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Ligand 3-dehydroquinic acid

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

chorismate metabolism, quinate degradation

KEGG

Biosynthesis of amino acids, Biosynthesis of secondary metabolites, Phenylalanine, tyrosine and tryptophan biosynthesis

MetaCyc

3-dehydroquinate biosynthesis I, 3-dehydroquinate biosynthesis II (archaea), chorismate biosynthesis from 3-dehydroquinate, gallate biosynthesis, quinate degradation I, quinate degradation II more

Show all BRENDA pathways known for 3-dehydroquinic acid

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (19 results)

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Show Natural Substrate (19 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.24

3-dehydroquinate + NADH = quinate + NAD+

286365, 286359, 286364

-

1.1.1.25

3-dehydroquinate = 3-dehydroshikimate + H2O

740724

-

1.1.1.282

3-dehydroquinate + NADPH + H+ = L-quinate + NADP+

657079

-

4.2.1.10

3-dehydroquinate = 3-dehydroshikimate + H2O

714749, 729166, 714751, 714752, 716099, 730168, 730537, 691374, 714521, 715639, 730780, 729133, 690276, 691819, 714238, 730899, 729270, 729076

1j2y, 3D-view

4.2.1.10

3-dehydroquinate = 3-dehydroshikimate + H2O

714749, 729166, 714751, 714752, 716099, 730168, 730537, 691374, 714521, 715639, 730780, 729133, 690276, 691819, 714238, 730899, 729270, 729076

3m7w, 3D-view

4.2.1.10

3-dehydroquinate = 3-dehydroshikimate + H2O

714749, 729166, 714751, 714752, 716099, 730168, 730537, 691374, 714521, 715639, 730780, 729133, 690276, 691819, 714238, 730899, 729270, 729076

3nnt, 3D-view

4.2.1.10

3-dehydroquinate = 3-dehydroshikimate + H2O

714749, 729166, 714751, 714752, 716099, 730168, 730537, 691374, 714521, 715639, 730780, 729133, 690276, 691819, 714238, 730899, 729270, 729076

5ydb, 3D-view

4.2.1.10

3-dehydroquinate = ?

5485, 5483, 5486, 5482, 5474, 5477

1j2y, 3D-view

4.2.1.10

3-dehydroquinate = ?

5485, 5483, 5486, 5482, 5474, 5477

3m7w, 3D-view

4.2.1.10

3-dehydroquinate = ?

5485, 5483, 5486, 5482, 5474, 5477

3nnt, 3D-view

4.2.1.10

3-dehydroquinate = ?

5485, 5483, 5486, 5482, 5474, 5477

5ydb, 3D-view

4.2.1.10

5-dehydroquinate = ?

5468, 5464, 5469, 5470

1j2y, 3D-view

4.2.1.10

5-dehydroquinate = ?

5468, 5464, 5469, 5470

3m7w, 3D-view

4.2.1.10

5-dehydroquinate = ?

5468, 5464, 5469, 5470

3nnt, 3D-view

4.2.1.10

5-dehydroquinate = ?

5468, 5464, 5469, 5470

5ydb, 3D-view

4.2.1.10

dehydroquinate = dehydroshikimate + H2O

681134

1j2y, 3D-view

4.2.1.10

dehydroquinate = dehydroshikimate + H2O

681134

3m7w, 3D-view

4.2.1.10

dehydroquinate = dehydroshikimate + H2O

681134

3nnt, 3D-view

4.2.1.10

dehydroquinate = dehydroshikimate + H2O

681134

5ydb, 3D-view

4.2.1.10

16 entries

In Vivo Product in Enzyme-catalyzed Reactions (22 results)

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Show Natural Product (22 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.24

L-quinate + NAD+ = 3-dehydroquinate + NADH + H+

0

-

1.1.1.24

L-quinate + NAD+ = 5-dehydroquinate + NADH + H+

0

-

1.1.1.24

quinate + NAD+ = 5-dehydroquinate + NADH + H+

0

-

1.1.1.24

quinic acid + NAD(P)+ = dehydroquinic acid + NAD(P)H + H+

0

-

1.1.1.25

L-quinate + NAD+ = 3-dehydroquinate + NADH + H+

0

-

1.1.1.25

L-quinate + NADP+ = 3-dehydroquinate + NADPH + H+

0

-

1.1.1.25

quinate + NAD+ = 3-dehydroquinate + NADH + H+

0

-

1.1.1.25

quinate + NADP+ = 3-dehydroquinate + NADPH + H+

0

-

1.1.1.282

L-quinate + NAD+ = 3-dehydroquinate + NADH + H+

0

-

1.1.1.282

L-quinate + NADP+ = 3-dehydroquinate + NADPH + H+

0

-

1.1.1.282

quinate + NAD+ = 3-dehydroquinate + NADH + H+

0

-

1.1.1.282

quinate + NADP+ = 3-dehydroquinate + NADPH + H+

0

-

1.1.5.8

quinate + pyrroloquinoline quinone = 3-dehydroquinate + pyrroloquinoline quinol

0

-

1.1.5.8

quinate + pyrroloquinoline-quinone = 3-dehydroquinate + reduced pyrroloquinoline-quinone

0

-

1.1.1.24

4 entries

1.1.1.25

4 entries

1.1.1.282

4 entries

1.1.5.8

2 entries

1.4.1.24

3,7-dideoxy-D-threo-hepto-2,6-diulosonic acid + H2O + NAD+ = 3-dehydroquinate + NH3 + NADH + H+

0

-

4.2.1.10

3-deoxy-D-arabino-heptulosonate 7-phosphate = 3-dehydroquinate + phosphate

0

1j2y, 3D-view

4.2.1.10

3-deoxy-D-arabino-heptulosonate 7-phosphate = 3-dehydroquinate + phosphate

0

3m7w, 3D-view

4.2.1.10

3-deoxy-D-arabino-heptulosonate 7-phosphate = 3-dehydroquinate + phosphate

0

3nnt, 3D-view

4.2.1.10

3-deoxy-D-arabino-heptulosonate 7-phosphate = 3-dehydroquinate + phosphate

0

5ydb, 3D-view

4.2.3.4

3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate = 3-dehydroquinate + phosphate

0

-

4.2.3.4

3-deoxy-D-arabino-heptulosonate 7-phosphate = 3-dehydroquinate + phosphate

0

-

4.2.3.4

3-deoxy-D-arabinoheptulosonate 7-phosphate = 3-dehydroquinate + phosphate

0

-

4.2.1.10

4 entries

4.2.3.4

3 entries

Substrate in Enzyme-catalyzed Reactions (29 results)

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Show Substrate (29 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.24

3-dehydroquinate + NADH = quinate + NAD+

286365, 286359, 286364

-

1.1.1.25

3-dehydroquinate + NADH + H+ = quinate + NAD+

724089

-

1.1.1.25

3-dehydroquinate + NADPH + H+ = quinate + NADP+

724089

-

1.1.1.25

3-dehydroquinate = 3-dehydroshikimate + H2O

740724

-

1.1.1.25

3 entries

1.1.1.282

3-dehydroquinate + NADPH + H+ = L-quinate + NADP+

656292, 657079

-

4.2.1.10

3-dehydroquinate = 3-dehydroshikimate

666869

1j2y, 3D-view

4.2.1.10

3-dehydroquinate = 3-dehydroshikimate

666869

3m7w, 3D-view

4.2.1.10

3-dehydroquinate = 3-dehydroshikimate

666869

3nnt, 3D-view

4.2.1.10

3-dehydroquinate = 3-dehydroshikimate

666869

5ydb, 3D-view

4.2.1.10

3-dehydroquinate = 3-dehydroshikimate + H2O

666281, 5473, 5474, 5483, 5476, 5481, 5482, 5467, 665979, 714749, 729166, 747022, 714751, 714752, 716099, 5480, 651312, 5477, 649154, 730168, 730537, 691374, 714521, 5466, 5479, 649195, 5486, 715639, 730780, 729133, 653902, 704811, 690276, 702935, 691819, 703225, 705060, 748427, 714238, 730899, 729270, 729076, 746712, 746640, 749133, 762187

1j2y, 3D-view

4.2.1.10

3-dehydroquinate = 3-dehydroshikimate + H2O

666281, 5473, 5474, 5483, 5476, 5481, 5482, 5467, 665979, 714749, 729166, 747022, 714751, 714752, 716099, 5480, 651312, 5477, 649154, 730168, 730537, 691374, 714521, 5466, 5479, 649195, 5486, 715639, 730780, 729133, 653902, 704811, 690276, 702935, 691819, 703225, 705060, 748427, 714238, 730899, 729270, 729076, 746712, 746640, 749133, 762187

3m7w, 3D-view

4.2.1.10

3-dehydroquinate = 3-dehydroshikimate + H2O

666281, 5473, 5474, 5483, 5476, 5481, 5482, 5467, 665979, 714749, 729166, 747022, 714751, 714752, 716099, 5480, 651312, 5477, 649154, 730168, 730537, 691374, 714521, 5466, 5479, 649195, 5486, 715639, 730780, 729133, 653902, 704811, 690276, 702935, 691819, 703225, 705060, 748427, 714238, 730899, 729270, 729076, 746712, 746640, 749133, 762187

3nnt, 3D-view

4.2.1.10

3-dehydroquinate = 3-dehydroshikimate + H2O

666281, 5473, 5474, 5483, 5476, 5481, 5482, 5467, 665979, 714749, 729166, 747022, 714751, 714752, 716099, 5480, 651312, 5477, 649154, 730168, 730537, 691374, 714521, 5466, 5479, 649195, 5486, 715639, 730780, 729133, 653902, 704811, 690276, 702935, 691819, 703225, 705060, 748427, 714238, 730899, 729270, 729076, 746712, 746640, 749133, 762187

5ydb, 3D-view

4.2.1.10

3-dehydroquinate = ?

5485, 5483, 5486, 5482, 5474, 5477

1j2y, 3D-view

4.2.1.10

3-dehydroquinate = ?

5485, 5483, 5486, 5482, 5474, 5477

3m7w, 3D-view

4.2.1.10

3-dehydroquinate = ?

5485, 5483, 5486, 5482, 5474, 5477

3nnt, 3D-view

4.2.1.10

3-dehydroquinate = ?

5485, 5483, 5486, 5482, 5474, 5477

5ydb, 3D-view

4.2.1.10

5-dehydroquinate = ?

5468, 5464, 5469, 5470

1j2y, 3D-view

4.2.1.10

5-dehydroquinate = ?

5468, 5464, 5469, 5470

3m7w, 3D-view

4.2.1.10

5-dehydroquinate = ?

5468, 5464, 5469, 5470

3nnt, 3D-view

4.2.1.10

5-dehydroquinate = ?

5468, 5464, 5469, 5470

5ydb, 3D-view

4.2.1.10

5-dehydroquinate = dehydroshikimate + H2O

5468, 5463, 5470, 747581, 5464

1j2y, 3D-view

4.2.1.10

5-dehydroquinate = dehydroshikimate + H2O

5468, 5463, 5470, 747581, 5464

3m7w, 3D-view

4.2.1.10

5-dehydroquinate = dehydroshikimate + H2O

5468, 5463, 5470, 747581, 5464

3nnt, 3D-view

4.2.1.10

5-dehydroquinate = dehydroshikimate + H2O

5468, 5463, 5470, 747581, 5464

5ydb, 3D-view

4.2.1.10

dehydroquinate = dehydroshikimate + H2O

681134

1j2y, 3D-view

4.2.1.10

dehydroquinate = dehydroshikimate + H2O

681134

3m7w, 3D-view

4.2.1.10

dehydroquinate = dehydroshikimate + H2O

681134

3nnt, 3D-view

4.2.1.10

dehydroquinate = dehydroshikimate + H2O

681134

5ydb, 3D-view

4.2.1.10

24 entries

Product in Enzyme-catalyzed Reactions (42 results)

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Show Product (42 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.166

(-)-quinate + NAD+ = 3-dehydroquinate + NADH + H+

286100

-

1.1.1.24

L-quinate + NAD+ = 3-dehydroquinate + NADH + H+

0

-

1.1.1.24

L-quinate + NADP+ = 3-dehydroquinate + NADPH + H+

0

-

1.1.1.24

L-quinate + NAD+ = 5-dehydroquinate + NADH + H+

0

-

1.1.1.24

quinate + NAD+ = 5-dehydroquinate + NADH + H+

0

-

1.1.1.24

quinic acid + NAD(P)+ = dehydroquinic acid + NAD(P)H + H+

0

-

1.1.1.25

L-quinate + NAD+ = 3-dehydroquinate + NADH + H+

0

-

1.1.1.25

L-quinate + NADP+ = 3-dehydroquinate + NADPH + H+

0

-

1.1.1.25

quinate + NAD(P)+ = 3-dehydroquinate + NAD(P)H + H+

0

-

1.1.1.25

quinate + NAD+ = 3-dehydroquinate + NADH + H+

0

-

1.1.1.25

quinate + NADP+ = 3-dehydroquinate + NADPH + H+

0

-

1.1.1.282

L-quinate + 3-acetylpyridine adenine dinucleotide = 3-dehydroquinate + ?

0

-

1.1.1.282

L-quinate + beta-NAD+ = 3-dehydroquinate + beta-NADH + H+

0

-

1.1.1.282

L-quinate + NAD(P)+ = 3-dehydroquinate + NAD(P)H + H+

0

-

1.1.1.282

L-quinate + NAD+ = 3-dehydroquinate + NADH + H+

0

-

1.1.1.282

L-quinate + NADP+ = 3-dehydroquinate + NADPH + H+

0

-

1.1.1.282

L-quinate + nicotinamide 1,N6-ethenoadenine dinucleotide = 3-dehydroquinate + ?

0

-

1.1.1.282

L-quinate + nicotinamide hypoxanthine dinucleotide = 3-dehydroquinate + ?

0

-

1.1.1.282

L-quinate + oxidized nicotinamide 1,N6-ethanoadenine dinucleotide = 3-dehydroquinate + reduced nicotinamide 1,N6-ethanoadenine dinucleotide

0

-

1.1.1.282

quinate + NAD(P)+ = 3-dehydroquinate + NAD(P)H + H+

0

-

1.1.1.282

quinate + NAD+ = 3-dehydroquinate + NADH + H+

0

-

1.1.1.282

quinate + NADP+ = 3-dehydroquinate + NADPH + H+

0

-

1.1.5.8

D-quinate + tetramethyl-p-phenylenediamine = 3-dehydroquinate + reduced tetramethyl-p-phenylenediamine

287799

-

1.1.5.8

quinate + 2,6-dichlorophenol indophenol = 3-dehydroquinate + reduced 2,6-dichlorophenol indophenol

0

-

1.1.5.8

quinate + 2,6-dichlorophenol-indophenol = 3-dehydroquinate + reduced 2,6-dichlorophenol-indophenol

0

-

1.1.5.8

quinate + ? = 3-dehydroquinate + ?

0

-

1.1.5.8

quinate + phenazine methosulfate = 3-dehydroquinate + reduced phenazine methosulfate

0

-

1.1.5.8

quinate + potassium ferricyanide = 3-dehydroquinate + reduced potassium ferricyanide

0

-

1.1.5.8

quinate + pyrroloquinoline quinone = 3-dehydroquinate + pyrroloquinoline quinol

0

-

1.1.5.8

quinate + pyrroloquinoline-quinone = 3-dehydroquinate + reduced pyrroloquinoline-quinone

0

-

1.4.1.24

2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate + H2O + NAD+ = 3-dehydroquinate + NH3 + NADH + H+

0

-

1.4.1.24

3,7-dideoxy-D-threo-hepto-2,6-diulosonic acid + H2O + NAD+ = 3-dehydroquinate + NH3 + NADH + H+

0

-

4.2.1.10

3-deoxy-D-arabino-heptulosonate 7-phosphate = 3-dehydroquinate + phosphate

0

1j2y, 3D-view

4.2.1.10

3-deoxy-D-arabino-heptulosonate 7-phosphate = 3-dehydroquinate + phosphate

0

3m7w, 3D-view

4.2.1.10

3-deoxy-D-arabino-heptulosonate 7-phosphate = 3-dehydroquinate + phosphate

0

3nnt, 3D-view

4.2.1.10

3-deoxy-D-arabino-heptulosonate 7-phosphate = 3-dehydroquinate + phosphate

0

5ydb, 3D-view

4.2.3.4

3-deoxy-arabino-heptulonate 7-phosphate = 3-dehydroquinate + phosphate

0

-

4.2.3.4

3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate = 3-dehydroquinate + phosphate

0

-

4.2.3.4

3-deoxy-D-arabino-heptulosonate 7-phosphate = 3-dehydroquinate + phosphate

0

-

4.2.3.4

3-deoxy-D-arabino-heptulosonic acid 7-phosphate = 3-dehydroquinate + phosphate

137619, 137623, 137624, 137628

-

4.2.3.4

3-deoxy-D-arabinoheptulosonate 7-phosphate = 3-dehydroquinate + phosphate

0

-

4.2.3.4

7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate

0

-

1.1.1.24

5 entries

1.1.1.25

5 entries

1.1.1.282

11 entries

1.1.5.8

8 entries

1.4.1.24

2 entries

4.2.1.10

4 entries

4.2.3.4

6 entries

Inhibitor in Enzyme-catalyzed Reactions (9 results)

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Show Inhibitors (9 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.24

-

286358

-

4.2.1.10

-

665986

1j2y, 3D-view

4.2.1.10

-

665986

3m7w, 3D-view

4.2.1.10

-

665986

3nnt, 3D-view

4.2.1.10

-

665986

5ydb, 3D-view

4.2.1.10

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

714105

1j2y, 3D-view

4.2.1.10

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

714105

3m7w, 3D-view

4.2.1.10

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

714105

3nnt, 3D-view

4.2.1.10

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

714105

5ydb, 3D-view

4.2.1.10

8 entries

3D Structure of Enzyme-Ligand-Complex (PDB) (28 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (28 entries)

EC NUMBER

ENZYME 3D STRUCTURE

4.2.1.10

1j2y, 3D-view

4.2.1.10

3m7w, 3D-view

4.2.1.10

3nnt, 3D-view

4.2.1.10

5ydb, 3D-view

4.2.1.10

1j2y, 3D-view

4.2.1.10

3m7w, 3D-view

4.2.1.10

3nnt, 3D-view

4.2.1.10

5ydb, 3D-view

4.2.1.10

1j2y, 3D-view

4.2.1.10

3m7w, 3D-view

4.2.1.10

3nnt, 3D-view

4.2.1.10

5ydb, 3D-view

4.2.1.10

1j2y, 3D-view

4.2.1.10

3m7w, 3D-view

4.2.1.10

3nnt, 3D-view

4.2.1.10

5ydb, 3D-view

4.2.1.10

1j2y, 3D-view

4.2.1.10

3m7w, 3D-view

4.2.1.10

3nnt, 3D-view

4.2.1.10

5ydb, 3D-view

4.2.1.10

1j2y, 3D-view

4.2.1.10

3m7w, 3D-view

4.2.1.10

3nnt, 3D-view

4.2.1.10

5ydb, 3D-view

4.2.1.10

1j2y, 3D-view

4.2.1.10

3m7w, 3D-view

4.2.1.10

3nnt, 3D-view

4.2.1.10

5ydb, 3D-view

4.2.1.10

28 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (56 results)

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Show Turnover Number (56 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.1.1.24

281

-

pH 7.5, 30°C, EcDQD/SDH4a, quinate formation

762187

1.1.1.25

0.36

-

pH 7.0, 30°C

724089

1.1.1.25

114

-

pH 7.0, 30°C

724089

1.1.1.282

9.31

-

pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADPH

724089

1.1.1.282

114

-

pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADH

724089

4.2.1.10

0.015

-

mutant K170M, pH 7.5, 37°C

715639

4.2.1.10

0.06

-

at pH 7.0, 25°C

703225

4.2.1.10

0.15

-

at pH 7.0, 25°C

703225

4.2.1.10

0.34

-

pH 7.5, 25°C

714751

4.2.1.10

1.1

-

pH 7.2, 25°C

747022

4.2.1.10

1.4

-

pH 7.5, 25°C

716099

4.2.1.10

2

-

-

5477

4.2.1.10

3.8

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

4.6

-

pH 7.5, 25°C

714751

4.2.1.10

4.63

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

5.2

-

pH 7, 25°C

651312

4.2.1.10

5.33

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

6.3

-

pH 7.5, 25°C

716099

4.2.1.10

6.88

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

6.9

-

pH 8.3, temperature not specified in the publication, mutant Q236A

714238

4.2.1.10

7.15

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

9.06

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

10.46

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

10.59

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

11.92

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

13.53

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

18

-

mutant enzyme E86A, at pH 7.5 and 37°C

730899

4.2.1.10

18.72

-

pH 7.0, 25°C

746640

4.2.1.10

20

-

-

5481

4.2.1.10

23.96

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

29.53

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

31.7

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

42.2

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

50.2

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

52.26

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

59.61

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

61

-

pH 7.5, 25°C

714751

4.2.1.10

75.11

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

77.06

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

78

-

mutant enzyme E86Q, at pH 7.5 and 37°C

730899

4.2.1.10

78.87

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

84

-

pH 7.5, 25°C

716099

4.2.1.10

102.15

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

102.7

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

107

-

pH 8.3, temperature not specified in the publication, mutant S232A

714238

4.2.1.10

110

-

pH 7.5, 25°C

749133

4.2.1.10

119.98

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

124

-

pH 7, 25°C

651312

4.2.1.10

125

-

wild-type enzyme, pH 7.5, 37°C

715639

4.2.1.10

154

-

pH 7.0, 25°C

747022

4.2.1.10

184.43

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

208.96

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

210

-

pH 8.3, temperature not specified in the publication, wild-type enzyme

714238

4.2.1.10

210

-

wild-type enzyme, pH 7.5, 37°C

715639

4.2.1.10

211.83

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

310

-

wild type enzyme, at pH 7.5 and 37°C

730899

1.1.1.25

2 entries

1.1.1.282

2 entries

4.2.1.10

51 entries

K_M Value (70 results)

top print hide

Show KM Value (70 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.24

0.047

-

-

286365

1.1.1.24

0.45

-

-

286365

1.1.1.24

1

-

-

286364

1.1.1.24

1.4

-

pH 7.5, 30°C, EcDQD/SDH4a, quinate formation

762187

1.1.1.25

0.00036

-

pH 7.0, 30°C

724089

1.1.1.25

0.42

-

pH 7.0, 30°C

724089

1.1.1.282

0.42

-

pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADH

724089

1.1.1.282

1

-

pH 10, 20°C, cosubstrate NADPH, form P1 of quinate (shikimate) dehydrogenase

657079

1.1.1.282

1.141

-

pH 7.0, temperature not specified in the publication, recombinant enzyme, with NADPH

724089

1.1.1.282

5.3

-

pH 10, 20°C, cosubstrate NADPH, form P2 of quinate (shikimate) dehydrogenase

657079

4.2.1.10

0.015

-

-

5483

4.2.1.10

0.015

-

at pH 7.0, 25°C

703225

4.2.1.10

0.015

-

pH 7.2, 25°C

747022

4.2.1.10

0.018

-

-

5473, 5474, 5479

4.2.1.10

0.018

-

-

666281

4.2.1.10

0.021

-

wild-type enzyme, pH 7.5, 37°C

715639

4.2.1.10

0.024

-

pH 7, 25°C

651312

4.2.1.10

0.024

-

pH 7.2, 25°C

747022

4.2.1.10

0.03

-

mutant enzyme E86Q, at pH 7.5 and 37°C

730899

4.2.1.10

0.033

-

mutant K170M, pH 7.5, 37°C

715639

4.2.1.10

0.036

-

pH 7.5, 25°C

714751

4.2.1.10

0.036

-

wild-type enzyme, pH 7.5, 37°C

715639

4.2.1.10

0.037

-

-

5482

4.2.1.10

0.04

-

apparent Km, pDQD

691374

4.2.1.10

0.046

-

mutant enzyme E86A, at pH 7.5 and 37°C

730899

4.2.1.10

0.05

-

apparent Km, sDQD

691374

4.2.1.10

0.052

-

pH 7.5, 25°C

716099

4.2.1.10

0.053

-

wild type enzyme, at pH 7.5 and 37°C

730899

4.2.1.10

0.064

-

-

666281

4.2.1.10

0.065

-

pH 7.5, 25°C

749133

4.2.1.10

0.0679

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

0.075

-

pH 7.5, 25°C

714751

4.2.1.10

0.0769

-

pH 7.5, 25°C

716099

4.2.1.10

0.1

-

pH 7, 25°C

651312

4.2.1.10

0.1071

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

0.121

-

-

5486

4.2.1.10

0.1316

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

0.134

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

0.1415

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

0.15

-

-

5483

4.2.1.10

0.15

-

-

666281

4.2.1.10

0.1588

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

0.1599

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

0.1807

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

0.1877

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

0.2026

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

0.2032

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

0.21

-

pH 7.5, 25°C

714751

4.2.1.10

0.2107

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

0.228

-

pH 7.5, 25°C

716099

4.2.1.10

0.2555

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

0.2814

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

0.3045

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

0.3685

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

0.4008

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

0.44

-

-

5463

4.2.1.10

0.4485

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

0.4787

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

0.48

-

at pH 7.0, 25°C

703225

4.2.1.10

0.5261

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

0.59

-

-

5477

4.2.1.10

0.6

-

-

5480

4.2.1.10

0.6016

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

0.6173

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

0.6245

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

0.65

-

-

666281

4.2.1.10

0.778

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

0.8704

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

1.2186

-

pH not specified in the publication, temperature not specified in the publication

746712

4.2.1.10

2.94

-

pH 7.0, 25°C

746640

1.1.1.24

4 entries

1.1.1.25

2 entries

1.1.1.282

4 entries

4.2.1.10

60 entries

K_i Value (2 results)

top print hide

Show KI Value (2 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

4.2.1.10

0.2

-

recombinant enzyme, pH 7.0, 25°C

714105

4.2.1.10

0.37

-

-

665986

4.2.1.10

2 entries

References & Links

Literature References (71)

top print hide

Show Reference (71 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

5463

13198937

Aromatic biosynthesis. XII. Conversion of 5-dehydroquinic acid to 5-dehydroshikimic acid by 5-dehydroquinase

1954

Mitsuhashi, S.; Davis, B.D.

Biochim. Biophys. Acta

15

54-61

5464

4263953

Purification and stability of the multienzyme complex encoded in the arom gene cluster of Neurospora crassa

1972

Jacobson, J.W.; Hart, B.A.; Doy, C.H.; Giles, N.H.

Biochim. Biophys. Acta

289

1-12

5466

687649

Purification and characterization of 3-dehydroquinate hydrolase and shikmate oxidoreductase. Evidence for a bifunctional enzyme

1978

Polley, L.D.

Biochim. Biophys. Acta

526

259-266

5467

-

Some properties of the initial four enzymes involved in shikimic acid biosynthesis in tea plant

1979

Saijo, R.; Takeo, T.

Agric. Biol. Chem.

43

1427-1432

5468

6270920

Aggregation und Trennbarkeit der Enzyme des Shikimat-Pathway bei Hefen

1981

Bode, R.; Birnbaum, D.

Z. Allg. Mikrobiol.

21

417-422

5469

6287167

Cloning and expression in Escherichia coli K-12 of the biosynthetic dehydroquinase function of the arom cluster gene from the eucaryote, Aspergillus nidulans

1982

Kinghorn, J.R.; Hawkins, A.R.

Mol. Gen. Genet.

186

145-152

5470

2993794

Cloning of the ARO cluster gene of Neurospora crassa and its expression in Escherichia coli

1985

Catchside, D.E.A.; Storer, P.J.; Klein, B.

Mol. Gen. Genet.

199

446-451

5473

2950851

Purification and characterization of 3-dehydroquinase from Escherichia coli

1986

Chaudhuri, S.; Lambert, J.M.; McColl, L.A.; Coggins, J.R.

Biochem. J.

239

699-704

5474

3037262

3-Dehydroquinate dehydratase from Escherichia coli

1987

Chaudhuri, S.; Duncan, K.; Coggins, J.R.

Methods Enzymol.

142

320-324

5476

2949740

Sequence analysis and transformation by the catabolic 3-dehydroquinase (QUTE) gene from Aspergillus nidulans

1986

da Silva, A.J.F.; Whittington, H.; Clements, J.; Roberts, C.; Hawkins, A.R

Biochem. J.

240

481-488

5477

8912695

Cloning, sequencing, expression, purification and preliminary characterization of a type II dehydroquinase from Helicobacter pylori

1996

Bottomley, J.R.; Clayton, C.L.; Chalk, P.A.; Kleanthous, C.

Biochem. J.

319

559-565

5479

8216229

Characterization of the type I dehydroquinase from Salmonella typhi

1993

Moore, J.D.; Hawkins, A.R.; Charles, I.G.; Deka, R.; Coggins, J.R.; Cooper, A.; Kelly, S.M.; Price, N.C.

Biochem. J.

295

277-285

5480

2306211

The purification and characterization of 3-dehydroquinase from Streptomyces coelicolor

1990

White, P.J.; Young, J.; Hunter, I.S.; Nimmo, H.G.; Coggins, J.R.

Biochem. J.

265

735-738

5481

1329726

Inducible overproduction of the Aspergillus nidulans pentafunctional AROM protein and the type-I and -II 3-dehydroquinase from Salmonella typhi and Mycobacterium tuberculosis

1992

Moore, J.D.; Lamb, H.K.; Garbe, T.; Servos, S.; Dougan, G.; Charles, I.G.; Hawkins, A.R.

Biochem. J.

287

173-181

5482

8050603

The characterisation of the shikimate pathway enzyme dehydroquinase from Pisum sativum

1994

Deka, R.K.; Anton, I.A.; Dunbar, B.; Coggins, J.R.

FEBS Lett.

349

397-402

5483

1554351

A comparison of the enzymological and biophysical properties of two distinct classes of dehydroquinase enzymes

1992

Kleanthous, C.; Deka, R.; Davis, K.; Kelly, S.M.; Cooper, A.; Harding, S.E.; Price, N.C.; Hawkins, A.R.; Coggins, J.R.

Biochem. J.

282

687-695

5485

10360352

The two types of 3-dehydroquinase have distinct structures but catalyze the same overall reaction

1999

Gourley, D.G.; Shrive, A.K.; Polikarpov, I.; Krell, T.; Coggins, J.R.; Hawkins, A.R.; Isaacs, N.W.; Sawyer, L.

Nat. Struct. Biol.

6

521-525

5486

1479361

Purification and characterization of a dual function 3-dehydroquinate dehydratase from Amycolatopsis methanolica

1992

Euverink, G.J.W.; Hessels, G.I.; Vrijbloed, J.W.; Coggins, J.R.; Dijkhuizen, L.

J. Gen. Microbiol.

138

2449-2457

137619

-

Chemical inhibition of dehydroquinate synthase

1989

Myrvold, S.; Reimer, L.M.; Pompliano,D.L.; Frost, J.W.

J. Am. Chem. Soc.

111

1861-1866

137623

3037261

Dehydroquinate synthase from Escherichia coli, and its substrate 3-deoxy-D-arabino-heptulosonic acid 7-phosphate

1987

Mehdi, S.; Frost, J.W.; Knowles, J.R.

Methods Enzymol.

142

306-314

137624

2824247

The anatomy of a multifunctional enzyme

1987

Coggins, J.R.; Duncan, K.; Anton, I.A.; Boocock, M.R.; Chaudhuri, S.; Lambert, J.M.; Lewendon, A.; Millar, G.; Mousdale, D.M.; Smith, D.D.S.

Biochem. Soc. Trans.

15

754-759

137628

3157372

The 3-dehydroquinate synthase activity of the pentafunctional arom enzyme complex of Neurospora crassa is Zn2+-dependent

1985

Lambert, J.M.; Boocock, M.R.; Coggins, J.R.

Biochem. J.

226

817-829

286100

4375976

A new nicotinamide-adenine dinucleotide-dependent hydroaromatic dehydrogenase of Lactobacillus plantarum and its role in formation of (-)t-3,t-4-dihydrocyclohexane-c-1carboxylate

1974

Whiting, G.C.; Coggins, R.A.

Biochem. J.

141

35-42

286358

-

Aromatic metabolism in plants III. Quinate dehydrogenase from mung bean cell suspension cultures

1966

Gamborg, O.L.

Biochim. Biophys. Acta

128

483-491

286359

-

The reversible association of quinate:NAD+ oxidoreductase from carrot cells with a putative regulatory subunit depends on light conditions

1983

Graziana, A.; Ranjeva, R.; Salimath, B.P.; Boudet, A.M.

FEBS Lett.

163

306-311

286364

-

Broad-specificity quinate (shikimate) dehydrogenase from Pinus taeda needles

2000

Ossipov, V.; Bonner, C.; Ossipova, S.; Jensen, R.

Plant Physiol.

38

923-928

286365

-

Purification and characterization of the quinate: oxidoreductase from Phaseolus mungo sprouts

1993

Kang, X.; Scheibe, R.

Phytochemistry

33

769-773

287799

3044290

Bacterial NAD(P)-independent quinate dehydrogenase is a quinoprotein

1988

Van Kleef, M.A.G.; Duine, J.A.

Arch. Microbiol.

150

32-36

649154

11173479

Crystallization and preliminary X-ray crystallographic analysis of type II dehydroquinase from Helicobacter pylori

2001

Kwak, J.E.; Lee, J.Y.; Han, B.W.; Moon, J.J.; Sohn, S.H.; Suh, S.W.

Acta Crystallogr. Sect. D

57

279-280

649195

11976491

Comparison of different crystal forms of 3-dehydroquinase from Salmonella typhi and its implication for the enzyme activity

2002

Lee, W.H.; Perles, L.A.; Nagem, R.A.; Shrive, A.K.; Hawkins, A.; Sawyer, L.; Polikarpov, I.

Acta Crystallogr. Sect. D

58

798-804

651312

12387860

Specificity of substrate recognition by type II dehydroquinases as revealed by binding of polyanions

2002

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.

FEBS Lett.

530

24-30

653902

11937054

The structure and mechanism of the type II dehydroquinase from Streptomyces coelicolor

2002

Roszak, A.W.; Robinson, D.A.; Krell, T.; Hunter, I.S.; Fredrickson, M.; Abell, C.; Coggins, J.R.; Lapthorn, A.J.

Structure

10

493-503

656292

15596430

Site-directed mutagenesis of the active site region in the quinate/shikimate 5-dehydrogenase YdiB of Escherichia coli

2005

Lindner, H.A.; Nadeau, G.; Matte, A.; Michel, G.; Menard, R.; Cygler, M.

J. Biol. Chem.

280

7162-7169

657079

-

Broad-specificity quinate (shikimate) dehydrogenase from Pinus taeda needles

2000

Ossipov, V.; Bonner, C.; Ossipova, S.; Jensen, R.

Plant Physiol. Biochem.

38

923-928

665979

16033267

Structure-based design, synthesis, and biological evaluation of inhibitors of Mycobacterium tuberculosis type II dehydroquinase

2005

Sanchez-Sixto, C.; Prazeres, V.F.; Castedo, L.; Lamb, H.; Hawkins, A.R.; Gonzalez-Bello, C.

J. Med. Chem.

48

4871-4881

665986

16480265

Crystal structures of Helicobacter pylori type II dehydroquinase inhibitor complexes: New Directions for Inhibitor Design

2006

Robinson, D.A.; Stewart, K.A.; Price, N.C.; Chalk, P.A.; Coggins, J.R.; Lapthorn, A.J.

J. Med. Chem.

49

1282-1290

666281

15379642

Inhibitors of types I and II dehydroquinase

2004

Le Sann, C.; Gower, M.A.; Abell, A.D.

Mini Rev. Med. Chem.

4

747-756

666869

15229896

Crystal structures of Staphylococcus aureus type I dehydroquinase from enzyme turnover experiments

2004

Nichols, C.E.; Lockyer, M.; Hawkins, A.R.; Stammers, D.K.

Proteins

56

625-628

681134

17463052

Functional analysis of the essential bifunctional tobacco enzyme 3-dehydroquinate dehydratase/shikimate dehydrogenase in transgenic tobacco plants

2007

Ding, L.; Hofius, D.; Hajirezaei, M.R.; Fernie, A.R.; Boernke, F.; Sonnewald, U.

J. Exp. Bot.

58

2053-2067

690276

18931429

Structure and lability of archaeal dehydroquinase

2008

Smith, N.N.; Gallagher, D.T.

Acta Crystallogr. Sect. F

64

886-892

691374

18540103

A novel 3-dehydroquinate dehydratase catalyzing extracellular formation of 3-dehydroshikimate by oxidative fermentation of Gluconobacter oxydans IFO 3244

2008

Adachi, O.; Ano, Y.; Toyama, H.; Matsushita, K.

Biosci. Biotechnol. Biochem.

72

1475-1482

691819

18200648

Competitive inhibitors of Helicobacter pylori type II dehydroquinase: synthesis, biological evaluation, and NMR studies

2008

Sanchez-Sixto, C.; Prazeres, V.F.; Castedo, L.; Suh, S.W.; Lamb, H.; Hawkins, A.R.; Canada, F.J.; Jimenez-Barbero, J.; Gonzalez-Bello, C.

ChemMedChem

3

756-770

702935

-

Cold stress regulation of a bi-functional 3-dehydroquinate dehydratase/shikimate dehydrogenase (DHQ/SDH)-like gene in the freshwater green alga Spirogyra varians

2009

Han, J.; Lee, K.; Yoon, M.; Kang, S.; Kim, G.

Botanica Marina

52

178-185

703225

19856378

2-Substituted-3-dehydroquinic acids as potent competitive inhibitors of type II dehydroquinase

2009

Prazeres, V.; Castedo, L.; Lamb, H.; Hawkins, A.; González-Bello, C.

ChemMedChem

4

1980-1984

704811

26609719

Theoretical study of the reaction mechanism of Streptomyces coelicolor type II dehydroquinase

2009

Blomberg, L.; Mangold, M.; Mitchell, J.; Blumberger, J.

J. Chem. Theory Comput.

5

1284-1294

705060

19911771

Synthesis and biological evaluation of new nanomolar competitive inhibitors of Helicobacter pylori type II dehydroquinase. Structural details of the role of the aromatic moieties with essential residues

2010

Prazeres, V.F.; Tizon, L.; Otero, J.M.; Guardado-Calvo, P.; Llamas-Saiz, A.L.; van Raaij, M.J.; Castedo, L.; Lamb, H.; Hawkins, A.R.; Gonzalez-Bello, C.

J. Med. Chem.

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714105

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Structural investigation of inhibitor designs targeting 3-dehydroquinate dehydratase from the shikimate pathway of Mycobacterium tuberculosis

2011

Dias, M.V.; Snee, W.C.; Bromfield, K.M.; Payne, R.J.; Palaninathan, S.K.; Ciulli, A.; Howard, N.I.; Abell, C.; Sacchettini, J.C.; Blundell, T.L.

Biochem. J.

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A conserved surface loop in type I dehydroquinate dehydratases positions an active site arginine and functions in substrate binding

2011

Light, S.H.; Minasov, G.; Shuvalova, L.; Peterson, S.N.; Caffrey, M.; Anderson, W.F.; Lavie, A.

Biochemistry

50

2357-2363

714521

20460715

Purification and characterization of membrane-bound 3-dehydroshikimate dehydratase from Gluconobacter oxydans IFO 3244, a new enzyme catalyzing extracellular protocatechuate formation

2010

Shinagawa, E.; Adachi, O.; Ano, Y.; Yakushi, T.; Matsushita, K.

Biosci. Biotechnol. Biochem.

74

1084-1088

714749

20815012

Understanding the key factors that control the inhibition of type II dehydroquinase by (2R)-2-benzyl-3-dehydroquinic acids

2010

Peon, A.; Otero, J.M.; Tizon, L.; Prazeres, V.F.; Llamas-Saiz, A.L.; Fox, G.C.; van Raaij, M.J.; Lamb, H.; Hawkins, A.R.; Gago, F.; Castedo, L.; Gonzalez-Bello, C.

ChemMedChem

5

1726-1733

714751

21275049

Synthesis and evaluation of potent ene-yne inhibitors of type II dehydroquinases as tuberculosis drug leads

2011

Tran, A.; Cergol, K.; West, N.; Randall, E.; Britton, W.; Bokhari, S.; Ibrahim, M.; Lapthorn, A.; Payne, R.

ChemMedChem

6

262-265

714752

21275050

Tetrahydrobenzothiophene derivatives: conformationally restricted inhibitors of type II dehydroquinase

2011

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.

ChemMedChem

6

266-272

715639

21087925

Insights into the mechanism of type I dehydroquinate dehydratases from structures of reaction intermediates

2011

Light, S.H.; Minasov, G.; Shuvalova, L.; Duban, M.E.; Caffrey, M.; Anderson, W.F.; Lavie, A.

J. Biol. Chem.

286

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Rapid assembly of potent type II dehydroquinase inhibitors via 'click' chemistry

2010

Tran, A.; Cergol, K.; Britton, W.; Imran Bokhari, S.; Ibrahim, M.; Lapthorn, A.; Payne, R.

MedChemComm

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271-275

724089

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Characterization of shikimate dehydrogenase homologues of Corynebacterium glutamicum

2013

Kubota, T.; Tanaka, Y.; Hiraga, K.; Inui, M.; Yukawa, H.

Appl. Microbiol. Biotechnol.

97

8139-8149

729076

24352733

Overexpression of a type II 3-dehydroquinate dehydratase enhances the biotransformation of quinate to 3-dehydroshikimate in Gluconobacter oxydans

2014

Nishikura-Imamura, S.; Matsutani, M.; Insomphun, C.; Vangnai, A.S.; Toyama, H.; Yakushi, T.; Abe, T.; Adachi, O.; Matsushita, K.

Appl. Microbiol. Biotechnol.

98

2955-2963

729133

23396056

Crystal structure of type I 3-dehydroquinate dehydratase of Aquifex aeolicus suggests closing of active site flap is not essential for enzyme action

2013

Devi, A.S.; Ebihara, A.; Kuramitsu, S.; Yokoyama, S.; Kumarevel, T.; Ponnuraj, K.

Biochem. Biophys. Res. Commun.

432

350-354

729166

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Mechanistic insight into the reaction catalysed by bacterial type II dehydroquinases

2014

Coderch, C.; Lence, E.; Peon, A.; Lamb, H.; Hawkins, A.R.; Gago, F.; Gonzalez-Bello, C.

Biochem. J.

458

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Crystal structures of type I dehydroquinate dehydratase in complex with quinate and shikimate suggest a novel mechanism of Schiff base formation

2014

Light, S.H.; Antanasijevic, A.; Krishna, S.N.; Caffrey, M.; Anderson, W.F.; Lavie, A.

Biochemistry

53

872-880

730168

24689821

Exploring the water-binding pocket of the type II dehydroquinase enzyme in the structure-based design of inhibitors

2014

Blanco, B.; Sedes, A.; Peon, A.; Otero, J.M.; van Raaij, M.J.; Thompson, P.; Hawkins, A.R.; Gonzalez-Bello, C.

J. Med. Chem.

57

3494-3510

730537

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New insights into the mechanism of the Schiff base hydrolysis catalyzed by type I dehydroquinate dehydratase from S. enterica: a theoretical study

2012

Yao, Y.; Li, Z.S.

Org. Biomol. Chem.

10

7037-7044

730780

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Discovery of selective inhibitors of the Clostridium difficile dehydroquinate dehydratase

2014

Ratia, K.; Light, S.H.; Antanasijevic, A.; Anderson, W.F.; Caffrey, M.; Lavie, A.

PLoS ONE

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Reassessing the type I dehydroquinate dehydratase catalytic triad: kinetic and structural studies of Glu86 mutants

2013

Light, S.H.; Anderson, W.F.; Lavie, A.

Protein Sci.

22

418-424

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24942735

Molecular characterization of quinate and shikimate metabolism in Populus trichocarpa

2014

Guo, J.; Carrington, Y.; Alber, A.; Ehlting, J.

J. Biol. Chem.

289

23846-23858

746640

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Structure of type II dehydroquinase from Pseudomonas aeruginosa

2014

Reiling, S.; Kelleher, A.; Matsumoto, M.; Robinson, G.; Asojo, O.

Acta Crystallogr. Sect. F

70

1485-1491

746712

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Unraveling the kinetic diversity of microbial 3-dehydroquinate dehydratases of shikimate pathway

2015

Liu, C.; Liu, Y.; Sun, Q.; Jiang, C.; Liu, S.

AMB Express

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Insights into substrate binding and catalysis in bacterial type I dehydroquinase

2014

Maneiro, M.; Peon, A.; Lence, E.; Otero, J.M.; Van Raaij, M.J.; Thompson, P.; Hawkins, A.R.; Gonzalez-Bello, C.

Biochem. J.

462

415-424

747581

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Design and structural analysis of aromatic inhibitors of type II dehydroquinase from Mycobacterium tuberculosis

2015

Howard, N.I.; Dias, M.V.; Peyrot, F.; Chen, L.; Schmidt, M.F.; Blundell, T.L.; Abell, C.

ChemMedChem

10

116-133

748427

26043661

Structure-based virtual screening as a tool for the identification of novel inhibitors against Mycobacterium tuberculosis 3-dehydroquinate dehydratase

2015

Petersen, G.O.; Saxena, S.; Renuka, J.; Soni, V.; Yogeeswari, P.; Santos, D.S.; Bizarro, C.V.; Sriram, D.

J. Mol. Graph. Model.

60

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Identification of polyketide inhibitors targeting 3-dehydroquinate dehydratase in the shikimate pathway of Enterococcus faecalis

2014

Cheung, V.W.; Xue, B.; Hernandez-Valladares, M.; Go, M.K.; Tung, A.; Aguda, A.H.; Robinson, R.C.; Yew, W.S.

PLoS ONE

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Dehydroquinate dehydratase/shikimate dehydrogenases involved in gallate biosynthesis of the aluminum-tolerant tree species Eucalyptus camaldulensis

2020

Tahara, K.; Nishiguchi, M.; Funke, E.; Miyazawa, S.I.; Miyama, T.; Milkowski, C.

Planta

253

3

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