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Ligand 2-deoxy-D-glucose

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Product in Enzyme-catalyzed Reactions (1 result)

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Show Natural Product (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.2.1.112

H2O + a 2-deoxy-alpha-D-glucoside = 2-deoxy-D-glucose + an alcohol

646569

-

Substrate in Enzyme-catalyzed Reactions (67 results)

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Show Substrate (67 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.118

2-deoxy-D-glucose + NAD+ = 2-deoxy-D-glucono-1,5-lactone + NADH + H+

285778, 639110

-

1.1.1.118

2-deoxy-D-glucose + NADP+ = ? + NADPH

639110

-

1.1.1.118

2 entries

1.1.1.119

2-deoxy-D-glucose + NADP+ = 2-deoxy-D-glucono-1,5-lactone + NADPH + H+

285780, 285781

-

1.1.1.121

2-deoxy-D-glucose + NAD+ = 2-deoxy-D-glucono-1,5-lactone + NADH + H+

719111

-

1.1.1.121

2-deoxy-D-glucose + NAD+ = 2-deoxy-D-glucono-delta-lactone + NADH + H+

747502

-

1.1.1.121

2-deoxy-D-glucose + NAD+ = ? + NADH

285791, 285794

-

1.1.1.121

2-deoxy-D-glucose + NAD+ = ? + NADH + H+

697263

-

1.1.1.121

2-deoxy-D-glucose + NADP+ = 2-deoxy-D-glucono-1,5-lactone + NADPH + H+

719111

-

1.1.1.121

5 entries

1.1.1.179

2-deoxy-D-glucose + NADP+ = 2-deoxy-D-glucono-1,5-lactone + NADPH + H+

286124, 286126

-

1.1.1.19

2-deoxyglucose + NADPH + H+ = ?

286143

-

1.1.1.359

2-deoxy-D-glucose + NADP+ + H2O = ?

639110

-

1.1.1.431

2-deoxy-D-glucose + NADPH + H+ = ?

764945

-

1.1.1.47

2-deoxy-D-glucose + NAD(P)+ = ?

656567, 656156

-

1.1.1.47

2-deoxy-D-glucose + NAD+ = 2-deoxy-D-glucono-1,5-lactone + NADH + H+

639101, 668130, 639123, 639124, 639110, 639126, 679613

-

1.1.1.47

2-deoxy-D-glucose + NAD+ = ?

679615

-

1.1.1.47

2-deoxy-D-glucose + NADP+ = 2-deoxy-D-glucono-1,5-lactone + NADPH + H+

639115, 639101, 639110, 639123

-

1.1.1.47

4 entries

1.1.2.11

2-deoxy-D-glucose + phenazine methosulfate = 2-deoxy-3-dehydro-D-glucose + reduced phenazine methosulfate

763936

-

1.1.3.10

2-deoxy-D-glucose + O2 = 2-deoxy-3-dehydro-D-glucose + H2O2

654320

-

1.1.3.10

2-deoxy-D-glucose + O2 = 2-deoxy-3-keto-D-glucose + H2O2

389647, 389646, 389637, 389638

-

1.1.3.10

2-deoxy-D-glucose + O2 = ?

686372

-

1.1.3.4

2-deoxy-D-glucose + O2 + H2O = 2-deoxy-D-glucono-1,5-lactone + H2O2

389806, 389828, 389835, 389805, 389789, 389830, 389796, 654236, 696865

-

1.1.3.4

2-deoxy-D-glucose + O2 = 2-deoxy-D-glucono-1,5-lactone + H2O2

743775

-

1.1.3.4

2-deoxy-D-glucose + O2 = ?

673385

-

1.1.3.4

2-deoxy-d-glucose + O2 = ? + H2O2

763681

-

1.1.3.10

3 entries

1.1.3.4

4 entries

1.1.3.5

2-deoxy-D-glucose + O2 = 2-deoxy-D-glucono-1,5-lactone + H2O2

287636, 287634, 287635

-

1.1.5.2

2-deoxy-D-glucose + 2,6-dichlorophenolindolphenol = 2-deoxy-D-glucono-1,5-lactone + ?

654947

-

1.1.5.2

2-deoxy-D-glucose + 2,6-dichlorophenolindophenol = 2-deoxy-D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol

713001

-

1.1.5.2

2-deoxy-D-glucose + oxidized N-methylphenazonium methyl sulfate = 2-deoxy-D-glucono-1,5-lactone + reduced N-methylphenazonium methyl sulfate

639220

-

1.1.5.2

2-deoxy-D-glucose + phenazine methosulfate = 2-deoxy-D-glucono-1,5-lactone + reduced phenazine methosulfate

746918

-

1.1.5.2

2-deoxy-D-glucose + pyrroloquinoline quinone = 2-deoxy-D-glucono-1,5-lactone + pyrroloquinoline quinol

639213, 639195, 639216

-

1.1.5.2

2-deoxy-D-glucose + ubiquinone = 2-deoxy-D-glucono-1,5-lactone + ubiquinol

724081, 654865, 655101, 655363, 741370

-

1.1.5.9

2-deoxy-D-glucose + 2,6-dichlorophenolindophenol = 2-deoxy-D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol

740363, 739924

-

1.1.5.9

2-deoxy-D-glucose + a quinone = 2-deoxy-D-glucono-1,5-lactone + a quinol

723928

-

1.1.99.13

2-deoxy-D-glucose + 2,6-dichlorophenolindophenol = 3-dehydro-2-deoxy-D-glucose + reduced 2,6-dichlorophenolindophenol

739877, 739878, 741470

-

1.1.99.13

2-deoxy-D-glucose + acceptor = 2-deoxy-3-dehydro-D-glucose + reduced acceptor

389892, 389893

-

1.1.5.2

6 entries

1.1.5.9

2 entries

1.1.99.13

2 entries

1.1.99.18

2-deoxy-D-glucose + 2,6-dichlorophenol indophenol = 2-deoxy-D-glucono-1,5-lactone + reduced 2,6-dichlorophenol indophenol

654237

-

1.1.99.28

2-Deoxy-D-glucose + D-fructose = ?

10911, 10900

-

1.1.99.29

2-deoxy-D-glucose + 1,4-benzoquinone = ?

644547

-

1.1.99.29

2-deoxy-D-glucose + acceptor = ?

686372, 695788

-

1.1.99.29

2-deoxy-D-glucose + ferricenium ion = ?

644547

-

1.1.99.29

3 entries

1.1.99.35

2-deoxy-D-glucose + oxidized 2,6-dichlorophenolindophenol = 2-deoxy-D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol

639209, 639216, 639218

-

1.3.1.20

2-deoxy-D-glucose + NADP+ = 2-deoxy-D-glucono-1,5-lactone + NADPH + H+

286128

-

2.4.1.2

starch + 2-deoxy-D-glucose = ?

488879

-

2.4.1.20

alpha-D-glucose 1-phosphate + 2-deoxy-D-glucose = ?

735893, 637868, 637865, 637855, 637863, 637869, 637859, 637860

-

2.4.1.20

alpha-D-glucose 1-phosphate + 2-deoxy-D-glucose = ? + phosphate

719128

-

2.4.1.20

alpha-D-glucose 1-phosphate + 2-deoxy-D-glucose = phosphate + ?

758413

-

2.4.1.231

2-deoxy-D-glucose + alpha-D-glucose 1-phosphate = ?

674984

-

2.4.1.231

2-deoxy-D-glucose + alpha-D-glucose 1-phosphate = ? + phosphate

674984

-

2.4.1.247

2-deoxy-D-glucose + alpha-D-galactose 1-phosphate = beta-D-galactosyl-(1->4)-2-deoxy-D-glucose + phosphate

722132

-

2.4.1.247

2-deoxy-D-glucose + alpha-D-galactose 1-phosphate = D-galactosyl-beta-1,3-2-deoxy-D-glucose + phosphate

693235

-

2.4.1.20

3 entries

2.4.1.231

2 entries

2.4.1.247

2 entries

2.4.1.25

starch + 2-deoxy-D-glucose = ?

489003

-

2.4.1.281

2-deoxy-D-glucose + alpha-D-mannose 1-phosphate = 4-O-beta-D-mannopyranosyl-2-deoxy-D-glucopyranose + phosphate

725502

-

2.4.1.31

alpha-D-glucose 1-phosphate + 2-deoxy-D-glucose = ?

489045, 719230

-

2.4.1.8

2-deoxy-D-arabino-hexose + beta-D-glucose 1-phosphate = ? + phosphate

719229

-

2.4.1.8

2-deoxy-D-glucose + beta-D-glucose 1-phosphate = 2-deoxy-3-O-alpha-D-glucopyranosyl-D-arabino-hexopyranose + phosphate

756222

-

2.4.1.8

2 entries

2.7.1.1

ATP + 2-deoxy-D-glucose = ADP + 2-deoxy-D-glucose 6-phosphate

640259, 641067, 641068, 672188, 703358, 640220, 660949, 640242, 640209, 641066, 640215, 641061, 640255, 673410, 674266, 739239, 640251, 640230, 640228, 640240, 640243, 640208, 640226, 640206, 640237, 661535, 660912, 685006

-

2.7.1.162

ATP + 2-deoxy-D-glucose = ADP + 2-deoxy-alpha-D-glucose 1-phosphate

723238

-

2.7.1.2

ATP + 2-deoxy-D-glucose = ADP + 2-deoxy-D-glucose 6-phosphate

661779, 641062

-

2.7.1.62

phosphoramidate + 2-deoxy-D-glucose = 2-deoxy-D-glucose 1-phosphate + NH3

636971

-

2.7.1.7

ATP + 2-deoxy-D-glucose = ADP + 2-deoxy-D-glucose 6-phosphate

641894

-

2.7.1.7

ATP + 2-deoxy-D-mannose = ADP + 2-deoxy-D-mannose 6-phosphate

641894, 641892

-

2.7.1.7

CTP + 2-deoxy-D-mannose = CDP + 2-deoxy-D-mannose 6-phosphate

641892

-

2.7.1.7

GTP + 2-deoxy-D-mannose = GDP + 2-deoxy-D-mannose 6-phosphate

641892

-

2.7.1.7

ITP + 2-deoxy-D-mannose = IDP + 2-deoxy-D-mannose 6-phosphate

641892

-

2.7.1.7

5 entries

3.1.3.9

2-deoxy-D-glucose + diphosphate = ?

134941

-

4.1.3.3

2-deoxy-D-glucose + pyruvate = ?

749150

-

5.4.2.5

2-Deoxy-D-glucose + alpha-D-glucose 1-phosphate = D-Glucose + 2-deoxy-D-glucose 6-phosphate

3330

-

Product in Enzyme-catalyzed Reactions (7 results)

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Show Product (7 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.1.3.12

2-Deoxy-D-glucose 6-phosphate + H2O = 2-Deoxy-D-glucose + phosphate

0

-

3.1.3.23

2-Deoxy-D-glucose 6-phosphate + H2O = 2-Deoxy-D-glucose + phosphate

0

-

3.1.3.58

2-Deoxy-D-glucose 6-phosphate + H2O = 2-Deoxy-D-glucose + phosphate

0

-

3.1.3.68

2-Deoxy-D-glucose 6-phosphate + H2O = 2-Deoxy-D-glucose + phosphate

25141, 0

-

3.1.3.9

2-Deoxy-D-glucose 6-phosphate + H2O = 2-Deoxy-D-glucose + phosphate

651331

-

3.2.1.112

H2O + a 2-deoxy-alpha-D-glucoside = 2-deoxy-D-glucose + an alcohol

646569

-

3.2.1.112

H2O + p-nitrophenyl-2-deoxy-alpha-D-glucoside = 2-deoxy-D-glucose + p-nitrophenol

646569

-

3.2.1.112

2 entries

Activator in Enzyme-catalyzed Reactions (6 results)

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Show Activating Compound (6 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.7.11.20

-

665496

-

2.7.11.31

-

761034

-

2.7.11.31

blocks glucose utilization and increases the intracellular AMP concentration, activation is suppressed by compound C

693205

-

2.7.11.31

2 entries

2.7.11.5

-

640600

-

3.2.1.207

activation substrate p-nitrophenyl-alpha-D-glucoside

136904

-

3.2.1.54

0.01 M, relative activity 140%

136620

-

Inhibitor in Enzyme-catalyzed Reactions (19 results)

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Show Inhibitors (19 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.44

-

286835, 286883

-

1.1.3.4

-

389806

-

2.4.1.212

-

722741

-

2.4.1.22

0.4 M, 68% inhibition

488942

-

2.4.1.228

inhibits the Gb3S promoter activity in dose dependent manner

692526

-

2.4.1.31

25-30% inhibition at 20 mM

489045

-

2.7.1.1

-

640257

-

2.7.1.1

2-deoxy-D-glucose is readily phosphorylated by hexokinase II but the product is not further processed by glucose-6-phosphate isomerase and thus accumulates in the cell to inhibit hexokinase II by a negative feedback loop

758656

-

2.7.1.1

competitive, compound also inhibits the parasite growth in vitro at concentrations nontoxic to host cells

739618

-

2.7.1.1

compound is nearly 2fold less toxic Plasmodium falciparum lines overexpressing hexokinase compared with control parasites. Although catalytic activity is higher in in overexpressing cells, they accumulate phospho-2-deoxy-D-glucose at the same rate as control parasites

738229

-

2.7.1.1

low substrate inhibition

660949

-

2.7.1.1

5 entries

2.7.1.199

inhibitor of isoform EIICBAGlc1

736756

-

2.7.1.7

-

641892

-

3.2.1.1

-

393462

-

3.2.1.21

-

702717

-

3.2.1.21

82.7% residual activity of cellobiase produced in the presence of 2-deoxy-D-glucose at 1 mg/ml

703071

-

3.2.1.21

2 entries

3.2.1.58

slight

136647

-

3.2.1.8

-

171653

-

5.1.3.3

competitive

2369

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (27 results)

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Show Turnover Number (27 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.1.1.121

6.9

-

pH 7.4, 50°C

747502

1.1.1.121

6.93

-

-

697263

1.1.1.121

2 entries

1.1.1.179

22

-

-

286126

1.1.1.431

6.8

-

pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH

764945

1.1.5.2

69

-

pH 7.5, 70°C, mutant enzyme Y156A

746918

1.1.5.2

128

-

pH 7.5, 70°C, mutant enzyme Y156K

746918

1.1.5.2

180.6

-

at pH 7.0 and 25°C

741370

1.1.5.2

331

-

pH 7.0, wild-type enzyme

639216

1.1.5.2

1060

-

pH 7.0, mutant enzyme E277K

639216

1.1.5.2

1141

-

pH 7.5, 70°C, wild-type enzyme

746918

1.1.99.35

331

-

wild-type, pH 7.0

639216

1.1.99.35

1063

-

mutant E277K, pH 7.0

639216

2.4.1.20

7.83

-

mutant enzyme Y648V, at pH 6.0 and 37°C

735893

2.4.1.20

11.6

-

-

637865

2.4.1.20

16

-

-

637868

2.4.1.20

18.3

-

-

637869

2.4.1.20

21.5

-

pH 6.0, 37°C

719128

2.4.1.20

21.5

-

wild type enzyme, at pH 6.0 and 37°C

735893

2.4.1.20

119

-

mutant enzyme Y648F, at pH 6.0 and 37°C

735893

1.1.5.2

6 entries

1.1.99.35

2 entries

2.4.1.20

7 entries

2.4.1.231

0.27

-

-

674984

2.4.1.247

2

8

-

693235

2.4.1.247

3.7

-

recombinant enzyme, pH 7.0, 37°C, reverse reaction

722132

2.4.1.247

2 entries

2.4.1.281

11.7

-

apparent value, pH 6.5, 37°C, synthetic reaction, cosubstrate alpha-D-mannose 1-phosphate

725502

2.4.1.31

1

-

pH 6.0, 40°C, reverse reaction

719230

2.4.1.8

39.2

-

pH 8.0, 37°C

756222

2.7.1.1

29

-

wild-type enzyme

672188

2.7.1.1

33.7

-

wild-type, pH 9.0, 36°C

739239

2.7.1.1

2 entries

K_M Value (73 results)

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Show KM Value (73 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.119

39

-

-

285780, 285781

1.1.1.121

1.6

-

-

285794

1.1.1.121

24.3

-

pH 8.0, 37°C

719111

1.1.1.121

300

-

-

697263

1.1.1.121

300

-

pH 7.4, 50°C

747502

1.1.1.121

4 entries

1.1.1.179

54

-

-

286126

1.1.1.19

500

-

-

286143

1.1.1.431

0.058

-

pH 7.0, 25°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH

764945

1.1.1.47

4.2

-

pH 6.5

639115

1.1.3.10

11.3

-

pH 7.3, 22°C, wild-type enzyme

654320

1.1.3.10

11.85

-

100 mM ethanolamine buffer, pH 10.5

686372

1.1.3.10

55

-

oxygen concentration 1.07 mM

389646

1.1.3.10

79

-

pH 7.3, 22°C, mutant enzyme E540K with a C-terminal His6-tag

654320

1.1.3.10

99.3

-

pH 7.3, 22°C, mutant enzyme K312E with a C-terminal His6-tag

654320

1.1.3.4

8.3

-

recombinant enzyme

389835

1.1.3.4

20

-

-

389830

1.1.3.4

28.1

49.8

pH 5.0, 25°C

654236

1.1.5.2

0.000004

-

pH 7.5, 70°C, wild-type enzyme

746918

1.1.5.2

0.00008

-

pH 7.5, 70°C, mutant enzyme Y156A

746918

1.1.5.2

0.00014

-

pH 7.5, 70°C, mutant enzyme Y156K

746918

1.1.5.2

0.5

-

at pH 7.0 and 25°C

741370

1.1.5.2

1.6

-

wild-type enzyme

639213

1.1.5.2

3.5

-

recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C

654865

1.1.5.2

13.6

-

-

639195

1.1.5.2

22

-

pH 8.5, reaction with N-methylphenazonium methyl sulfate as electron acceptor

639220

1.1.5.2

32

-

mutant enzyme H262

639213

1.1.5.2

88

-

pH 7.0, mutant enzyme E277K

639216

1.1.5.2

90

-

pH 7.0, wild-type enzyme

639216

1.1.3.10

5 entries

1.1.3.4

3 entries

1.1.5.2

11 entries

1.1.99.29

0.65

-

0.1 M ethanolamine buffer at pH 9.4

686372

1.1.99.35

88

-

mutant E277K, pH 7.0

639216

1.1.99.35

90

-

wild-type, pH 7.0

639216

2.4.1.20

24.3

-

-

637865

2.4.1.20

47

-

-

637868

2.4.1.20

56.9

-

-

637869

2.4.1.20

60.2

-

pH 6.0, 37°C

719128

2.4.1.20

60.2

-

wild type enzyme, at pH 6.0 and 37°C

735893

2.4.1.20

73

-

-

637855

2.4.1.20

83.1

-

mutant enzyme Y648F, at pH 6.0 and 37°C

735893

2.4.1.20

164

-

mutant enzyme Y648V, at pH 6.0 and 37°C

735893

2.4.1.20

168

-

-

637860

2.4.1.20

250

-

-

637863

2.4.1.247

51

-

recombinant enzyme, pH 7.0, 37°C, reverse reaction

722132

2.4.1.247

290

-

-

693235

1.1.99.35

2 entries

2.4.1.20

10 entries

2.4.1.247

2 entries

2.4.1.281

90.7

-

apparent value, pH 6.5, 37°C, synthetic reaction, cosubstrate alpha-D-mannose 1-phosphate

725502

2.4.1.31

0.7

-

pH 6.0, 40°C, reverse reaction

719230

2.4.1.8

47.8

-

pH 8.0, 37°C

756222

2.7.1.1

0.033

-

hexokinase III, at 30°C, pH 8.1

640240

2.7.1.1

0.1

-

rat brain enzyme, hexokinase I

640220

2.7.1.1

0.125

-

-

640220

2.7.1.1

0.125

-

bovine heart enzyme, hexokinase II

640220

2.7.1.1

0.134

-

at 30°C, pH 8.1

640251

2.7.1.1

0.152

-

HKI, at 25°C, pH 7.4

640259

2.7.1.1

0.18

-

HKI, at 25°C, pH 7.4

640259

2.7.1.1

0.187

-

at 50°C, pH 7.5

640255

2.7.1.1

0.33

-

90°C, pH 6.2

641061

2.7.1.1

0.44

-

pH 7.5, 50°C, ATP as phosphoryl donor

674266

2.7.1.1

0.5

-

hexokinase I, at 37°C, pH 8.1

640237

2.7.1.1

0.56

-

hexokinase Ib, at 37°C, pH 7.2

640230

2.7.1.1

0.613

-

HKII, at 25°C, pH 7.4

640259

2.7.1.1

0.77

-

hexokinase Ia, at 37°C, pH 7.2

640230

2.7.1.1

0.9

-

hexokinase Ia

640228

2.7.1.1

1.16

-

hexokinase Ic, at 37°C, pH 7.2

640230

2.7.1.1

1.33

-

erythrocyte enzyme

640206

2.7.1.1

1.9

-

30°C, pH 7.5, S151A

641068

2.7.1.1

2

-

at 37°C, pH 8.1

640243

2.7.1.1

2

-

hexokinase Ib

640228

2.7.1.1

3.6

-

-

640215

2.7.1.1

5.66

-

wild-type, pH 9.0, 36°C

739239

2.7.1.1

9

-

rat liver enzyme, hexokinase IV

640220

2.7.1.1

18

-

30°C, pH 7.5, wild-type

641068

2.7.1.1

19.2

-

pH 8.0, 30°C

660949

2.7.1.7

10

-

pH 7.5, 25°C

641894

2.7.1.7

15

-

pH 7.5, 25°C

641892

2.7.1.1

25 entries

2.7.1.7

2 entries

K_i Value (6 results)

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Show KI Value (6 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.7.1.1

0.34

-

pH 7.5, temperature not specified in the publication

739618

2.7.1.1

0.5

-

fructose as substrate

640257

2.7.1.1

4

-

fructose as substrate

640257

2.7.1.1

40.7

-

pH 8.0, 30°C, versus MgATP2-

660949

2.7.1.1

4 entries

2.7.1.199

0.0397

-

solubilized isoform EIICBAGlc1, at pH 7.5 and 37°C

736756

2.7.1.7

15

-

pH 7.5, 25°C

641892

IC₅₀ Value (1 result)

top print hide

Show IC50 Value (1 entry)

EC NUMBER

IC50 VALUE

IC50 VALUE MAXIMUM

COMMENTARY

LITERATURE

2.7.1.1

5.75

-

pH 7.5, temperature not specified in the publication

739618

References & Links

Literature References (155)

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Show Reference (155 entries)

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5653182

Purification and specificity of cellobiose phosphorylase from Clostridium thermocellum

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2899-2904

637859

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Cellobiose phosphorylase from Cellovibrio gilvus

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468-472

637860

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Synthetic reaction of Cellvibrio gilvus cellobiose phosphorylase

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40-44

637863

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Purification and properties of cellobiose phosphorylase from Clostridium thermocellum

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212-216

637865

-

Role of non-covalent enzyme-substrate interactions in the reaction catalysed by cellobiose phosphorylase from Cellulomonas uda

2000

Nidetzky, B.; Eis, C.; Albert, M.

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351

649-659

637868

12596851

Characterization of a cellobiose phosphorylase from a hyperthermophilic eubacterium, Thermotoga maritima MSB8

2002

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Biosci. Biotechnol. Biochem.

66

2578-2586

637869

12153715

Kinetic studies of a recombinant cellobiose phosphorylase (CBP) of the Clostridium thermocellum YM4 strain expressed in Escherichia coli

2002

Kim, Y.K.; Kitaoka, M.; Krishnareddy, M.; Mori, Y.; Hayashi, K.

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132

197-203

639101

1629157

Cloning, nucleotide sequences, and enzymatic properties of glucose dehydrogenase isoenzymes from Bacillus megaterium IAM1030

1992

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174

5013-5020

639110

3827812

Glucose dehydrogenase from the thermoacidophilic archaebacterium Sulfolobus solfataricus

1986

Giardina, P.; DeBasia, M.G.; DeRosa, M.; Gambacort, A.; Buonocore, V.

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239

517-522

639115

6415053

Glycerol protection and purification of Bacillus subtilis glucose dehydrogenase

1983

Ramaley, R.F.; Vasantha, N.

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258

12558-12565

639123

-

Reactivation of inactivated D-glucose dehydrogenase of a Bacillus species by pyridine and adenine nucleotides

1979

Yokota, A.; Sasajima, K.; Yoneda, M.

Agric. Biol. Chem.

43

271-278

639124

21162

Location and properties of glucose dehydrogenase in sporulating cells and spores of Bacillus subtilis

1977

Fujita, Y.; Ramaley, R.; Freese, E.

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282-293

639126

2530

D-Glucose dehydrogenase from Bacillus megaterium M1286: purification, properties and structure

1975

Pauly, H.E.; Pfleiderer, G.

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356

1613-1623

639195

-

The in vivo and in vitro substrate specificity of quinoprotein glucose dehydrogenase of Acinetobacter calcoaceticus LMD79.41

1987

Dokter, P.; Pronk, J.T.; van Schie, B.J.; van Dijken, J.P.; Duine, J.A.

FEMS Microbiol. Lett.

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195-200

639209

9753475

On the mechanism and specificity of soluble, quinoprotein glucose dehydrogenase in the oxidation of aldose sugars

1998

Olsthoorn, A.J.; Duine, J.A.

Biochemistry

37

13854-13861

639213

-

Characterization of the membrane quinoprotein glucose dehydrogenase from Escherichia coli and characterization of a site-directed mutant in which histidine-262 has been changed to tyrosine

1999

Cozier, G.E.; Salleh, R.A.; Anthony, C.

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340

639-647

639216

10544015

Construction and characterization of mutant water-soluble PQQ glucose dehydrogenases with altered K(m) values--site-directed mutagenesis studies on the putative active site

1999

Igarashi, S.; Ohtera, T.; Yoshida, H.; Witarto, A.B.; Sode, K.

Biochem. Biophys. Res. Commun.

264

820-824

639218

10771051

Increasing the thermal stability of the water-soluble pyrroloquinoline quinone glucose dehydrogenase by single amino acid replacement

2000

Sode, K.; Ootera, T.; Shirahane, M.; Witarto, A.B.; Igarashi, S.; Yoshida, H.

Enzyme Microb. Technol.

26

491-496

639220

10518528

Active-site structure of the soluble quinoprotein glucose dehydrogenase complexed with methylhydrazine: A covalent cofactor-inhibitor complex

1999

Oubrie, A.; Rozeboom, H.J.; Dijkstra, B.W.

Proc. Natl. Acad. Sci. USA

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11787-11791

640206

-

Hexokinase from rabbit red blood cells

1982

Fornaini, G.; Dacha, M.; Magnani, M.; Stocchi, V.

Methods Enzymol.

90

3-10

640208

-

Hexokinases from Drosophila melanogaster

1982

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Methods Enzymol.

90

16-21

640209

-

Hexokinase from Ascaris suum muscle

1982

Supowit, S.C.; Harris, B.G.

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90

21-25

640215

6315879

Retinal hexokinase: kinetic properties and the effect of cyclic 3,5-adenosine monophosphate

1983

Liu, S.S.; Witkovsky, P.; Yang, C.Y.

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41

1694-1701

640220

1889417

Competitive inhibition of liver glucokinase by its regulatory protein

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200

545-551

640226

6768723

Multiple forms of Drosophila hexokinase. Purification, biochemical and immunological characterization

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Moser, D.; Johnson, L.; Lee, C.Y.

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255

4673-4679

640228

7263629

Rabbit red blood cell hexokinase. Evidence for two distinct forms, and their purification and characterization from reticulocytes

1981

Stocchi, V.; Magnani, M.; Canestrari, F.; Dacha, M.; Fornaini, G.

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256

7856-7862

640230

7061426

Multiple forms of human red blood cell hexokinase. Preparation, characterization, and age dependence

1982

Stocchi, V.; Magnani, M.; Canestrari, F.; Dacha, M.; Fornaini, G.

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2357-2364

640237

3341751

Purification, properties, and evidence for two subtypes of human placenta hexokinase type I

1988

Magnani, M.; Stocchi, V.; Serafini, G.; Chiarantini, L.; Fornaini, G.

Arch. Biochem. Biophys.

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388-399

640240

6639059

Pig red blood cell hexokinase: Evidence for the presence of hexokinase types II and III, and their purification and characterization

1983

Stocchi, V.; Magnani, M.; Novelli, G.; Dacha, M.; Fornaini, G.

Arch. Biochem. Biophys.

226

365-376

640242

8031843

Characterization and regulatory properties of a single hexokinase from the citric acid accumulating fungus Aspergillus niger

1994

Steinb÷ck, F.; Choojun, S.; Held, I.; Roehr, M.; Kubicek, C.P.

Biochim. Biophys. Acta

1200

215-223

640243

7114848

Solubilization, purification, and properties of rabbit brain hexokinase

1982

Magnani, M.; Serafini, G.; Stocchi, V.; Bossu, M.; Dacha, M.

Arch. Biochem. Biophys.

216

449-454

640251

9440232

Purification and properties of buffalo (Bubalus bubalis) erythrocyte hexokinase

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Comp. Biochem. Physiol. B

118

395-401

640255

12626506

The hexokinase of the hyperthermophile Thermoproteus tenax. ATP-dependent hexokinases and ADP-dependent glucokinases, two alternatives for glucose phosphorylation in Archaea

2003

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18744-18753

640257

8549830

Schizosaccharomyces pombe possesses an unusual and a conventional hexokinase: Biochemical and molecular characterization of both hexokinases

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FEBS Lett.

378

185-189

640259

11295420

Kinetic characterization of hexokinase isoenzymes from glioma cells: Implications for FDG imaging of human brain tumors

2001

Muzi, M.; Freeman, S.D.; Burrows, R.C.; Wiseman, R.W.; Link, J.M.; Krohn, K.A.; Graham, M.M.; Spence, A.M.

Nucl. Med. Biol.

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107-116

640600

6756316

The reversible phosphorylation of isocitrate dehydrogenase of Salmonella typhimurium

1982

Wang, J.Y.J.; Koshland, D.E.

Arch. Biochem. Biophys.

218

59-67

641061

12374829

The first archaeal ATP-dependent glucokinase, from the hyperthermophilic crenarchaeon Aeropyrum pernix, represents a monomeric, extremely thermophilic ROK glucokinase with broad hexose specificity

2002

Hansen, T.; Reichstein, B.; Schmid, R.; Schonheit, P.

J. Bacteriol.

184

5955-5965

641062

12761185

Cloning, expression, and characterization of the first archaeal ATP-dependent glucokinase from aerobic hyperthermophilic archaeon Aeropyrum pernix

2003

Sakuraba, H.; Mitani, Y.; Goda, S.; Kawarabayasi, Y.; Ohshima, T.

J. Biochem.

133

219-224

641066

12383517

Cloning and characterization of glucokinase from a methylotrophic yeast Hansenula polymorpha: different effects on glucose repression in H. polymorpha and Saccharomyces cerevisiae

2002

Laht, S.; Karp, H.; Kotka, P.; Jarviste, A.; Alamae, T.

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296

195-203

641067

8679719

Kinetics and specificity of human B-cell glucokinase: relevance to hexose-induced insulin release

1996

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Biochim. Biophys. Acta

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73-78

641068

7730377

Human beta-cell glucokinase. Dual role of Ser-151 in catalysis and hexose affinity

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641892

4635821

Identification and properties of an inducible mannokinase from Streptomyces violaceoruber

1972

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Biochim. Biophys. Acta

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641894

4557975

Purification and properties of the mannokinase from Escherichia coli

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Arch. Biochem. Biophys.

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644547

11511865

Screening of basidiomycete fungi for the quinone-dependent sugar C-2/C-3 oxidoreductase, pyranose dehydrogenase, and properties of the enzyme from Macrolepiota rhacodes

2001

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Indentification of a glycosidase activity with apparent specificity for 2-deoxy-D-glucose in glycosidic linkage

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12965222

Identification and characterisation of a new human glucose-6-phosphatase isoform

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159-164

654236

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Extracellular glucose oxidase of Penicillium funiculosum 46.1

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Appl. Biochem. Microbiol.

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368-374

654237

14714477

Isolation and characterization of a cellobiose dehydrogenase formed by a nonsporulating mycelial fungus INBI 2-26(-)

2003

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15660220

Engineering of pyranose 2-oxidase from Peniophora gigantea towards improved thermostability and catalytic efficiency

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67

654-663

654865

12686133

The metal ion in the active site of the membrane glucose dehydrogenase of Escherichia coli

2003

James, P.L.; Anthony, C.

Biochim. Biophys. Acta

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200-205

654947

15113562

Engineering PQQ glucose dehydrogenase with improved substrate specificity. Site-directed mutagenesis studies on the active center of PQQ glucose dehydrogenase

2004

Igarashi, S.; Hirokawa, T.; Sode, K.

Biomol. Eng.

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81-89

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Links to other databases for 2-deoxy-D-glucose

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