethyl)phenyl]ethynyl]cyclohex-2-ene-1-carboxylic acid
-
-
(1R,4R,5R)-3-(1,3-benzothiazol-2-ylethynyl)-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
-
-
(1R,4R,5R)-3-(1-benzofuran-5-yl)-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
-
-
(1R,4R,5R)-3-(1-benzofuran-6-yl)-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
-
-
(1R,4R,5R)-3-(1-benzothiophen-5-yl)-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
-
-
(1R,4R,5R)-3-(1-benzothiophen-6-yl)-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
-
-
(1R,4R,5R)-3-(2-carboxy-vinyl)-1,4,5-trihydroxy-cyclohex-2-enecarboxylic acid
-
-
(1R,4R,5R)-3-(3,5-difluorophenyl)-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
-
-
(1R,4R,5R)-3-(3-carbonitrilethien-2-yl)-1,4,5-trihydroxycyclohex-2-en-1-carboxylic acid
-
-
(1R,4R,5R)-3-(3-fluorophenyl)-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
-
-
(1R,4R,5R)-3-(4-fluorophenyl)-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
-
-
(1R,4R,5R)-3-(furan-2-yl)-1,4,5-trihydroxycyclohex-2-en-1-carboxylic acid
-
-
(1R,4R,5R)-3-(tert-butylcarbamoyl)-1,4,5-trihydroxycyclohex-2-enecarboxylic acid
-
-
(1R,4R,5R)-3-(tert-butylcarbamoyl)-1,4,5-trihydroxycyclohex-2-enecarboxylic acid
-
-
(1R,4R,5R)-3-furan-3-yl-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
-
-
(1R,4R,5R)-3-[(4-fluorophenyl)ethynyl]-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
-
-
(1R,4R,5R)-3-[1-(4-fluorophenyl)-1H-1,2,3-triazol-4-yl]-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
-
competitive inhibitor
(1R,4R,5R)-3-[1-(furan-2-ylmethyl)-1H-1,2,3-triazol-4-yl]-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
-
competitive inhibitor
(1R,4S,5R)-1,3,4,5-tetrahydroxycyclohex-2-ene-1-carboxylate
-
-
(1R,4S,5R)-1,4,5-trihydroxy-3-[(1E)-3-phenoxyprop-1-en-1-yl]cyclohex-2-ene-1-carboxylic acid
P0A4Z6
-
(1R,4S,5R)-3,3-difluoro-1,4,5-trihydroxycyclohexane-1-carboxylic acid
-
inhibitor is selective for the type II dehydroquinase over the type I dehydroquinase
(1R,4S,5R)-3,3-difluoro-1,4,5-trihydroxycyclohexane-1-carboxylic acid
-
-
(1R,4S,5R)-3,3-difluoro-1,4,5-trihydroxycyclohexane-1-carboxylic acid
-
inhibitor is selective for the type II dehydroquinase over the type I dehydroquinase
(1R,4S,5R)-3-(1-benzothiophen-2-ylmethoxy)-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
-
a competitive inhibitor
(1R,4S,5R)-3-fluoro-1,4,5-trihydroxy-2-cyclohexene-1-carboxylic acid
-
inhibitor is selective for the type II dehydroquinase over the type I dehydroquinase
(1R,4S,5R)-3-fluoro-1,4,5-trihydroxy-2-cyclohexene-1-carboxylic acid
-
-
(1R,4S,5R)-3-fluoro-1,4,5-trihydroxy-2-cyclohexene-1-carboxylic acid
-
inhibitor is selective for the type II dehydroquinase over the type I dehydroquinase
(1S,3R,4R)-1,3,4-trihydroxy-5-cyclohexene-1-carboxylic acid
-
-
-
(1S,3R,4R)-1,3,4-trihydroxy-5-methylenecyclohexanecarboxylic acid
-
-
(1S,3R,4R,5E)-1,3,4-trihydroxy-5-(methylimino)cyclohexanecarboxylic acid
-
-
(1S,4R,5R)-3-(3-benzoylphenyl)-1,4,5-trihydroxycyclohex-2-enecarboxylic acid
P0A4Z6
-
-
(2R)-2-p-methoxybenzyl-3-dehydroquinic acid
-
a reversible, competitive inhibitor of DHQ2
-
(2R)-2-p-methoxybenzyl-3-dehydroquinic acid
-
a reversible, competitive inhibitor of DHQ2, pH not specified in the publication, temperature not specified in the publication
-
(2R)-2-p-methylbenzyl-3-dehydroquinic acid
-
a reversible, competitive inhibitor of DHQ2
-
(2R)-2-p-methylbenzyl-3-dehydroquinic acid
-
a reversible, competitive inhibitor of DHQ2, pH not specified in the publication, temperature not specified in the publication
-
(2R)-2-pentafluoro-benzyl-3-dehydroquinic acid
-
a reversible, competitive inhibitor of DHQ2
-
(2R)-2-pentafluoro-benzyl-3-dehydroquinic acid
-
a reversible, competitive inhibitor of DHQ2, pH not specified in the publication, temperature not specified in the publication
-
(3R,5R,6R)-3,5,6-trihydroxycyclohex-1-ene-1,3-dicarboxylic acid
-
-
(3R,5R,6R)-3,5,6-trihydroxycyclohex-1-ene-1,3-dicarboxylic acid
-
a competitive inhibitor
(3R,5R,6R)-3-carbamoyl-3,5,6-trihydroxycyclohex-1-enecarboxylic acid
-
-
(4R,6R,7S)-2-(1-cyclopropylethyl)-4,6,7-trihydroxy-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
-
(4R,6R,7S)-2-ethenyl-4,6,7-trihydroxy-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
-
(4R,6R,7S)-2-ethyl-4,6,7-trihydroxy-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
-
(4R,6R,7S)-2-[(1E)-2-cyclopropylprop-1-en-1-yl]-4,6,7-trihydroxy-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
-
(4R,6R,7S)-4,6,7-trihydroxy-2-(2-hydroxyethyl)-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
-
(4R,6R,7S)-4,6,7-trihydroxy-2-(prop-2-en-1-yl)-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
-
(4R,6R,7S)-4,6,7-trihydroxy-2-(propan-2-yl)-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
-
(4R,6R,7S)-4,6,7-trihydroxy-2-methyl-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
-
(4R,6R,7S)-4,6,7-trihydroxy-2-[(1Z)-prop-1-en-1-yl]-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
-
(4R,6R,7S)-4,6,7-trihydroxy-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
-
1,3,4-trihydroxy-5-hydroxyiminocyclohexanecarboxylic acid
-
-
1,3,4-trihydroxy-5-hydroxyiminocyclohexanecarboxylic acid
-
poor inhibition
1,3,4-trihydroxy-5-hydroxyiminocyclohexanecarboxylic acid
-
-
1,3,4-trihydroxy-5-oxocyclohexanecarboxylic acid
-
-
1,3,4-trihydroxy-5-oxocyclohexanecarboxylic acid
-
poor inhibition
1,3,4-trihydroxy-5-oxocyclohexanecarboxylic acid
-
-
1,3,4-trihydroxycyclohexanecarboxylic acid
-
-
1,3,4-trihydroxycyclohexanecarboxylic acid
-
poor inhibition
1,3,4-trihydroxycyclohexanecarboxylic acid
-
-
1,4,5-trihydroxycyclohex-2-enecarboxylic acid
-
-
1,4,5-trihydroxycyclohex-2-enecarboxylic acid
-
poor inhibition
1,4,5-trihydroxycyclohex-2-enecarboxylic acid
-
-
2,3-anhydroquinate
-
-
2,3-anhydroquinate
P0A4Z6
mimics the flattened enol/enolate reaction intermediate and serves as an anchor molecule for four of the inhibitors investigated, overview. Structure of MtDHQase in complex with a 2,3-anhydroquinate moiety attached to a biaryl group shows that this group extends to an active-site subpocket inducing significant structural rearrangement
2,3-anhydroquinic acid
-
poor inhibition
2,3-anhydroquinic acid
-
-
3-deoxyquinic acid
-
poor inhibition
3-deoxyquinic acid
-
-
3-[(3R,5R,6R)-3-carboxy-3,5,6-trihydroxycyclohex-1-en-1-yl]benzoic acid
-
-
3-[4-[(3R,5R,6R)-3-carboxy-3,5,6-trihydroxycyclohex-1-en-1-yl]-1H-1,2,3-triazol-1-yl]benzoic acid
-
competitive inhibitor
4-hydroxy-2-hydroxymethyl-4-methyl-pent-2-enedioic acid
-
-
benzo[b]thiophen-5-yl-3-dehydroquinic acid
-
a reversible, competitive inhibitor of DHQ2
-
benzo[b]thiophen-5-yl-3-dehydroquinic acid
-
a reversible, competitive inhibitor of DHQ2, pH not specified in the publication, temperature not specified in the publication
-
carbaphosphonate
-
-
citrazinic acid
P0A4Z6
a planar analogue of the reaction product, complex structure, overview
-
Cl-
-
no significant effect
Cu2+
-
partial
D-(+)-tartrate
-
-
Fe2+
-
partial
-
guanidine hydrochloride
-
55 C, irreversible inactivation
hydroxylamine
-
partial
N-tetrazol-5-yl-9-oxo-9H-xanthene-2-sulfonamide
-
-
NaBH4
-
irreversible inactivation in presence of 3-dehydroquinate
NaBH4
-
irreversible inactivation in presence of 3-dehydroquinate
SDS
-
55 C, irreversible inactivation
sodium (1R,4S,5R)-1,4,5-trihydroxy-3-(5-methylbenzo[b]-thiophen-2-yl)methoxycyclohex-2-en-1-carboxylate
-
-
sodium (1R,4S,5R)-1,4,5-trihydroxy-3-(benzo[b]thiophen-2-yl)methoxycyclohex-2-en-1-carboxylate
-
-
sodium (1R,4S,5R)-1,4,5-trihydroxy-3-(thien-2-yl)methoxycyclohex-2-en-1-carboxylate
-
-
sodium (1R,4S,5R)-1,4,5-trihydroxy-3-[(benzo[b]thiophen-5-yl)methoxy]cyclohex-2-en-1-carboxylate
-
-
Zn2+
-
partial
iodoacetamide
-
partial
additional information
-
Ki-values for (1S,3R,4R,5E)-1,3,4-trihydroxy-5-(methylimino)cyclohexanecarboxylic acid and (1S,3R,4R)-1,3,4-trihydroxy-5-methylenecyclohexanecarboxylic acid are above 25 mM
-
additional information
-
the in silico design, synthesis, and biological evaluation of ten potent type II dehydroquinase inhibitors are described. These compounds contain an anhydroquinate core, incorporated as a mimic of the enolate reaction intermediate. This substructure is attached by a variety of linking units to a terminal phenyl group that binds in an adjacent pocket. Inhibitors are synthesised from (-)-quinic acid using palladium-catalysed Stille and carboamidation chemistry. Several inhibitors exhibited nanomolar inhibition constants
-
additional information
-
nanomolar competitive inhibitors
-
additional information
-, Q6PUF9, Q6PUG0
RNA interference of NtDHD/SHD-1 strongly inhibits DHD/SHD activity in transgenic tobacco plants
-
additional information
P0A4Z6
active-site binding of inhibitors, structure, overview
-
additional information
-
binding mechanism of (2R)-2-benzyl-3-dehydroquinic acids, molecular dynamics simulations, overview
-
additional information
-
development of a range of ene-yne-based inhibitors, active site docking study using enzyme structure PDB ID 2WKS, overview
-
additional information
-
development of a range of ene-yne-based inhibitors, overview
-
additional information
-
development of a range of ene-yne-based inhibitors, active site docking study using enzyme structure PDB ID 1GU1, overview
-
additional information
-
inhibitor design and synthesis, binding structure and inhibition mechanism, overview
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.015
-
3-dehydroquinate
-
-
0.015
-
3-dehydroquinate
-
at pH 7.0, 25C
0.018
-
3-dehydroquinate
-
-
0.021
-
3-dehydroquinate
-
wild-type enzyme, pH 7.5, 37C
0.024
-
3-dehydroquinate
-
pH 7, 25C
0.033
-
3-dehydroquinate
-
mutant K170M, pH 7.5, 37C
0.036
-
3-dehydroquinate
-
pH 7.5, 25C
0.036
-
3-dehydroquinate
Clostridium difficile
-
wild-type enzyme, pH 7.5, 37C
0.037
-
3-dehydroquinate
-
-
0.04
-
3-dehydroquinate
-
apparent Km, pDQD
0.05
-
3-dehydroquinate
-
apparent Km, sDQD
0.052
-
3-dehydroquinate
-
pH 7.5, 25C
0.075
-
3-dehydroquinate
-
pH 7.5, 25C
0.0769
-
3-dehydroquinate
-
pH 7.5, 25C
0.1
-
3-dehydroquinate
-
pH 7, 25C
0.121
-
3-dehydroquinate
-
-
0.15
-
3-dehydroquinate
-
-
0.21
-
3-dehydroquinate
-
pH 7.5, 25C
0.228
-
3-dehydroquinate
-
pH 7.5, 25C
0.44
-
3-dehydroquinate
-
-
0.48
-
3-dehydroquinate
-
at pH 7.0, 25C
0.59
-
3-dehydroquinate
-
-
0.6
-
3-dehydroquinate
-
-
0.064
-
Dehydroquinate
-
-
0.15
-
Dehydroquinate
-
-
0.65
-
Dehydroquinate
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.015
-
3-dehydroquinate
-
mutant K170M, pH 7.5, 37C
0.06
-
3-dehydroquinate
-
at pH 7.0, 25C
0.15
-
3-dehydroquinate
-
at pH 7.0, 25C
0.34
-
3-dehydroquinate
-
pH 7.5, 25C
1.4
-
3-dehydroquinate
-
pH 7.5, 25C
2
-
3-dehydroquinate
-
-
4.6
-
3-dehydroquinate
-
pH 7.5, 25C
5.2
-
3-dehydroquinate
-
pH 7, 25C
6.3
-
3-dehydroquinate
-
pH 7.5, 25C
6.9
-
3-dehydroquinate
-
pH 8.3, temperature not specified in the publication, mutant Q236A
61
-
3-dehydroquinate
-
pH 7.5, 25C
84
-
3-dehydroquinate
-
pH 7.5, 25C
107
-
3-dehydroquinate
-
pH 8.3, temperature not specified in the publication, mutant S232A
124
-
3-dehydroquinate
-
pH 7, 25C
125
-
3-dehydroquinate
Clostridium difficile
-
wild-type enzyme, pH 7.5, 37C
210
-
3-dehydroquinate
-
pH 8.3, temperature not specified in the publication, wild-type enzyme
210
-
3-dehydroquinate
-
wild-type enzyme, pH 7.5, 37C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00000045
-
3-dehydroquinate
-
mutant K170M, pH 7.5, 37C
3631
0.001
-
3-dehydroquinate
-
wild-type enzyme, pH 7.5, 37C
3631
0.0035
-
3-dehydroquinate
Clostridium difficile
-
wild-type enzyme, pH 7.5, 37C
3631
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.000026
-
(1R,2R,4S,5R)-1,4,5-trihydroxy-2-(4-methoxybenzyl)-3-oxocyclohexanecarboxylic acid
-
pH 7.0, 25C, 50 mM Tris-HOAc
0.00017
-
(1R,2R,4S,5R)-1,4,5-trihydroxy-2-(4-methoxybenzyl)-3-oxocyclohexanecarboxylic acid
-
pH 7.0, 25C, 50 mM Tris-HCl
0.000089
-
(1R,2R,4S,5R)-1,4,5-trihydroxy-2-(4-methylbenzyl)-3-oxocyclohexanecarboxylic acid
-
pH 7.0, 25C, 50 mM Tris-HOAc
0.00025
-
(1R,2R,4S,5R)-1,4,5-trihydroxy-2-(4-methylbenzyl)-3-oxocyclohexanecarboxylic acid
-
pH 7.0, 25C, 50 mM Tris-HCl
0.00076
-
(1R,2R,4S,5R)-1,4,5-trihydroxy-3-oxo-2-(prop-2-en-1-yl)cyclohexanecarboxylic acid
-
pH 7.0, 25C, 50 mM Tris-HOAc
0.0093
-
(1R,2R,4S,5R)-1,4,5-trihydroxy-3-oxo-2-(prop-2-en-1-yl)cyclohexanecarboxylic acid
-
pH 7.0, 25C, 50 mM Tris-HCl
0.0017
-
(1R,2R,4S,5R)-1,4,5-trihydroxy-3-oxo-2-propylcyclohexanecarboxylic acid
-
pH 7.0, 25C, 50 mM Tris-HOAc
0.02
-
(1R,2R,4S,5R)-1,4,5-trihydroxy-3-oxo-2-propylcyclohexanecarboxylic acid
-
pH 7.0, 25C, 50 mM Tris-HCl
0.000028
-
(1R,2R,4S,5R)-2-(1-benzothiophen-5-yl)-1,4,5-trihydroxy-3-oxocyclohexanecarboxylic acid
-
pH 7.0, 25C, 50 mM Tris-HOAc
0.00016
-
(1R,2R,4S,5R)-2-(1-benzothiophen-5-yl)-1,4,5-trihydroxy-3-oxocyclohexanecarboxylic acid
-
pH 7.0, 25C, 50 mM Tris-HCl
0.0001
-
(1R,2R,4S,5R)-2-benzyl-1,4,5-trihydroxy-3-oxocyclohexanecarboxylic acid
-
pH 7.0, 25C, 50 mM TrisHCl
0.0014
-
(1R,2R,4S,5R)-2-benzyl-1,4,5-trihydroxy-3-oxocyclohexanecarboxylic acid
-
pH 7.0, 25C, 50 mM Tris-HCl
0.000047
-
(1R,2R,4S,5R)-2-[difluoro(pentafluorophenyl)methyl]-1,4,5-trihydroxy-3-oxocyclohexanecarboxylic acid
-
pH 7.0, 25C, 50 mM Tris-HOAc
0.0026
-
(1R,2R,4S,5R)-2-[difluoro(pentafluorophenyl)methyl]-1,4,5-trihydroxy-3-oxocyclohexanecarboxylic acid
-
pH 7.0, 25C, 50 mM Tris-HCl
0.0001
-
(1R,2S,4S,5R)-1,4,5-trihydroxy-2-(4-methoxybenzyl)-3-oxocyclohexanecarboxylic acid
-
pH 7.0, 25C, 50 mM Tris-HOAc
0.00142
-
(1R,2S,4S,5R)-1,4,5-trihydroxy-2-(4-methoxybenzyl)-3-oxocyclohexanecarboxylic acid
-
pH 7.0, 25C, 50 mM Tris-HCl
0.00009
-
(1R,2S,4S,5R)-1,4,5-trihydroxy-2-(4-methylbenzyl)-3-oxocyclohexanecarboxylic acid
-
pH 7.0, 25C, 50 mM Tris-HOAc
0.00097
-
(1R,2S,4S,5R)-1,4,5-trihydroxy-2-(4-methylbenzyl)-3-oxocyclohexanecarboxylic acid
-
pH 7.0, 25C, 50 mM Tris-HCl
0.00185
-
(1R,2S,4S,5R)-1,4,5-trihydroxy-3-oxo-2-(prop-2-en-1-yl)cyclohexanecarboxylic acid
-
pH 7.0, 25C, 50 mM Tris-HOAc
0.0215
-
(1R,2S,4S,5R)-1,4,5-trihydroxy-3-oxo-2-(prop-2-en-1-yl)cyclohexanecarboxylic acid
-
pH 7.0, 25C, 50 mM Tris-HCl
0.000056
-
(1R,2S,4S,5R)-2-(1-benzothiophen-5-yl)-1,4,5-trihydroxy-3-oxocyclohexanecarboxylic acid
-
pH 7.0, 25C, 50 mM Tris-HOAc
0.0009
-
(1R,2S,4S,5R)-2-(1-benzothiophen-5-yl)-1,4,5-trihydroxy-3-oxocyclohexanecarboxylic acid
-
pH 7.0, 25C, 50 mM Tris-HCl
0.00009
-
(1R,2S,4S,5R)-2-benzyl-1,4,5-trihydroxy-3-oxocyclohexanecarboxylic acid
-
pH 7.0, 25C, 50 mM Tris-HOAc
0.00118
-
(1R,2S,4S,5R)-2-benzyl-1,4,5-trihydroxy-3-oxocyclohexanecarboxylic acid
-
pH 7.0, 25C, 50 mM Tris-HCl
0.000074
-
(1R,2S,4S,5R)-2-[difluoro(pentafluorophenyl)methyl]-1,4,5-trihydroxy-3-oxocyclohexanecarboxylic acid
-
pH 7.0, 25C, 50 mM Tris-HOAc
0.00097
-
(1R,2S,4S,5R)-2-[difluoro(pentafluorophenyl)methyl]-1,4,5-trihydroxy-3-oxocyclohexanecarboxylic acid
-
pH 7.0, 25C, 50 mM Tris-HCl
2.44
-
(1R,3R,4R)-1,3,4-trihydroxy-5-(3,5-difluoro)phenylcyclohex-5-en-1-carboxylic acid
-
pH 8.2, 25C
150
-
(1R,3R,4R)-1,3,4-trihydroxy-5-(3-carboxylic)phenylcyclohex-5-en-1-carboxylic acid
-
pH 8.2, 25C
1.5
-
(1R,3R,4R)-1,3,4-trihydroxy-5-(3-fluoro)phenylcyclo-hex-5-en-1-carboxylic acid
-
pH 8.2, 25C
95
-
(1R,3R,4R)-1,3,4-trihydroxy-5-(3-hydroxy)phenylcyclohex-5-en-1-carboxylic acid
-
pH 8.2, 25C
0.054
-
(1R,3R,4R)-1,3,4-trihydroxy-5-(3-nitro)phenylcyclohex-5-en-1-carboxylic acid
-
pH 8.2, 25C
2.125
-
(1R,3R,4R)-1,3,4-trihydroxy-5-(3-trifluoromethyl)phenylcyclohex-5-en-1-carboxylic acid
-
pH 8.2, 25C
1.8
-
(1R,3R,4R)-1,3,4-trihydroxy-5-(4-fluoro)phenylcyclo-hex-5-en-1-carboxylic acid
-
pH 8.2, 25C
17
-
(1R,3R,4R)-1,3,4-trihydroxy-5-(4-trifluoromethyl)phenylcyclohex-5-en-1-carboxylic acid
-
pH 8.2, 25C
0.83
-
(1R,3R,4R)-1,3,4-trihydroxy-5-(furan-3-yl)phenylcyclohex-5-en-1-carboxylic acid
-
pH 8.2, 25C
45
-
(1R,3R,4R)-1,3,4-trihydroxy-5-(pyridine-3-yl)cyclohex-5-en-1-carboxylic acid
-
pH 8.2, 25C
0.59
-
(1R,3R,4R)-1,3,4-trihydroxy-5-(thiophen-3-yl)phenyl-cyclohex-5-en-1-carboxylic acid
-
pH 8.2, 25C
1.5
-
(1R,3R,4R)-1,3,4-trihydroxy-5-phenylcyclohex-5-en-1-carboxylic acid
-
pH 8.2, 25C
0.37
-
(1R,4R,5R)-1,4,5-trihydroxy-2-cyclohexene-1-carboxylic acid
-
-
0.0000057
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(1-phenyl-1H-1,2,3-triazol-4-yl)cyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.000039
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(1-phenyl-1H-1,2,3-triazol-4-yl)cyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.000225
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(1-phenyl-1H-1,2,3-triazol-4-yl)cyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.063
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(1H-1,2,3-triazol-4-yl)cyclohex-2-en-1-carboxylic acid
-
-
0.141
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(2-nitrophenyl)cyclohex-2-ene-1-carboxylic acid
-
-
0.11
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(2-nitrothien-3-yl)cyclohex-2-en-1-carboxylic acid
-
-
0.0046
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(3-bromothien-2-yl)cyclohex-2-en-1-carboxylic acid
-
-
0.128
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(3-hydroxyphenyl)cyclohex-2-ene-1-carboxylic acid
-
-
0.000054
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(3-nitrophenyl)cyclohex-2-ene-1-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.0384
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(3-nitrophenyl)cyclohex-2-ene-1-carboxylic acid
-
-
0.001
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(3-nitrothien-2-yl)cyclohex-2-en-1-carboxylic acid
-
-
0.00049
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(3-phenoxyphenyl)cyclohex-2-ene-1-carboxylic acid
-
in 50 mM Tris-HCl, pH 7, at 25C
0.00049
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(3-phenoxyphenyl)cyclohex-2-ene-1-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.0068
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(4-nitrophenyl)cyclohex-2-ene-1-carboxylic acid
-
-
0.00054
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(thien-2-yl)cyclohex-2-en-1-carboxylic acid
-
-
0.00025
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(thiophen-2-yl)cyclohex-2-ene-1-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.00054
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(thiophen-2-yl)cyclohex-2-ene-1-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.00059
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(thiophen-2-yl)cyclohex-2-ene-1-carboxylic acid
-
in 50 mM Tris-HCl, pH 7, at 25C
0.0037
-
(1R,4R,5R)-1,4,5-trihydroxy-3-naphthalen-2-ylcyclohex-2-ene-1-carboxylic acid
-
-
0.0074
-
(1R,4R,5R)-1,4,5-trihydroxy-3-phenylcyclohex-2-ene-1-carboxylic acid
-
-
0.056
-
(1R,4R,5R)-1,4,5-trihydroxy-3-pyridin-3-ylcyclohex-2-ene-1-carboxylic acid
-
-
0.0018
-
(1R,4R,5R)-1,4,5-trihydroxy-3-thiophen-3-ylcyclohex-2-ene-1-carboxylic acid
-
-
0.00012
-
(1R,4R,5R)-1,4,5-trihydroxy-3-[(1E)-3-phenoxyprop-1-en-1-yl]cyclohex-2-ene-1-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.000048
-
(1R,4R,5R)-1,4,5-trihydroxy-3-[1-(2-hydroxyphenyl)-1H-1,2,3-triazol-4-yl]cyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.000157
-
(1R,4R,5R)-1,4,5-trihydroxy-3-[1-(2-hydroxyphenyl)-1H-1,2,3-triazol-4-yl]cyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.00033
-
(1R,4R,5R)-1,4,5-trihydroxy-3-[1-(2-hydroxyphenyl)-1H-1,2,3-triazol-4-yl]cyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.000078
-
(1R,4R,5R)-1,4,5-trihydroxy-3-[1-(3-nitrophenyl)-1H-1,2,3-triazol-4-yl]cyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.00023
-
(1R,4R,5R)-1,4,5-trihydroxy-3-[1-(3-nitrophenyl)-1H-1,2,3-triazol-4-yl]cyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.000538
-
(1R,4R,5R)-1,4,5-trihydroxy-3-[1-(3-nitrophenyl)-1H-1,2,3-triazol-4-yl]cyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.0000057
-
(1R,4R,5R)-1,4,5-trihydroxy-3-[1-(pyridin-3-yl)-1H-1,2,3-triazol-4-yl]cyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.000136
-
(1R,4R,5R)-1,4,5-trihydroxy-3-[1-(pyridin-3-yl)-1H-1,2,3-triazol-4-yl]cyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.000375
-
(1R,4R,5R)-1,4,5-trihydroxy-3-[1-(pyridin-3-yl)-1H-1,2,3-triazol-4-yl]cyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.000073
-
(1R,4R,5R)-1,4,5-trihydroxy-3-[1-(thiophen-2-ylmethyl)-1H-1,2,3-triazol-4-yl]cyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.000925
-
(1R,4R,5R)-1,4,5-trihydroxy-3-[1-(thiophen-2-ylmethyl)-1H-1,2,3-triazol-4-yl]cyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.001579
-
(1R,4R,5R)-1,4,5-trihydroxy-3-[1-(thiophen-2-ylmethyl)-1H-1,2,3-triazol-4-yl]cyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.00038
-
(1R,4R,5R)-1,4,5-trihydroxy-3-[3-(phenylsulfanyl)phenyl]cyclohex-2-ene-1-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.139
-
(1R,4R,5R)-1,4,5-trihydroxy-3-[3-(trifluoromethyl)phenyl]cyclohex-2-ene-1-carboxylic acid
-
-
0.00014
-
(1R,4R,5R)-1,4,5-trihydroxy-3-[3-phenoxy-prop-(E)-enyl]-cyclohex-2-enecarboxylic acid
P0A4Z6
recombinant enzyme, pH 7.0, 25C
-
0.0084
-
(1R,4R,5R)-1,4,5-trihydroxy-3-[4-(trifluoromethyl)phenyl]cyclohex-2-ene-1-carboxylic acid
-
-
0.03
-
(1R,4R,5R)-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
-
-
0.06
-
(1R,4R,5R)-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
-
-
0.2
-
(1R,4R,5R)-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
-
-
3
-
(1R,4R,5R)-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
-
-
0.0142
-
(1R,4R,5R)-3-(1-benzofuran-5-yl)-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
-
-
0.0071
-
(1R,4R,5R)-3-(1-benzofuran-6-yl)-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
-
-
0.0036
-
(1R,4R,5R)-3-(1-benzothiophen-5-yl)-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
-
-
0.0081
-
(1R,4R,5R)-3-(1-benzothiophen-6-yl)-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
-
-
0.025
-
(1R,4R,5R)-3-(2-carboxy-vinyl)-1,4,5-trihydroxy-cyclohex-2-enecarboxylic acid
-
pH 7.0
0.105
-
(1R,4R,5R)-3-(2-carboxy-vinyl)-1,4,5-trihydroxy-cyclohex-2-enecarboxylic acid
-
pH 7.0
0.0205
-
(1R,4R,5R)-3-(3,5-difluorophenyl)-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
-
-
0.4
-
(1R,4R,5R)-3-(3-carbonitrilethien-2-yl)-1,4,5-trihydroxycyclohex-2-en-1-carboxylic acid
-
larger than 0.400 mM
0.0094
-
(1R,4R,5R)-3-(3-fluorophenyl)-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
-
-
0.011
-
(1R,4R,5R)-3-(4-fluorophenyl)-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
-
-
0.001
-
(1R,4R,5R)-3-(furan-2-yl)-1,4,5-trihydroxycyclohex-2-en-1-carboxylic acid
-
-
0.027
-
(1R,4R,5R)-3-(tert-butylcarbamoyl)-1,4,5-trihydroxycyclohex-2-enecarboxylic acid
-
pH 7.0
0.027
-
(1R,4R,5R)-3-(tert-butylcarbamoyl)-1,4,5-trihydroxycyclohex-2-enecarboxylic acid
P0A4Z6
recombinant enzyme, pH 7.0, 25C
0.029
-
(1R,4R,5R)-3-(tert-butylcarbamoyl)-1,4,5-trihydroxycyclohex-2-enecarboxylic acid
-
pH 7.0
0.00485
-
(1R,4R,5R)-3-furan-3-yl-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
-
-
0.000029
-
(1R,4R,5R)-3-[1-(4-fluorophenyl)-1H-1,2,3-triazol-4-yl]-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.000154
-
(1R,4R,5R)-3-[1-(4-fluorophenyl)-1H-1,2,3-triazol-4-yl]-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.000561
-
(1R,4R,5R)-3-[1-(4-fluorophenyl)-1H-1,2,3-triazol-4-yl]-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.000217
-
(1R,4R,5R)-3-[1-(furan-2-ylmethyl)-1H-1,2,3-triazol-4-yl]-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.002122
-
(1R,4R,5R)-3-[1-(furan-2-ylmethyl)-1H-1,2,3-triazol-4-yl]-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.0022
-
(1R,4R,5R)-3-[1-(furan-2-ylmethyl)-1H-1,2,3-triazol-4-yl]-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.0023
-
(1R,4S,5R)-1,4,5-trihydroxy-3-[(1E)-3-phenoxyprop-1-en-1-yl]cyclohex-2-ene-1-carboxylic acid
P0A4Z6
recombinant enzyme, pH 7.0, 25C
0.7
-
(1R,4S,5R)-3,3-difluoro-1,4,5-trihydroxycyclohexane-1-carboxylic acid
-
-
8
-
(1R,4S,5R)-3,3-difluoro-1,4,5-trihydroxycyclohexane-1-carboxylic acid
-
-
0.00013
-
(1R,4S,5R)-3-(1-benzothiophen-2-ylmethoxy)-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.01
-
(1R,4S,5R)-3-fluoro-1,4,5-trihydroxy-2-cyclohexene-1-carboxylic acid
-
-
0.015
-
(1R,4S,5R)-3-fluoro-1,4,5-trihydroxy-2-cyclohexene-1-carboxylic acid
-
-
1.5
-
(1R,4S,5R)-3-fluoro-1,4,5-trihydroxy-2-cyclohexene-1-carboxylic acid
-
-
0.015
-
(1S,3R,4R)-1,3,4-trihydroxy-5-methylenecyclohexanecarboxylic acid
-
-
0.02
-
(1S,3R,4R)-1,3,4-trihydroxy-5-methylenecyclohexanecarboxylic acid
-
-
0.5
-
(1S,3R,4R)-1,3,4-trihydroxy-5-methylenecyclohexanecarboxylic acid
-
-
0.6
-
(1S,3R,4R)-1,3,4-trihydroxycyclohexanecarboxylic acid
-
-
1.2
-
(1S,3R,4R)-1,3,4-trihydroxycyclohexanecarboxylic acid
-
-
1.5
-
(1S,3R,4R)-1,3,4-trihydroxycyclohexanecarboxylic acid
-
-
4.5
-
(1S,3R,4R)-1,3,4-trihydroxycyclohexanecarboxylic acid
-
-
0.7
-
(1S,3R,4R,5E)-1,3,4-trihydroxy-5-(methylimino)cyclohexanecarboxylic acid
-
-
2.2
-
(1S,3R,4R,5E)-1,3,4-trihydroxy-5-(methylimino)cyclohexanecarboxylic acid
-
-
2.5
-
(1S,3R,4R,5E)-1,3,4-trihydroxy-5-(methylimino)cyclohexanecarboxylic acid
-
-
0.011
-
(1S,4R,5R)-3-(3-benzoylphenyl)-1,4,5-trihydroxycyclohex-2-enecarboxylic acid
P0A4Z6
recombinant enzyme, pH 7.0, 25C
-
0.000032
-
(3R,5R,6R)-3,5,6-trihydroxycyclohex-1-ene-1,3-dicarboxylic acid
-
pH 7.0
0.00094
-
(3R,5R,6R)-3,5,6-trihydroxycyclohex-1-ene-1,3-dicarboxylic acid
-
pH 7.0
0.00094
-
(3R,5R,6R)-3,5,6-trihydroxycyclohex-1-ene-1,3-dicarboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.00024
-
(3R,5R,6R)-3-carbamoyl-3,5,6-trihydroxycyclohex-1-enecarboxylic acid
-
pH 7.0
0.016
-
(3R,5R,6R)-3-carbamoyl-3,5,6-trihydroxycyclohex-1-enecarboxylic acid
-
pH 7.0
0.2
-
2,3-anhydroquinate
P0A4Z6
recombinant enzyme, pH 7.0, 25C
0.37
-
2,3-anhydroquinate
-
-
0.76
-
3-hydroxy-cyclohex-1-ene-1,3-dicarboxylic acid
-
pH 7.0
1.7
-
3-hydroxy-cyclohex-1-ene-1,3-dicarboxylic acid
-
pH 7.0
0.15
-
3-[(3R,5R,6R)-3-carboxy-3,5,6-trihydroxycyclohex-1-en-1-yl]benzoic acid
-
-
0.00172
-
3-[4-[(3R,5R,6R)-3-carboxy-3,5,6-trihydroxycyclohex-1-en-1-yl]-1H-1,2,3-triazol-1-yl]benzoic acid
-
pH 7.5, 25C
0.003126
-
3-[4-[(3R,5R,6R)-3-carboxy-3,5,6-trihydroxycyclohex-1-en-1-yl]-1H-1,2,3-triazol-1-yl]benzoic acid
-
pH 7.5, 25C
0.00578
-
3-[4-[(3R,5R,6R)-3-carboxy-3,5,6-trihydroxycyclohex-1-en-1-yl]-1H-1,2,3-triazol-1-yl]benzoic acid
-
pH 7.5, 25C
0.65
-
4-hydroxy-2-hydroxymethyl-4-methyl-pent-2-enedioic acid
-
pH 7.0
1
-
4-hydroxy-2-hydroxymethyl-4-methyl-pent-2-enedioic acid
-
pH 7.0
0.47
-
4-hydroxy-4-methyl-pent-2-enedioic acid
-
pH 7.0
0.99
-
4-hydroxy-4-methyl-pent-2-enedioic acid
-
pH 7.0
0.0000008
-
carbaphosphonate
-
-
0.0025
-
citrate
-
-
0.3
-
citrazinic acid
P0A4Z6
recombinant enzyme, pH 7.0, 25C
-
0.02
-
N-tetrazol-5-yl-9-oxo-9H-xanthene-2-sulfonamide
-
-
7
-
phosphate
-
pH 7, 25C
0.00013
-
sodium (1R,4S,5R)-1,4,5-trihydroxy-3-(5-methylbenzo[b]-thiophen-2-yl)methoxycyclohex-2-en-1-carboxylate
-
in 50 mM Tris-HCl, pH 7, at 25C
0.000132
-
sodium (1R,4S,5R)-1,4,5-trihydroxy-3-(benzo[b]thiophen-2-yl)methoxycyclohex-2-en-1-carboxylate
-
in 50 mM Tris-HCl, pH 7, at 25C
0.00092
-
sodium (1R,4S,5R)-1,4,5-trihydroxy-3-(thien-2-yl)methoxycyclohex-2-en-1-carboxylate
-
in 50 mM Tris-HCl, pH 7, at 25C
0.000166
-
sodium (1R,4S,5R)-1,4,5-trihydroxy-3-[(benzo[b]thiophen-5-yl)methoxy]cyclohex-2-en-1-carboxylate
-
in 50 mM Tris-HCl, pH 7, at 25C
11
-
sulfate
-
pH 7, 25C
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.000028
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(phenylethynyl)cyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.000253
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(phenylethynyl)cyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.000356
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(phenylethynyl)cyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.000171
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(pyridin-3-ylethynyl)cyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.000712
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(pyridin-3-ylethynyl)cyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.002194
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(pyridin-3-ylethynyl)cyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.000168
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(quinolin-3-ylethynyl)cyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.000885
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(quinolin-3-ylethynyl)cyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.001203
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(quinolin-3-ylethynyl)cyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.0000071
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(thiophen-2-ylethynyl)cyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.000187
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(thiophen-2-ylethynyl)cyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.000316
-
(1R,4R,5R)-1,4,5-trihydroxy-3-(thiophen-2-ylethynyl)cyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.0000022
-
(1R,4R,5R)-1,4,5-trihydroxy-3-[(3-nitrophenyl)ethynyl]cyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.000098
-
(1R,4R,5R)-1,4,5-trihydroxy-3-[(3-nitrophenyl)ethynyl]cyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.000133
-
(1R,4R,5R)-1,4,5-trihydroxy-3-[(3-nitrophenyl)ethynyl]cyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.0000069
-
(1R,4R,5R)-1,4,5-trihydroxy-3-[[3-(trifluoromethyl)phenyl]ethynyl]cyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.000103
-
(1R,4R,5R)-1,4,5-trihydroxy-3-[[3-(trifluoromethyl)phenyl]ethynyl]cyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.000108
-
(1R,4R,5R)-1,4,5-trihydroxy-3-[[3-(trifluoromethyl)phenyl]ethynyl]cyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.0000075
-
(1R,4R,5R)-3-(1,3-benzothiazol-2-ylethynyl)-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.000094
-
(1R,4R,5R)-3-(1,3-benzothiazol-2-ylethynyl)-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.000126
-
(1R,4R,5R)-3-(1,3-benzothiazol-2-ylethynyl)-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.000012
-
(1R,4R,5R)-3-[(4-fluorophenyl)ethynyl]-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.000106
-
(1R,4R,5R)-3-[(4-fluorophenyl)ethynyl]-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.000548
-
(1R,4R,5R)-3-[(4-fluorophenyl)ethynyl]-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
-
pH 7.5, 25C
0.000026
-
(2R)-2-p-methoxybenzyl-3-dehydroquinic acid
-
pH not specified in the publication, temperature not specified in the publication
-
0.00017
-
(2R)-2-p-methoxybenzyl-3-dehydroquinic acid
-
pH and temperature not specified in the publication
-
0.000089
-
(2R)-2-p-methylbenzyl-3-dehydroquinic acid
-
pH not specified in the publication, temperature not specified in the publication
-
0.00025
-
(2R)-2-p-methylbenzyl-3-dehydroquinic acid
-
pH and temperature not specified in the publication
-
0.000047
-
(2R)-2-pentafluoro-benzyl-3-dehydroquinic acid
-
pH not specified in the publication, temperature not specified in the publication
-
0.0026
-
(2R)-2-pentafluoro-benzyl-3-dehydroquinic acid
-
pH and temperature not specified in the publication
-
0.00000084
-
(4R,6R,7S)-2-(1-cyclopropylethyl)-4,6,7-trihydroxy-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
pH 7.5, 25C
0.00009
-
(4R,6R,7S)-2-(1-cyclopropylethyl)-4,6,7-trihydroxy-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
pH 7.5, 25C
0.0006
-
(4R,6R,7S)-2-(1-cyclopropylethyl)-4,6,7-trihydroxy-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
pH 7.5, 25C
0.000052
-
(4R,6R,7S)-2-ethenyl-4,6,7-trihydroxy-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
pH 7.5, 25C
0.00081
-
(4R,6R,7S)-2-ethenyl-4,6,7-trihydroxy-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
pH 7.5, 25C
0.00126
-
(4R,6R,7S)-2-ethenyl-4,6,7-trihydroxy-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
pH 7.5, 25C
0.000069
-
(4R,6R,7S)-2-ethyl-4,6,7-trihydroxy-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
pH 7.5, 25C
0.00032
-
(4R,6R,7S)-2-ethyl-4,6,7-trihydroxy-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
pH 7.5, 25C
0.0000011
-
(4R,6R,7S)-2-[(1E)-2-cyclopropylprop-1-en-1-yl]-4,6,7-trihydroxy-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
pH 7.5, 25C
0.00011
-
(4R,6R,7S)-2-[(1E)-2-cyclopropylprop-1-en-1-yl]-4,6,7-trihydroxy-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
pH 7.5, 25C
0.00108
-
(4R,6R,7S)-2-[(1E)-2-cyclopropylprop-1-en-1-yl]-4,6,7-trihydroxy-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
pH 7.5, 25C
0.000022
-
(4R,6R,7S)-4,6,7-trihydroxy-2-(2-hydroxyethyl)-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
pH 7.5, 25C
0.000049
-
(4R,6R,7S)-4,6,7-trihydroxy-2-(2-hydroxyethyl)-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
pH 7.5, 25C
0.000122
-
(4R,6R,7S)-4,6,7-trihydroxy-2-(2-hydroxyethyl)-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
pH 7.5, 25C
0.00086
-
(4R,6R,7S)-4,6,7-trihydroxy-2-(prop-2-en-1-yl)-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
pH 7.5, 25C
0.0018
-
(4R,6R,7S)-4,6,7-trihydroxy-2-(prop-2-en-1-yl)-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
pH 7.5, 25C
0.038
-
(4R,6R,7S)-4,6,7-trihydroxy-2-(prop-2-en-1-yl)-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
pH 7.5, 25C
0.00019
-
(4R,6R,7S)-4,6,7-trihydroxy-2-(propan-2-yl)-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
pH 7.5, 25C
0.0019
-
(4R,6R,7S)-4,6,7-trihydroxy-2-(propan-2-yl)-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
pH 7.5, 25C
0.0034
-
(4R,6R,7S)-4,6,7-trihydroxy-2-(propan-2-yl)-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
pH 7.5, 25C
0.0004
-
(4R,6R,7S)-4,6,7-trihydroxy-2-methyl-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
pH 7.5, 25C
0.0016
-
(4R,6R,7S)-4,6,7-trihydroxy-2-methyl-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
pH 7.5, 25C
0.00315
-
(4R,6R,7S)-4,6,7-trihydroxy-2-methyl-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
pH 7.5, 25C
0.000093
-
(4R,6R,7S)-4,6,7-trihydroxy-2-[(1Z)-prop-1-en-1-yl]-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
pH 7.5, 25C
0.000097
-
(4R,6R,7S)-4,6,7-trihydroxy-2-[(1Z)-prop-1-en-1-yl]-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
pH 7.5, 25C
0.00035
-
(4R,6R,7S)-4,6,7-trihydroxy-2-[(1Z)-prop-1-en-1-yl]-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
pH 7.5, 25C
0.0003
-
(4R,6R,7S)-4,6,7-trihydroxy-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
pH 7.5, 25C
0.0097
-
(4R,6R,7S)-4,6,7-trihydroxy-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
pH 7.5, 25C
0.034
-
(4R,6R,7S)-4,6,7-trihydroxy-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
-
pH 7.5, 25C
0.000028
-
benzo[b]thiophen-5-yl-3-dehydroquinic acid
-
pH not specified in the publication, temperature not specified in the publication
-
0.00016
-
benzo[b]thiophen-5-yl-3-dehydroquinic acid
-
pH and temperature not specified in the publication
-
0.061
-
HTS 11955
-
-
0.0845
-
RH00573
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0002
-
-
sDQD, cell-free extract
0.0036
-
-
sDQD, purification step DEAE-cellulose
0.02
-
-
pDQD, membrane fraction
0.07
-
-
pDQD, solubilizez fraction
0.089
-
-
-
0.09
-
-
pDQD, purification step DEAE-cellulose
0.096
-
-
-
0.2
-
-
sDQD, purification step DEAE-Sephadex A-50
0.28
-
-
pDQD, purification step DEAE-Sephadex A-50
0.45
-
-
sDQD, purification step Sephadex G-200
0.83
-
-
sDQD, heat treatment
0.97
-
-
pDQD, purification step Hydroxyapatite
additional information
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
-
-
enzymatic assay
7
-
P0A4Z6
assay at
7.2
-
-
activity assay
7.5
8
-
activity assay
7.5
-
Clostridium difficile, Salmonella enterica
-
assay at
8.3
-
-
assay at
9
-
-, Q6PUF9, Q6PUG0
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
9
-
pH 6.5: about 65% of maximal activity, pH 9.0: about 95% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
-, Q6PUF9, Q6PUG0
assay at room temperature
25
-
-
activity assay
25
-
-
activity assay
25
-
P0A4Z6
assay at
30
45
-, Q6PUF9, Q6PUG0
-
37
-
-
enzymatic assay
37
-
Clostridium difficile, Salmonella enterica
-
assay at
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
-
-, O30011
calculated pI-value
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
young and mature
Manually annotated by BRENDA team
-, Q6PUF9, Q6PUG0
;
Manually annotated by BRENDA team
Emericella nidulans WA53
-
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Gluconobacter oxydans IFO 3244
-
cDQD
-
Manually annotated by BRENDA team
-, Q6PUF9, Q6PUG0
DHD/SHD-2; NtDHD/SHD-2 is the cytosolic isoenzyme
Manually annotated by BRENDA team
-
cytosolic isozyme sDQD
Manually annotated by BRENDA team
Gluconobacter oxydans IFO 3244
-
cytosolic isozyme sDQD
-
Manually annotated by BRENDA team
-
membrane-bound isoform mDQD
Manually annotated by BRENDA team
Gluconobacter oxydans IFO 3244
-
membrane-bound isoform mDQD; pDQD
-
Manually annotated by BRENDA team
Gluconobacter oxydans IFO 3244
-
pDQD
-
-
Manually annotated by BRENDA team
-, Q6PUF9, Q6PUG0
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Bacillus subtilis (strain 168)
Bifidobacterium longum subsp. longum (strain JDM301)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Clostridium difficile (strain 630)
Clostridium difficile (strain 630)
Geobacillus kaustophilus (strain HTA426)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Salmonella typhi
Salmonella typhi
Salmonella typhi
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Staphylococcus aureus (strain MRSA252)
Staphylococcus aureus (strain MRSA252)
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
16000
-
-
pDQD, determined by SDS-PAGE, suggesting a multisubunit structure composed of 12 subunits
16270
-
-
putative deduced molecular weight
22200
-
-, O30011
determined by mass spectrometry
44000
53000
-
sedimentation velocity determination and equilibrium sedimentation
47000
-
-
sDQD, determined by SDS-PAGE, suggesting a multisubunit structure composed of eight subunits
47270
-
-
putative deduced molecular weight
49500
-
-
bifunctional enzyme with activities of ec 1.1.1.25 and ec 4.2.1.10, sucrose density gradient centrifugation
52000
-
-, O30011
determined by size-exclusion chromatography
58000
-
-
gel filtration
135000
-
-
gel filtration
167000
-
-
sucrose density gradient centrifugation
185000
232000
-
light scattering method
189000
-
-
sDQD, determined by gel filtration
190000
200000
-
determination of sedimentation velocity and equilibrium sedimentation
191000
-
-
pDQD, determined by gel filtration
209000
-
-
gel filtration
230000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 10000, SDS-PAGE
?
-
x * 18200, calculation from nucleotide sequence
?
-
x * 16505, calculation from nucleotide sequence
?
Emericella nidulans WA53
-
x * 16505, calculation from nucleotide sequence
-
dimer
-
2 * 29000, SDS-PAGE
dimer
-
2 * 27466
dimer
Escherichia coli AB2848/pKS201
-
2 * 29000, SDS-PAGE
-
dodecamer
-
12 * 16000-18000, SDS-PAGE; 12 * 18483, calculation from nucleotide sequence
dodecamer
-
12 * 16000, SDS-PAGE
dodecamer
-
12 * 16505
dodecamer
-
10 * 10000, SDS-PAGE
dodecamer
-
crystallographic data
dodecamer
-
homododecamer, four trimers are arranged in a tetrahedral manner, crystallographic data
dodecamer
-
dodecamer of 23 symmetry, with each of the four trimers occupying the face of a tetrahedron
dodecamer
-
x-ray crystallography
homodimer
-, O30011
-
monomer
-
1 * 43500-48000, bifunctional enzyme with activities of ec 1.1.1.25 and ec 4.2.1.10, SDS-PAGE, gel filtration in presence of 6 M guanidine hydrochloride
multimer
Gluconobacter oxydans IFO 3244
-
-
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystals obtained in space and on earth using the counter-diffusion technique
-
vapor diffusion hanging-drop technique, crystal structure of DHQ-SDH with shikimate bound at the SDH site and tartrate at the DHQ site
Q9SQT8
the structure of the 3-dehydroquinate dehydratase dimer is determined at 2.33 A resolution
-, O30011
wild-type enzyme post-dehydration covalent intermediate, from 100 mM Tris, pH 8.5, 30% w/v PEG 500, X-ray diffraction structure determination and analysis at 2.20 A resolution
Clostridium difficile
-
DHQ2 in complex with (2R)-2-p-methoxybenzyl-3-dehydroquinic acid, sitting drop vapour diffusion method, 20 mg/ml protein in 50 mM Tris-HCl, pH 7.5, 1 mM 2-mercaptoethanol, 1 mM EDTA, and 200 mM NaCl, with addition of (2R)-2-p-methoxybenzyl-3-dehydroquinic acid at 0.25 M in methanol and added at a ratio of 1:20 v/v, mixing of 0.002 ml protein solution with 0.002 ml reservoir solution containing 31% w/v PEG 4000 and 0.1 M sodium citrate, pH 5.0, and equilibation against 0.15 ml reservoir solution, room temperature, X-ray diffraction structure determination and analysis at 2.4-2.5 A resolution, modelling
-
DHQ2 in complex with inhibitors (4R,6R,7S)-4,6,7-trihydroxy-2-[(1Z)-prop-1-en-1-yl]-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid and (4R,6R,7S)-2-(1-cyclopropylethyl)-4,6,7-trihydroxy-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid, X-ray diffraction structure determination and analysis at 1.95 and 1.85 A resolution, respectively
-
DHQase-AH9095 complex
-
hanging drop vapor diffusion method
-
sitting drop vapor diffusion method, crystal structures of type II dehydroquinase with the inhibitors 2,3-anhydroquinate, citrate or N-tetrazol-5-yl-9-oxo-9H-xanthene-2-sulfonamide
-
sitting drop vapor diffusion method, using 26% (w/v) polyethyleneglycol 4000 and 0.1 M 2-(N-morpholino)ethanesulfonic acid sodium hydroxide, pH 5.0
-
the crystal structure of dehydroquinate synthase complexed with NAD is determined at 2.4 A resolution
-
truncated form of type II DHQase
-
DHQ2 in complex with (2R)-2-p-methoxybenzyl-3-dehydroquinic acid, sitting drop vapour diffusion method, 20 mg/ml protein in 50 mM Tris-HCl, pH 7.5, 1 mM 2-mercaptoethanol, 1 mM EDTA, and 200 mM NaCl, with addition of (2R)-2-p-methoxybenzyl-3-dehydroquinic acid at 0.25 M in methanol and added at a ratio of 1:20 v/v, mixing of 0.002 ml protein solution with 0.002 ml reservoir solution containing 32% v/v 2-methyl-2,4-pentanediol, 0.3 M ammonium sulfate and 0.1 M HEPES, pH 7.5, and equilibation against 0.15 ml reservoir solution, room temperature, X-ray diffraction structure determination and analysis at 2.4-2.5 A resolution, modelling
-
enzyme in complex with product 3-dehydroshikimate, X-ray diffraction structure determination and analysis
P0A4Z6
hanging drop vapor diffusion method
-
purified recombinant DHQD by sitting drop vaour diffusion method, generation of three different crystal forms, the protein solution contains 500 mM NaCl and 10 mM Tris-HCl, pH 8.3, mixing of protein and reservoir solution in a 1:1 ratio at room temperature, the reservoir solutions contain: 200 mM MgCl2 and 20% PEG 3350, or 170 mM NH4OAc, pH 4.6, 25.5% PEG 4000, and 15% glycerol, or 200 mM MgCl2, 100 mM Tris, pH 8.5, and 20% PEG 3350 for the wild-type enzyme in open or in closed conformation of for the mutant Q236A, X-ray diffraction structure determination and analysis at 1.03-1.93 A resolution. The Q236A enzyme crystallized in another crystal form that diffracts to a significantly higher resolution than any of the wild-type crystals
-
wild-type enzyme pre-dehydration covalent intermediate, and mutant K170M in complex with 3-dehydroquinate, crystallization of the wild-type enzyme from 170 mM NH4OAc, pH 4.6, 25.5% w/v PEG 4000, 15% v/v glycerol, the mutant is crystallized from 50 mM K2PO4, pH 6.0, 20% w/v PEG 8000, X-ray diffraction structure determination and analysis at 1.6-1.95 A resolution
-
sitting-drop vapor-diffusion method
-
large DHQaseCA1 inhibitor complex
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3
-
-
reversible dissociation into inactive subunits
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
57
-
-
Tm: 57C, irreversible thermal denaturation
70
-
-
10 min, stable
70
-
-
10 min, not stable
82
-
-
irreversible thermal denaturation involves at least three transitions. The first is a broad shoulder at approximately 82C, the second is a shoarp doublet at 86C and the final transition occurs at 95C
additional information
-
-
extremly resistant to thermal denaturation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
guanidine hydrochloride, the type II enzyme from Aspergillus nidulans unfolds at concentrations of denaturant 4fold greater than type I enzyme from E. coli and through a series of discrete transitions, while the type I enzyme from E. coli unfolds in a single transition
-
extremly resistant to denaturation by urea and guanidine hydrochloride at 25C
-
irreversible inactivation by SDS and guanidine hydrochloride at 55C
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-15C, stable for 6 months
-
-20C, 50 mM Tris-HCl buffer, pH 7.5, 0.4 mM dithiothreitol, 50 mM KCl, 50% v/v glycerol, 1 mM benzamidine, at a protein concentration of 2 mg/ml, stable for 1-2 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
HiTrap-Q anion-exchange media is used
-, O30011
periplasmic and cytosolic 3-dehydroquinate dehydratases are purified using a DEAE-cellulose, a DEAE-Sephadex A-50, a Hydroxyapatite and a Sephadex G-200 column
-
purified by immobilized nickel-ion chromatography
-
using a Q Sepharose, a phenyl Sepharose, a hydroxyapatite and a Sephacryl S300 column
-
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, cleavage of the His-tag, and gel filtration
P0A4Z6
catabolic isoenzyme
-
multienzyme complex with the activities of ec 1.1.1.25, ec 4.2.1.10, 5-dehydroquinate synthetase, 3-enolpyruvylshikimic acid 5-phosphate synthetase and shikimic acid kinase
-
bifunctional enzyme with activities of ec 1.1.1.25 and ec 4.2.1.10
-
recombinant His-tagged DHQD from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli
-
the full-length gene At3g06350 encoding DHQ-SDH and expression construct DELTA88DHQ-SDH, representing residues 89-603, are PCR amplified from Arabidopsis thaliana cDNA and clons into a modified pET28 vector at the NdeI and BamHI site, expression in Escherichia coli
Q9SQT8
into the vector pET3a for expression in Escherichia coli BL21DE3 Codon Plus cells
-, O30011
aroC gene expressed in both Bacillus subtilis and Escherichia coli
-
3-dehydroquinase domain
-
catabolic isoenzyme
-
expression of the arom gene cluster encoding the biosynthetic isoenzyme in Escherichia coli
-
expression in Escherichia coli
-
into the pQE30 vector for expression in Escherichia coli JM109 cells
-
into the vector pET21a for expression in Escherichia coli BL21DE3 cells
-
type II dehydroquinase, expressed in Escherichia coli
-
expressed in Escherichia coli
-
gene aroD, expression in Escherichia coli strain BL21(DE3) as His6-tagged protein. The enzyme is cloned with a thrombin cleavage site or the pET28b vector with a modified tobacco etch virus cleavage site after the N-terminal His6 tag
P0A4Z6
overexpression in Escherichia coli
-
catabolic isoenzyme expressed in Escherichia coli
-
the biosynthetic isoenzyme produced by the aro cluster, expression in Escherichia coli
-
DNA and amino acid sequence determination and analysis; NtDHD/SHD-1 is expressed in Escherichia coli; NtDHD/SHD-2
-, Q6PUF9, Q6PUG0
overexpression of His-tagged DHQD from MCSG7 expression vector in Escherichia coli strain BL21(DE3)
-
overexpression in Escherichia coli
-
expressed in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
isozyme 3 is down-regulated (28%) at 4C
-
the expression of SVCR3 is not affected by light intensity alone up to 0.2 mM photon m-2 s-1 at temperatures higher than 10C, very little SVCR3 is expressed at 20C regardless of the light intensity
-
when combined with light (above 0.05 mM photon m-2 s-1) the expression of SVCR3 increases more at 4C. Isozymes 1 and 2 are up-regulated (38% and 24%, respectively) at 4C
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
K170M
-
site-directed mutagenesis, methionine is closest in shape to a lysine but cannot form a Schiff base, mutation of Lys170 results in a dramatic loss in reactivity. Comparison of mutant and wild-type crystal structures, the K170M substrate-bound structure reveals that His143 adopts partial occupancies of both of the conformations observed in the wild-type structures, overview
Q236A
-
site-directed mutagenesis, substrate binding structure and kinetics compared to the wild-type enzyme, the mutant shows highly reduced catalytic activity. The loop mutant fails to induce a conformational change in Arg213
S232A
-
site-directed mutagenesis, substrate binding structure and kinetics compared to the wild-type enzyme, the mutant shows highly reduced catalytic activity
K170M
Salmonella enterica LT2
-
site-directed mutagenesis, methionine is closest in shape to a lysine but cannot form a Schiff base, mutation of Lys170 results in a dramatic loss in reactivity. Comparison of mutant and wild-type crystal structures, the K170M substrate-bound structure reveals that His143 adopts partial occupancies of both of the conformations observed in the wild-type structures, overview
-
R23A
-
reduced catalytic activity, replacement of Arg23 results in Tyr28 adopting an alternative conformation, more favourable than the one required for catalysis
additional information
-, Q6PUF9, Q6PUG0
expression of endogenous DHD/SHD-1 is suppressed by RNAi in transgenic tobacco plants, the transgenic lines with less than 40% of wild-type activity display severe growth retardation and reduced content of aromatic amino acids and downstream products such as cholorogenic acid and lignin, but accumulation of dehydroquinate and shikimate, possibly due to existence of a parallel extra-plastidic shikimate pathway into which dehydroquinate is diverted with a second gene DHD/SHD-2 in tobacco lacking a plastidic targeting sequence, the cytosolic shikimate synthesis cannot complement loss of the plastidial pathway, phenotype, overview
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
at 0.5 mM guanidinium chloride the enzyme dissociates into trimeric units with little or no change in the secondary or tertiary structure and a 55% increase of activity. At higher concentrations the enzyme undergoes sharp unfolding transitions. When the concentration is lowered from 6 M to 0.55 M the enzyme refolds in an efficient manner to form trimeric units with less than 35% regain of activity
-
at 0.5 mM guanidinium chloride the enzyme dissociates into trimeric units with little or no change in the secondary or tertiary structure and a 15% loss of activity. At higher concentrations the enzyme undergoes sharp unfolding transitions. When the concentration is lowered from 6M to 0.55 M the enzyme refolds in an efficient manner to form trimeric units with more than 75% regain of activity
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
drug development
-
the enzyme is an attractive target for the development of new antimicrobials and herbicides
medicine
-
dehydroquinate synthase is a target for microbial agents, anti-parasitic agents and herbicides
medicine
-
dehydroquinase is a target for the development of new antibiotics
drug development
P0A4Z6
absence of the shikimate patway from humans makes the enzymes of this pathway potential drug targets
drug development
-
the enzyme is an attractive target for the development of new antimicrobials and herbicides
drug development
-
the absence of DHQD in humans and its essentiality in many pathogenic bacteria make the enzyme a target for the development of nontoxic antimicrobials and design of type I DHQD inhibiting molecules
drug development
-
the enzyme is an attractive target for the development of new antimicrobials and herbicides