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Ligand 2-keto-3-deoxy phosphogluconate

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

degradation of sugar acids, Entner Doudoroff pathway

KEGG

Carbon metabolism, Microbial metabolism in diverse environments, Pentose phosphate pathway

MetaCyc

3,6-anhydro-alpha-L-galactopyranose degradation, 4-deoxy-L-threo-hex-4-enopyranuronate degradation, alginate degradation, D-fructuronate degradation, D-galacturonate degradation I, D-glucosaminate degradation, Entner-Doudoroff pathway III (semi-phosphorylative), Entner-Doudoroff shunt more

Show all BRENDA pathways known for 2-keto-3-deoxy phosphogluconate

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (5 results)

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Show Natural Substrate (5 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

4.1.2.14

2-dehydro-3-deoxy-6-phospho-D-gluconate = pyruvate + D-glyceraldehyde 3-phosphate

695041, 748258, 748387, 748531, 748105, 747152

-

4.1.2.14

2-dehydro-3-deoxy-D-gluconate 6-phosphate = pyruvate + D-glyceraldehyde 3-phosphate

691381, 690279, 650823

-

4.1.2.14

2 entries

4.1.2.21

2-dehydro-3-deoxy-6-phospho-D-gluconate = pyruvate + D-glyceraldehyde 3-phosphate

695041

-

4.1.2.55

2-dehydro-3-deoxy-6-phospho-D-gluconate = pyruvate + D-glyceraldehyde 3-phosphate

747152

6g3z, 3D-view

4.1.2.55

2-dehydro-3-deoxy-D-gluconate 6-phosphate = pyruvate + D-glyceraldehyde 3-phosphate

719488, 657872

6g3z, 3D-view

4.1.2.55

2 entries

In Vivo Product in Enzyme-catalyzed Reactions (10 results)

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Show Natural Product (10 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.7.1.11

ATP + 2-dehydro-3-deoxy-D-gluconate = ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate

-

-

2.7.1.178

ATP + 2-dehydro-3-deoxy-D-gluconate = ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate

-

-

2.7.1.178

ATP + 2-dehydro-3-deoxy-D-gluconate = ADP + 6-phospho-2-dehydro-3-deoxy-D-gluconate

-

-

2.7.1.45

ATP + 2-dehydro-3-deoxy-D-gluconate = ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate

-

-

2.7.1.45

ATP + 2-dehydro-3-deoxy-D-gluconate = ADP + 6-phospho-2-dehydro-3-deoxy-D-gluconate

-

-

2.7.1.178

2 entries

2.7.1.45

2 entries

4.1.2.14

pyruvate + D-glyceraldehyde 3-phosphate = 2-dehydro-3-deoxy-6-phospho-D-gluconate

-

-

4.2.1.12

6-phospho-D-gluconate = 2-dehydro-3-deoxy-6-phospho-D-gluconate + H2O

-

-

4.2.1.12

6-phospho-D-gluconate = 6-phospho-2-dehydro-3-deoxy-D-gluconate + H2O

-

-

4.3.1.29

2-amino-2-deoxy-D-gluconate 6-phosphate = 2-dehydro-3-deoxy-6-phospho-D-gluconate + NH3

-

-

4.3.1.29

6-phospho-D-glucosaminate = 2-dehydro-3-deoxy-6-phospho-D-gluconate + NH3

-

-

4.2.1.12

2 entries

4.3.1.29

2 entries

Substrate in Enzyme-catalyzed Reactions (8 results)

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Show Substrate (8 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

4.1.2.14

2-dehydro-3-deoxy-6-phospho-D-gluconate = pyruvate + D-glyceraldehyde 3-phosphate

726975, 695041, 682518, 748258, 748387, 748531, 748105, 747152

-

4.1.2.14

2-dehydro-3-deoxy-D-gluconate 6-phosphate = pyruvate + D-glyceraldehyde 3-phosphate

4981, 4982, 664300, 678625, 682736, 649102, 650823, 691381, 4965, 4966, 4968, 4969, 4970, 4972, 4973, 4975, 4976, 4977, 4984, 4983, 704329, 4978, 4985, 701559, 4967, 4971, 4974, 4980, 586786, 690279, 4979, 649204, 653666

-

4.1.2.14

2 entries

4.1.2.20

2-dehydro-3-deoxy-6-phospho-D-gluconate = pyruvate + glyceraldehyde-3-phosphate

704334

-

4.1.2.21

2-dehydro-3-deoxy-6-phospho-D-gluconate = pyruvate + D-glyceraldehyde 3-phosphate

695041

-

4.1.2.51

2-dehydro-3-deoxy-D-gluconate 6-phosphate = pyruvate + D-glyceraldehyde 3-phosphate

704334

-

4.1.2.55

2-dehydro-3-deoxy-6-phospho-D-gluconate = pyruvate + D-glyceraldehyde 3-phosphate

747152

6g3z, 3D-view

4.1.2.55

2-dehydro-3-deoxy-D-gluconate 6-phosphate = pyruvate + D-glyceraldehyde 3-phosphate

719488, 657872

6g3z, 3D-view

4.1.2.55

2 entries

4.1.3.42

2-dehydro-3-deoxy-6-phospho-D-gluconate = ?

4984

-

Product in Enzyme-catalyzed Reactions (18 results)

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Show Product (18 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.7.1.11

ATP + 2-dehydro-3-deoxy-D-gluconate = ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate

-

-

2.7.1.178

ATP + 2-dehydro-3-deoxy-D-gluconate = ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate

-

-

2.7.1.178

ATP + 2-dehydro-3-deoxy-D-gluconate = ADP + 6-phospho-2-dehydro-3-deoxy-D-gluconate

-

-

2.7.1.45

ATP + 2-dehydro-3-deoxy-D-gluconate = ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate

-

-

2.7.1.45

ATP + 2-dehydro-3-deoxy-D-gluconate = ADP + 6-phospho-2-dehydro-3-deoxy-D-gluconate

, 636960

-

2.7.1.45

CTP + 2-dehydro-3-deoxy-D-gluconate = CDP + 6-phospho-2-dehydro-3-deoxy-D-gluconate

-

-

2.7.1.45

GTP + 2-dehydro-3-deoxy-D-gluconate = GDP + 6-phospho-2-dehydro-3-deoxy-D-gluconate

-

-

2.7.1.45

ITP + 2-dehydro-3-deoxy-D-gluconate = IDP + 6-phospho-2-dehydro-3-deoxy-D-gluconate

-

-

2.7.1.45

TTP + 2-dehydro-3-deoxy-D-gluconate = TDP + 6-phospho-2-dehydro-3-deoxy-D-gluconate

-

-

2.7.1.45

UTP + 2-dehydro-3-deoxy-D-gluconate = UDP + 6-phospho-2-dehydro-3-deoxy-D-gluconate

-

-

2.7.1.178

2 entries

2.7.1.45

7 entries

2.7.1.58

ATP + 2-dehydro-3-deoxy-D-gluconate = ADP + 2-dehydro-3-deoxy-6-phospho-D-gluconate

-

-

4.1.2.14

pyruvate + D-glyceraldehyde 3-phosphate = 2-dehydro-3-deoxy-6-phospho-D-gluconate

-

-

4.1.2.14

Pyruvate + D-glyceraldehyde 3-phosphate = 6-Phospho-2-dehydro-3-deoxy-D-gluconate

, 4967

-

4.1.2.14

2 entries

4.1.2.55

pyruvate + D-glyceraldehyde 3-phosphate = 2-dehydro-3-deoxy-D-gluconate 6-phosphate

-

6g3z, 3D-view

4.2.1.12

6-phospho-D-gluconate = 2-dehydro-3-deoxy-6-phospho-D-gluconate + H2O

-

-

4.2.1.12

6-phospho-D-gluconate = 6-phospho-2-dehydro-3-deoxy-D-gluconate + H2O

4981, 33654, 33657, 33658, 33653, 33656, 33648, 33651, 33655, , 33650, 33652, 33649, 4980, 33645, 33647

-

4.3.1.29

2-amino-2-deoxy-D-gluconate 6-phosphate = 2-dehydro-3-deoxy-6-phospho-D-gluconate + NH3

-

-

4.3.1.29

6-phospho-D-glucosaminate = 2-dehydro-3-deoxy-6-phospho-D-gluconate + NH3

-

-

4.2.1.12

2 entries

4.3.1.29

2 entries

Activator in Enzyme-catalyzed Reactions (2 results)

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Show Activating Compound (2 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.7.7.27

activation

643144, 643135

-

2.7.7.27

fructose 6-phosphate and pyruvate analog, less effective than fructose bisphosphate

643144

-

2.7.7.27

2 entries

3D Structure of Enzyme-Ligand-Complex (PDB) (1 result)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (1 entry)

EC NUMBER

ENZYME 3D STRUCTURE

4.1.2.55

6g3z, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (31 results)

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Show Turnover Number (31 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

4.1.2.14

0.00029

-

mutant enzyme S184D, in 100 mM HEPES, pH 7.5

682736

4.1.2.14

0.0026

-

mutant enzyme S184L, in 100 mM HEPES, pH 7.5

682736

4.1.2.14

0.0063

-

wild type enzyme, in 100 mM HEPES, pH 7.5

682736

4.1.2.14

0.02

-

mutant enzyme T161V, in 20 mM HEPES, pH 7.5, at 23°C

678625

4.1.2.14

0.0333

-

-

586786

4.1.2.14

2

-

pH 7.5, 40°C

586786

4.1.2.14

2.5

-

KA3 variant, pH 7.5, 25°C

650823

4.1.2.14

3.2

-

mutant enzyme S184D, in 100 mM HEPES, pH 7.5

682736

4.1.2.14

3.9

-

pH 7.5, 70°C

586786

4.1.2.14

7.8

-

KA3-L1 variant, pH 7.5, 25°C

650823

4.1.2.14

9.8

-

mutant enzyme T161A, in 20 mM HEPES, pH 7.5, at 23°C

678625

4.1.2.14

11.2

-

KA3-L2 variant, pH 7.5, 25°C

650823

4.1.2.14

27

-

mutant T161S, pH 7.5, 25°C

726975

4.1.2.14

31

-

mutant T161S/S184F, pH 7.5, 25°C

726975

4.1.2.14

40

-

mutant S184F, pH 7.5, 25°C

726975

4.1.2.14

41

-

mutant T161S/S18L, pH 7.5, 25°C

726975

4.1.2.14

52

-

KA2 variant, pH 7.5, 25°C

650823

4.1.2.14

74

-

mutant enzyme S184L, in 100 mM HEPES, pH 7.5

682736

4.1.2.14

80

-

wild type enzyme, in 20 mM HEPES, pH 7.5, at 23°C

678625

4.1.2.14

80

-

-

682518

4.1.2.14

83

-

wild-type, pH 7.5, 25°C

726975

4.1.2.14

83

-

wild type enzyme, in 100 mM HEPES, pH 7.5

682736

4.1.2.14

93

-

KA1-2 variant, pH 7.5, 25°C

650823

4.1.2.14

97

-

mutant enzyme S184A, in 100 mM HEPES, pH 7.5

682736

4.1.2.14

108

-

KA1-3 variant, pH 7.5, 25°C

650823

4.1.2.14

284

-

wild-type enzyme, pH 7.5, 25°C

650823

4.1.2.14

533

-

-

4965

4.1.2.14

27 entries

4.1.2.20

0.34

-

at 60°C in 50 mM sodium phosphate buffer (pH 6.2)

704334

4.1.2.51

0.34

-

pH 6.2, 60°C, enzyme purified from Picrophilus torridus

704334

4.1.2.51

0.36

-

pH 6.2, 60°C, recombinant enzyme

704334

4.1.2.51

2 entries

4.1.2.55

61.9

-

60°C, pH not specified in the publication

719488

K_M Value (37 results)

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Show KM Value (37 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

4.1.2.14

0.006

-

KA3-L1 variant, pH 7.5, 25°C

650823

4.1.2.14

0.03

-

KA2 variant, pH 7.5, 25°C

650823

4.1.2.14

0.03

-

KA3 variant, pH 7.5, 25°C

650823

4.1.2.14

0.038

-

-

4984

4.1.2.14

0.05

-

mutant T161S, pH 7.5, 25°C

726975

4.1.2.14

0.053

-

-

4979

4.1.2.14

0.06

-

pH 7.6, 25°C

664300

4.1.2.14

0.073

-

-

4972

4.1.2.14

0.1

-

wild-type, pH 7.5, 25°C

726975

4.1.2.14

0.1

-

wild type enzyme, in 100 mM HEPES, pH 7.5

682736

4.1.2.14

0.1

-

wild type enzyme, in 20 mM HEPES, pH 7.5, at 23°C

678625

4.1.2.14

0.1

-

-

682518

4.1.2.14

0.1

-

-

4971

4.1.2.14

0.11

-

-

4965

4.1.2.14

0.15

-

KA1-2 variant, pH 7.5, 25°C

650823

4.1.2.14

0.16

-

mutant enzyme S184A, in 100 mM HEPES, pH 7.5

682736

4.1.2.14

0.2

-

-

586786

4.1.2.14

0.2

-

mutant enzyme T161A, in 20 mM HEPES, pH 7.5, at 23°C

678625

4.1.2.14

0.21

-

KA1-3 variant, pH 7.5, 25°C

650823

4.1.2.14

0.22

-

pH 7.5, 40°C

586786

4.1.2.14

0.24

-

mutant T161S/S18L, pH 7.5, 25°C

726975

4.1.2.14

0.25

-

-

4978

4.1.2.14

0.29

-

at pH 7.0 and 42°C

748105

4.1.2.14

0.3

-

mutant enzyme T161V, in 20 mM HEPES, pH 7.5, at 23°C

678625

4.1.2.14

0.35

-

mutant enzyme S184L, in 100 mM HEPES, pH 7.5

682736

4.1.2.14

0.35

-

wild-type enzyme, pH 7.5, 25°C

650823

4.1.2.14

0.46

-

KA3-L2 variant, pH 7.5, 25°C

650823

4.1.2.14

0.69

-

mutant T161S/S184F, pH 7.5, 25°C

726975

4.1.2.14

0.9

-

pH 7.5, 70°C

586786

4.1.2.14

0.95

-

mutant enzyme S184L, in 100 mM HEPES, pH 7.5

682736

4.1.2.14

1.2

-

mutant enzyme S184D, in 100 mM HEPES, pH 7.5

682736

4.1.2.14

1.7

-

mutant S184F, pH 7.5, 25°C

726975

4.1.2.14

10.5

-

-

4983

4.1.2.14

33 entries

4.1.2.20

8

-

at 60°C in 50 mM sodium phosphate buffer (pH 6.2)

704334

4.1.2.51

2.5

-

pH 6.2, 60°C, recombinant enzyme

704334

4.1.2.51

8

-

pH 6.2, 60°C, enzyme purified from Picrophilus torridus

704334

4.1.2.51

2 entries

4.1.2.55

0.1

-

60°C, pH not specified in the publication

719488

References & Links

Literature References (60)

top print hide

Show Reference (60 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

4965

14245411

Crystallization and characteristics of 2-keto-3-deoxy-6-phosphogluconic aldolase

1964

Meloche, H.P.; Wood, W.A.

J. Biol. Chem.

239

3515-3518

4966

-

2-Keto-3-deoxy-6-phosphogluconic aldolase (crystalline)

1966

Meloche, H.P.; Ingram, J.M.; Wood, W.A.

Methods Enzymol.

9

520-524

4967

6049459

Bromopyruvate inactivation of 2-keto-3-deoxy-6-phosphogluconic aldolase. I. Kinetic evidence for active site specificity

1967

Meloche, H.P.

Biochemistry

6

2273-2280

4968

5555561

Structure of 2-keto-3-deoxy-6-phosphogluconate aldolase. I. Physical evidence for a three-subunit molecule

1971

Hammerstedt, R.H.; Möhler, H.; Decker, K.A.; Wood, W.A.

J. Biol. Chem.

246

2069-2074

4969

5555562

Structure of 2-keto-3-deoxy-6-phosphogluconate aldolase. II. Chemical evidence for a three-subunit molecule

1971

Robertson, D.C.; Hammerstedt, R.H.; Wood, W.A.

J. Biol. Chem.

246

2075-2083

4970

4690603

Confirmation of a trimeric subunit arrangement for 2-keto-3-deoxy-6-phosphogluconic aldolase using X-ray crystallographic methods

1973

Vandlen, R.L.; Ersfeld, D.L.; Tulinsky, A.; Wood, W.A.

J. Biol. Chem.

248

2251-2253

4971

-

2-Keto-3-deoxy-6-phosphogluconic and related aldolases

1972

Wood, W.A.

The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )

7

281-302

4972

-

2-Keto-3-deoxy-6-phosphogluconic aldolase

1975

Hammerstedt, R.H.; Möhler, H.; Decker, K.A.; Ehrsfeld, D.; Wood, W.A.

Methods Enzymol.

42C

258-264

4973

1158885

The stereochemistry at carbon 3 of pyruvate lyase condensation products. 2-Keto-3-deoxygluconate-6-phosphate aldolase

1975

Meloche, H.P.; Mehler, L.; Wurster, J.M.

J. Biol. Chem.

250

6870-6874

4974

1158886

The stereochemistry, at carbon 3 of pyruvate lyase condensation products. 2-Keto-3-deoxygluconate-6-phosphate and 2-keto-3-deoxygalactonate-6-phosphate aldolase of Pseudomonas saccharophila

1975

Meloche, H.P.; Monti, C.T.

J. Biol. Chem.

250

6875-6879

4975

447683

Interaction of the chiral pyruvate analog, 2-keto-3-bromobutyrate with pyruvate lyases. 2-Keto-3-deoxygluconate-6-phosphate aldolase of Pseudomonas putida

1979

Monti, C.T.; Waterbor, J.W.; Meloche, H.P.

J. Biol. Chem.

254

5862-5865

4976

6988426

Complete primary structure of 2-keto-3-deoxy-6-phosphogluconate aldolase

1980

Suzuki, N.; Wood, W.A.

J. Biol. Chem.

255

3427-3435

4977

7161801

Structure of 2-keto-3-deoxy-6-phosphogluconate aldolase at 2.8 A resolution

1982

Mavridis, I.M.; Hatada, M.H.; Tulinski, A.; Lebioda, L.

J. Mol. Biol.

162

419-444

4978

6326622

Use of differential dye-ligand chromatography with affinity elution for enzyme purification: 2-keto-3-deoxy-6-phosphogluconate aldolase from Zymomonas mobilis

1984

Scopes, R.K.

Anal. Biochem.

136

525-529

4979

-

Investigation of 2-oxo-3-deoxy-5-phosphogluconate aldolase from Zymomonas mobilis as a catalyst in organic synthesis

1995

Knappmann, B.R.; Steigel, A.; Kula, M.R.

Biotechnol. Appl. Biochem.

22

107-120

4980

16346876

Glucose catabolism in strains of acidophilic, heterotrophic bacteria

1985

Shuttleworth, K.L.; Unz, R.F.; Wichlacz, P.L.

Appl. Environ. Microbiol.

50

573-579

4981

-

Metabolism of glucose and gluconate in fast- and slow-growing rhizobia

1987

Chakrabarti, S.K.; Mishra, A.K.; Chakrabartty, P.K.

Phytochemistry

26

85-87

4982

-

Differential dye-ligand chromatography as a general purification protocol for 2-keto-3-deoxy-6-phosphogluconate aldolases

1995

Shelton, M.C.; Toone, E.J.

Tetrahedron

6

207-211

4983

8037447

The Entner-Doudoroff pathway in Helicobacter pylori

1994

Mendz, G.L.; Hazell, S.L.; Burns, B.P.

Arch. Biochem. Biophys.

312

349-356

4984

8166720

Purification and characterization of 2-keto-3-deoxy-6-phosphogluconate aldolase from Azotobacter vinelandii: evidence that the enzyme is bifunctional towards 2-keto-4-hydroxyglutarate cleavage

1994

Taha, T.S.; Deits, T.L.

Biochem. Biophys. Res. Commun.

200

459-466

4985

1809834

Cloning, characterization and expression of the Zymomonas mobilis eda gene that encodes 2-keto-3-deoxy-6-phosphogluconate aldolase of the Entner-Doudoroff pathway

1991

Conway, T.; Fliege, R.; Jones-Kilpatrick, D.; Liu, J.; Barnell, W.O.; Egan, S.E.

Mol. Microbiol.

5

2901-2911

33645

-

Metabolism of non-motile obligatory methylotrophic bacteria

1986

Trotsenko, Y.A.; Doronina, N.V.; Govorukhina, N.I.

FEMS Microbiol. Lett.

33

293-297

33647

16346836

Carbohydrate catabolism in Azospirillum amazonense

1985

Martinez-Drets, G.; Fabiano, E.; Cardona, A.

Appl. Environ. Microbiol.

50

183-185

33648

3922954

Cloning of genes specifying carbohydrate catabolism in Pseudomonas aeruginosa and Pseudomonas putida

1985

Cuskey, S.M.; Wolff, J.A.; Phibbs, P.V.; Olsen, R.H.

J. Bacteriol.

162

865-871

33649

-

Gluconate catabolism in cowpea rhizobia: evidence for a ketogluconate pathway

1984

Stowers, M.D.; Elkan, G.H.

Arch. Microbiol.

137

3-9

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Links to other databases for 2-keto-3-deoxy phosphogluconate

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