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Information on EC 4.2.1.10 - 3-dehydroquinate dehydratase and Organism(s) Streptomyces coelicolor and UniProt Accession P15474
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EC Tree
4.2.1.10 3-dehydroquinate dehydrataseSpecify your search results
Word Map
- 4.2.1.10
-
quinic
- 7-phosphate
-
3-deoxy-d-arabino-heptulosonate
- chorismate
-
pentafunctional
- dahp
- epsps
- 2-deoxy-scyllo-inosose
-
5-enolpyruvylshikimate
-
2-deoxystreptamine-containing
-
1.1.1.25
- 2-deoxystreptamine
- drug development
- medicine
- analysis
The taxonomic range for the selected organisms is: Streptomyces coelicolor
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
dehydroquinase, dehydroquinate synthase, 3-dehydroquinase, type ii dehydroquinase, dhqase, 3-dehydroquinate dehydratase, dhq synthase, dehydroquinate dehydratase, type i dehydroquinase, type i dhqd, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-dehydroquinase
-
-
-
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3-dehydroquinate dehydratase
-
-
-
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5-dehydroquinase
-
-
-
-
5-dehydroquinate dehydratase
-
-
-
-
5-dehydroquinate hydro-lyase
-
-
-
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dehydratase, 3-dehydroquinate
-
-
-
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dehydroquinase
-
-
-
-
dehydroquinate dehydratase
-
-
-
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DHQ synthase
-
-
-
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DHQase
-
-
-
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Type I dehydroquinase
-
-
-
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Type I DHQase
-
-
-
-
Type II dehydroquinase
Type II DHQase
Type II dehydroquinase
-
-
-
-
Type II DHQase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-dehydroquinate = 3-dehydroshikimate + H2O
the first step of the reaction involves the formation of an imine intermediate between the oxo group of the 3-dehydroquinate and the enzyme
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3-dehydroquinate = 3-dehydroshikimate + H2O
type II dehydroquinase catalyzes a trans-dehydration via an enolate intermediate
-
3-dehydroquinate = 3-dehydroshikimate + H2O
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
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3-dehydroquinate = 3-dehydroshikimate + H2O
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
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
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-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
3-dehydroquinate hydro-lyase (3-dehydroshikimate-forming)
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CAS REGISTRY NUMBER
COMMENTARY
9012-66-2
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
role in shikimate pathway
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
role in shikimate pathway
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(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-(thiophen-2-ylethynyl)cyclohex-2-ene-1-carboxylic acid
-
(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-[[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-[(4-fluorophenyl)ethynyl]-1,4,5-trihydroxycyclohex-2-ene-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-fluoro-1,4,5-trihydroxy-2-cyclohexene-1-carboxylic acid
inhibitor is selective for the type II dehydroquinase over the type I dehydroquinase
(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-[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)-3-(2-carboxy-vinyl)-1,4,5-trihydroxy-cyclohex-2-enecarboxylic acid
-
-
(1R,4R,5R)-3-(tert-butylcarbamoyl)-1,4,5-trihydroxycyclohex-2-enecarboxylic 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
(1S,3R,4R)-1,3,4-trihydroxy-5-methylenecyclohexanecarboxylic acid
-
-
(1S,3R,4R,5E)-1,3,4-trihydroxy-5-(methylimino)cyclohexanecarboxylic acid
-
-
(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
-
-
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
additional information
development of a range of ene-yne-based inhibitors, active site docking study using enzyme structure PDB ID 1GU1, overview
-
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
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additional information
-
inhibitor design and synthesis, binding structure and inhibition mechanism, overview
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.7
(1R,4S,5R)-3,3-difluoro-1,4,5-trihydroxycyclohexane-1-carboxylic acid
-
0.015
(1R,4S,5R)-3-fluoro-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, 25°C
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, 25°C
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, 25°C
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, 25°C
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, 25°C
0.025
(1R,4R,5R)-3-(2-carboxy-vinyl)-1,4,5-trihydroxy-cyclohex-2-enecarboxylic acid
-
pH 7.0
0.029
(1R,4R,5R)-3-(tert-butylcarbamoyl)-1,4,5-trihydroxycyclohex-2-enecarboxylic acid
-
pH 7.0
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, 25°C
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, 25°C
0.5
(1S,3R,4R)-1,3,4-trihydroxy-5-methylenecyclohexanecarboxylic acid
-
-
2.5
(1S,3R,4R,5E)-1,3,4-trihydroxy-5-(methylimino)cyclohexanecarboxylic acid
-
-
0.000032
(3R,5R,6R)-3,5,6-trihydroxycyclohex-1-ene-1,3-dicarboxylic acid
-
pH 7.0
0.00024
(3R,5R,6R)-3-carbamoyl-3,5,6-trihydroxycyclohex-1-enecarboxylic acid
-
pH 7.0
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, 25°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000028
(1R,4R,5R)-1,4,5-trihydroxy-3-(phenylethynyl)cyclohex-2-ene-1-carboxylic acid
Streptomyces coelicolor
pH 7.5, 25°C
0.000171
(1R,4R,5R)-1,4,5-trihydroxy-3-(pyridin-3-ylethynyl)cyclohex-2-ene-1-carboxylic acid
Streptomyces coelicolor
pH 7.5, 25°C
0.000168
(1R,4R,5R)-1,4,5-trihydroxy-3-(quinolin-3-ylethynyl)cyclohex-2-ene-1-carboxylic acid
Streptomyces coelicolor
pH 7.5, 25°C
0.0000071
(1R,4R,5R)-1,4,5-trihydroxy-3-(thiophen-2-ylethynyl)cyclohex-2-ene-1-carboxylic acid
Streptomyces coelicolor
pH 7.5, 25°C
0.0000022
(1R,4R,5R)-1,4,5-trihydroxy-3-[(3-nitrophenyl)ethynyl]cyclohex-2-ene-1-carboxylic acid
Streptomyces coelicolor
pH 7.5, 25°C
0.0000069
(1R,4R,5R)-1,4,5-trihydroxy-3-[[3-(trifluoromethyl)phenyl]ethynyl]cyclohex-2-ene-1-carboxylic acid
Streptomyces coelicolor
pH 7.5, 25°C
0.0000075
(1R,4R,5R)-3-(1,3-benzothiazol-2-ylethynyl)-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
Streptomyces coelicolor
pH 7.5, 25°C
0.000012
(1R,4R,5R)-3-[(4-fluorophenyl)ethynyl]-1,4,5-trihydroxycyclohex-2-ene-1-carboxylic acid
Streptomyces coelicolor
pH 7.5, 25°C
0.00000084
(4R,6R,7S)-2-(1-cyclopropylethyl)-4,6,7-trihydroxy-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
Streptomyces coelicolor
-
pH 7.5, 25°C
0.00081
(4R,6R,7S)-2-ethenyl-4,6,7-trihydroxy-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
Streptomyces coelicolor
-
pH 7.5, 25°C
0.00032
(4R,6R,7S)-2-ethyl-4,6,7-trihydroxy-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
Streptomyces coelicolor
-
pH 7.5, 25°C
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
Streptomyces coelicolor
-
pH 7.5, 25°C
0.000022
(4R,6R,7S)-4,6,7-trihydroxy-2-(2-hydroxyethyl)-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
Streptomyces coelicolor
-
pH 7.5, 25°C
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
Streptomyces coelicolor
-
pH 7.5, 25°C
0.0019
(4R,6R,7S)-4,6,7-trihydroxy-2-(propan-2-yl)-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
Streptomyces coelicolor
-
pH 7.5, 25°C
0.00315
(4R,6R,7S)-4,6,7-trihydroxy-2-methyl-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
Streptomyces coelicolor
-
pH 7.5, 25°C
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
Streptomyces coelicolor
-
pH 7.5, 25°C
0.0097
(4R,6R,7S)-4,6,7-trihydroxy-4,5,6,7-tetrahydro-1-benzothiophene-4-carboxylic acid
Streptomyces coelicolor
-
pH 7.5, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
dehydroquinase catalyzes the third step in the shikimate pathway, the reversible dehydration of 3-dehydroquinate to 3-dehydroshikimate
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dodecamer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R23A
reduced catalytic activity, replacement of Arg23 results in Tyr28 adopting an alternative conformation, more favourable than the one required for catalysis
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
RENATURED/Commentary
ORGANISM
UNIPROT
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 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
COMMENTARY
LITERATURE
drug development
-
the enzyme is an attractive target for the development of new antimicrobials and herbicides
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
White, P.J.; Young, J.; Hunter, I.S.; Nimmo, H.G.; Coggins, J.R.
The purification and characterization of 3-dehydroquinase from Streptomyces coelicolor
Biochem. J.
265
735-738
1990
Streptomyces coelicolor
Frederickson, M.; Parker, E.J.; Hawkins, A.R.; Coggins, J.R.; Abell, C.
Selective inhibition of type II dehydroquinases
J. Org. Chem.
64
2612-2613
1999
Aspergillus nidulans, Mycobacterium tuberculosis, Salmonella enterica subsp. enterica serovar Typhi, Streptomyces coelicolor
Gourley, D.G.; Shrive, A.K.; Polikarpov, I.; Krell, T.; Coggins, J.R.; Hawkins, A.R.; Isaacs, N.W.; Sawyer, L.
The two types of 3-dehydroquinase have distinct structures but catalyze the same overall reaction
Nat. Struct. Biol.
6
521-525
1999
Helicobacter pylori, Mycobacterium tuberculosis (P9WPX7), Mycobacterium tuberculosis H37Rv (P9WPX7), Salmonella enterica subsp. enterica serovar Typhi, Streptomyces coelicolor
Price, N.C.; Boam, D.J.; Kelly, S.M.; Duncan, D.; Krell, T.; Gourley, D.G.; Coggins, J.R.; Virden, R.; Hawkins, A.R.
The folding and assembly of the dodecameric type II dehydroquinases
Biochem. J.
338
195-202
1999
Mycobacterium tuberculosis, Streptomyces coelicolor
-
Evans, L.D.B.; Roszak, A.W.; Noble, L.J.; Robinson, D.A.; Chalk, P.A.; Matthews, J.L.; Coggins, J.R.; Price, N.C.; Lapthorn, A.J.
Specificity of substrate recognition by type II dehydroquinases as revealed by binding of polyanions
FEBS Lett.
530
24-30
2002
Streptomyces coelicolor, Mycobacterium tuberculosis (P9WPX7), Mycobacterium tuberculosis H37Rv (P9WPX7)
Toscano, M.D.; Frederickson, M.; Evans, D.P.; Coggins, J.R.; Abell, C.; Gonzalez-Bello, C.
Design, synthesis and evaluation of bifunctional inhibitors of type II dehydroquinase
Org. Biomol. Chem.
1
2075-2083
2003
Streptomyces coelicolor
Roszak, A.W.; Robinson, D.A.; Krell, T.; Hunter, I.S.; Fredrickson, M.; Abell, C.; Coggins, J.R.; Lapthorn, A.J.
The structure and mechanism of the type II dehydroquinase from Streptomyces coelicolor
Structure
10
493-503
2002
Streptomyces coelicolor (P15474), Streptomyces coelicolor
Le Sann, C.; Gower, M.A.; Abell, A.D.
Inhibitors of types I and II dehydroquinase
Mini Rev. Med. Chem.
4
747-756
2004
Aspergillus nidulans, Mycobacterium tuberculosis, Salmonella enterica subsp. enterica serovar Typhimurium, Streptomyces coelicolor
Frederickson, M.; Roszak, A.W.; Coggins, J.R.; Lapthorn, A.J.; Abell, C.
(1R,4S,5R)-3-Fluoro-1,4,5-trihydroxy-2-cyclohexene-1-carboxylic acid: the fluoro analogue of the enolate intermediate in the reaction catalyzed by type II dehydroquinases
Org. Biomol. Chem.
2
1592-1596
2004
Salmonella enterica subsp. enterica serovar Typhi, Streptomyces coelicolor (P15474), Mycobacterium tuberculosis (P9WPX7), Mycobacterium tuberculosis H37Rv (P9WPX7)
Stewart, K.A.; Robinson, D.A.; Lapthorn, A.J.
Type II dehydroquinase: molecular replacement with many copies
Acta Crystallogr. Sect. D
64
108-118
2008
Helicobacter pylori, Streptomyces coelicolor (P15474)
Toscano, M.D.; Payne, R.J.; Chiba, A.; Kerbarh, O.; Abell, C.
Nanomolar inhibition of type II dehydroquinase based on the enolate reaction mechanism
ChemMedChem
2
101-112
2007
Mycobacterium tuberculosis, Salmonella enterica subsp. enterica serovar Typhi, Streptomyces coelicolor
Payne, R.J.; Peyrot, F.; Kerbarh, O.; Abell, A.D.; Abell, C.
Rational design, synthesis, and evaluation of nanomolar type II dehydroquinase inhibitors
ChemMedChem
2
1015-1029
2007
Mycobacterium tuberculosis, Streptomyces coelicolor
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194-207
2007
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5
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2009
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262-265
2011
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Paz, S.; Tizon, L.; Otero, J.; Llamas-Saiz, A.; Fox, G.; Van Raaij, M.; Lamb, H.; Hawkins, A.; Lapthorn, A.; Castedo, L.; Gonzalez-Bello, C.
Tetrahydrobenzothiophene derivatives: conformationally restricted inhibitors of type II dehydroquinase
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6
266-272
2011
Helicobacter pylori, Mycobacterium tuberculosis, Streptomyces coelicolor
Tran, A.; Cergol, K.; Britton, W.; Imran Bokhari, S.; Ibrahim, M.; Lapthorn, A.; Payne, R.
Rapid assembly of potent type II dehydroquinase inhibitors via 'click' chemistry
MedChemComm
1
271-275
2010
Helicobacter pylori, Mycobacterium tuberculosis, Streptomyces coelicolor
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