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Ligand D-mannose 6-phosphate

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

d-mannose degradation

KEGG

Amino sugar and nucleotide sugar metabolism, Biosynthesis of cofactors, Biosynthesis of nucleotide sugars, Biosynthesis of secondary metabolites, Fructose and mannose metabolism, Lysosome, O-Antigen nucleotide sugar biosynthesis, Phosphotransferase system (PTS) more

Show all BRENDA pathways known for D-mannose 6-phosphate

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (8 results)

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Show Natural Substrate (8 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.224

D-mannose 6-phosphate + NADPH = ?

348008, 94715

-

1.1.1.224

D-mannose 6-phosphate + NADPH = D-mannitol 1-phosphate + NADP+

656972

-

1.1.1.224

2 entries

2.5.1.132

phosphoenolpyruvate + D-mannose 6-phosphate + H2O = 3-deoxy-D-glycero-D-galacto-nononate 9-phosphate + phosphate

737585, 671868, 685801, 736395, 738039

-

2.7.1.61

D-glucose + D-mannose 6-phosphate = D-glucose 6-phosphate + D-mannose

636972, 636973

-

5.3.1.8

D-Mannose 6-phosphate = ?

2813, 2624

-

5.3.1.8

D-Mannose 6-phosphate = D-Fructose 6-phosphate

727158, 728469, 702663, 706204, 701879, 701812, 702817, 702869, 701472, 701797, 705568, 726723, 728283

-

5.4.2.8

D-mannose 6-phosphate = alpha-D-mannose 1-phosphate

680450

-

5.4.2.8

D-mannose 6-phosphate = D-mannose 1-phosphate

3352, 3358, 3356, 2821

-

5.3.1.8

2 entries

5.4.2.8

2 entries

In Vivo Product in Enzyme-catalyzed Reactions (7 results)

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Show Natural Product (7 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.224

D-mannitol 1-phosphate + NADP+ = D-mannose 6-phosphate + NADPH + H+

0

-

2.7.1.1

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

0

-

2.7.1.63

(phosphate)n + mannose = (phosphate)n-1 + mannose 6-phosphate

0

-

2.7.1.7

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

0

-

5.3.1.8

D-fructose 6-phosphate = D-mannose 6-phosphate

652215

-

5.4.2.2

alpha-D-mannose 1-phosphate = D-mannose 6-phosphate

0

-

5.4.2.8

alpha-D-mannose 1-phosphate = D-mannose 6-phosphate

0

-

Substrate in Enzyme-catalyzed Reactions (27 results)

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Show Substrate (27 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.200

D-mannose 6-phosphate + NADPH = ?

347839

-

1.1.1.224

D-mannose 6-phosphate + NADPH + H+ = D-mannitol 1-phosphate + NADP+

700701

-

1.1.1.224

D-mannose 6-phosphate + NADPH = ?

348008, 94715

-

1.1.1.224

D-mannose 6-phosphate + NADPH = D-mannitol 1-phosphate + NADP+

348003, 348005, 656972, 94715, 348002, 348006, 348007, 348008

-

1.1.98.2

D-mannose 6-phosphate + oxidized coenzyme F420 = 6-phospho-D-mannono-1,5-lactone + reduced coenzyme F420

739925

-

1.1.98.2

D-mannose-6-phosphate + oxidized coenzyme F420 = ?

698547

-

2.4.1.15

UDP-alpha-D-glucose + D-mannose 6-phosphate = UDP + ?

727099

-

2.4.1.15

UDP-alpha-D-glucose + D-mannose 6-phosphate = UDP + alpha,alpha-1,1-trehalose 6-phosphate

702423

-

1.1.1.224

3 entries

1.1.98.2

2 entries

2.4.1.15

2 entries

2.4.1.216

mannose 6-phosphate + beta-D-glucose 1-phosphate = alpha-D-Glc-(1->1)-alpha-D-Man6P + phosphate

758932

-

2.5.1.132

phosphoenolpyruvate + D-mannose 6-phosphate + H2O = 3-deoxy-D-glycero-D-galacto-nononate 9-phosphate + phosphate

737585, 671868, 685801, 736395, 738039, 738566

-

2.5.1.57

D-mannose 6-phosphate + ? = ?

671716

-

2.5.1.57

D-mannose 6-phosphate + phosphoenolpyruvate + H2O = 2-keto-3-deoxy-D-glycero-D-galacto-nonulosonic acid 9-phosphate + phosphate

671868, 685801

-

2.5.1.57

D-mannose 6-phosphate + phosphoenolpyruvate + H2O = 2-keto-3-deoxy-D-glycero-D-galactononoic acid 9-phosphate + phosphate

637821

-

2.5.1.57

3 entries

2.7.1.61

D-glucose + D-mannose 6-phosphate = D-glucose 6-phosphate + D-mannose

636972, 636973

-

3.1.3.10

D-mannose 6-phosphate + H2O = D-mannose + phosphate

704914

-

3.1.3.12

D-mannose 6-phosphate + H2O = D-mannose + phosphate

134586

-

3.1.3.2

D-mannose 6-phosphate + H2O = D-mannose + phosphate

134783

-

3.1.3.23

D-mannose 6-phosphate + H2O = D-mannose + phosphate

94723, 94727, 730458, 730667, 94722

-

3.1.3.25

D-mannose 6-phosphate + H2O = ?

114235

-

3.1.3.58

D-mannose 6-phosphate + H2O = D-mannose + phosphate

655643, 646416

-

3.1.3.9

D-mannose 6-phosphate + H2O = D-mannose + phosphate

649729

-

5.3.1.8

D-Mannose 6-phosphate = ?

2813, 2624

-

5.3.1.8

D-Mannose 6-phosphate = D-Fructose 6-phosphate

2624, 2818, 2829, 3354, 727158, 728469, 661902, 702663, 2817, 2821, 2826, 2828, 2812, 2806, 2816, 2819, 661119, 2813, 693149, 2814, 2823, 2824, 692361, 706204, 2820, 2822, 2825, 749059, 701879, 2827, 2809, 2810, 661679, 748577, 701812, 702817, 662220, 690577, 671785, 746961, 702869, 701472, 701797, 705568, 726723, 728283, 749318, 747781, 2811, 2807, 714372

-

5.3.1.8

2 entries

5.3.1.9

D-Mannose 6-phosphate = D-Fructose 6-phosphate

662220

-

5.4.2.8

D-mannose 6-phosphate = alpha-D-mannose 1-phosphate

680450

-

5.4.2.8

D-mannose 6-phosphate = D-mannose 1-phosphate

682378, 3352, 3358, 3356, 2821

-

5.4.2.8

2 entries

5.5.1.4

D-Mannose 6-phosphate = myo-Inositol 1-phosphate

3695, 3692

-

Product in Enzyme-catalyzed Reactions (39 results)

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Show Product (39 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.224

D-mannitol 1-phosphate + NADP+ = D-mannose 6-phosphate + NADPH + H+

0

-

2.7.1.1

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

0

-

2.7.1.1

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

0

-

2.7.1.1

2 entries

2.7.1.147

ADP + D-mannose = AMP + D-mannose 6-phosphate

0

-

2.7.1.2

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

0

-

2.7.1.4

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

641483, 0, 641481

-

2.7.1.59

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

0

-

2.7.1.61

D-mannose + acetyl phosphate = D-mannose 6-phosphate + acetate

636972, 0

-

2.7.1.63

(phosphate)45 + D-mannose = (phosphate)44 + D-mannose 6-phosphate

0

-

2.7.1.63

(phosphate)n + D-mannose = (phosphate)n-1 + D-mannose 6-phosphate

0

-

2.7.1.63

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

0

-

2.7.1.63

(phosphate)n + mannose = (phosphate)n-1 + mannose 6-phosphate

0

-

2.7.1.7

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

0

-

2.7.1.7

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

0

-

2.7.1.7

dATP + D-mannose = dADP + D-mannose 6-phosphate

0

-

2.7.1.7

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

0

-

2.7.1.7

hexametaphosphate + D-mannose = pentaphosphate + D-mannose 6-phosphate

0

-

2.7.1.7

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

0

-

2.7.1.7

TTP + D-mannose = TDP + D-mannose 6-phosphate

0

-

2.7.1.7

UTP + D-mannose = UDP + D-mannose 6-phosphate

0

-

2.7.1.7

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

0, 641894, 641481, 641893

-

3.1.4.45

6-O-(N-acetyl-alpha-D-glucosaminyl)phosphono-D-mannopyranose + H2O = N-acetyl-D-glucosamine + 6-O-phosphono-D-mannopyranose

652287

-

3.1.4.45

6-O-(N-acetyl-alpha-D-glucosaminyl)phospho-D-mannose + H2O = N-acetyl-D-glucosamine + 6-phospho-D-mannose

0

-

3.1.4.45

6-O-(N-acetyl-alpha-D-glucosaminyl)phospho-D-mannose + H2O = N-acetyl-D-glucosamine + D-mannose 6-phosphate

0

-

2.7.1.63

4 entries

2.7.1.7

9 entries

3.1.4.45

3 entries

3.2.1.170

2-O-(6-phospho-alpha-D-mannosyl)-D-glycerate + H2O = D-mannose 6-phosphate + D-glycerate

0

-

5.3.1.8

D-fructose 6-phosphate = D-mannose 6-phosphate

0, 652215

-

5.3.1.9

D-fructose 6-phosphate = D-mannose 6-phosphate

0

-

5.4.2.10

D-Mannose 1-phosphate = D-Mannose 6-phosphate

210869

-

5.4.2.2

alpha-D-mannose 1-phosphate = D-mannose 6-phosphate

0

-

5.4.2.2

D-Mannose 1-phosphate = D-Mannose 6-phosphate

0

-

5.4.2.2

alpha-D-mannose 1-phosphate = D-mannose-6-phosphate

0

-

5.4.2.2

alpha-D-mannose-1-phosphate = D-mannose-6-phosphate

0

-

5.4.2.2

D-mannose-1-phosphate = D-mannose-6-phosphate

0

-

5.4.2.2

5 entries

5.4.2.5

D-Mannose + alpha-D-glucose 1-phosphate = D-Mannose 6-phosphate + D-glucose

3330

-

5.4.2.8

alpha-D-mannose 1-phosphate = D-mannose 6-phosphate

0

-

5.4.2.8

D-Mannose 1-phosphate = D-Mannose 6-phosphate

2821, 3356, 3359, 3349, 3355, 3354, 3358, 3362, 3350, 3357, 0, 3352, 3353, 3288, 3360

-

5.4.2.8

alpha-D-mannose-1-phosphate = D-mannose-6-phosphate

0

-

5.4.2.8

D-mannose-1-phosphate = D-mannose-6-phosphate

0

-

5.4.2.8

D-mannose-1-phosphate = mannose-6-phosphate

0

-

5.4.2.8

5 entries

Activator in Enzyme-catalyzed Reactions (6 results)

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Show Activating Compound (6 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.7.1.1

activates isoenzyme Hex II

640232

-

2.7.7.27

2 mM, 12fold activation

719739

-

2.7.7.27

A0.5 value 0.06 mM, Hill coefficient 2.9

738295

-

2.7.7.27

activation, less effective than D-fructose 6-phosphate

488901

-

2.7.7.27

3 entries

2.7.8.17

activates

645378

-

3.5.99.6

-

648219

-

Inhibitor in Enzyme-catalyzed Reactions (12 results)

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Show Inhibitors (12 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.140

potent inhibitor, IC50: 0.0075 mM

669655

-

1.1.1.200

about 30% inhibition at 20 mM

762130

-

2.7.1.7

competitive versus mannose and noncompetitive versus MgATP2-

641893

-

2.7.1.7

up to 20 mM no effect

641892, 641894

-

2.7.1.7

2 entries

3.1.4.12

Niemann-Pick disease fibroblasts

135186

-

3.1.4.45

-

730014

-

3.1.4.45

-

135492, 135498

-

5.3.1.9

-

651319

-

5.3.1.9

1.25 mM, residual activities are 18% and 38% in the direction of fructose 6-phosphate and glucose 6-phosphate formation, respectively

652190

-

5.3.1.9

-

2624

-

5.5.1.4

-

3684, 3692

-

5.5.1.4

competitive

3695

-

3.1.4.45

2 entries

5.3.1.9

3 entries

5.5.1.4

2 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (38 results)

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Show Turnover Number (38 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

2.5.1.132

0.0011

-

wild type enzyme, at pH 7.5 and 37°C

671868

2.5.1.132

0.0083

-

mutant enzyme M42L, at pH 7.5 and 37°C

671868

2.5.1.132

0.017

-

pH 7.5, 25°C

738039

2.5.1.57

0.008

-

mutant enzyme M42L, at 37°C

671868

2.5.1.57

0.011

-

wild type enzyme, at 37°C

671868

2.5.1.57

0.67

-

in 50 mM bicine pH 7.5 at 37°C

671716

3.1.3.23

26

-

mutant enzyme A69M, in 20 mM Tris-HCl(pH 7.0), 5 mM MgCl2, at 32°C

730667

3.1.3.23

32

-

mutant enzyme K71R, in 20 mM Tris-HCl(pH 7.0), 5 mM MgCl2, at 32°C

730667

3.1.3.23

32

-

wild type enzyme, in 20 mM Tris-HCl(pH 7.0), 5 mM MgCl2, at 32°C

730667

3.1.3.23

33

-

mutant enzyme I68M, in 20 mM Tris-HCl(pH 7.0), 5 mM MgCl2, at 32°C

730667

5.3.1.8

0.076

-

pH 7.1, 25°C

661119

5.3.1.8

0.25

-

mutant R472A, pH 7.0, 25°C

692361

5.3.1.8

0.54

-

mutant R479A, pH 7.0, 25°C

692361

5.3.1.8

0.75

-

mutant R373A, pH 7.0, 25°C

692361

5.3.1.8

0.84

-

pH 7.5, 30°C

748577

5.3.1.8

1.38

-

wild-type, pH 7.0, 25°C

692361

5.3.1.8

2.63

-

mutant E410A, pH 7.0, 25°C

692361

5.3.1.8

3.25

-

mutant E458A, pH 7.0, 25°C

692361

5.3.1.8

3.5

-

mutant N433A, pH 7.0, 25°C

692361

5.3.1.8

4.41

-

mutant H411A, pH 7.0, 25°C

692361

5.3.1.8

11

-

mutant enzyme W13A, pH 7.0, 80°C

714372

5.3.1.8

19

-

mutant enzyme E132A, pH 7.0, 80°C

714372

5.3.1.8

19.4

-

pH 7.6, 5 mM Mg2+, temperature not specified in the publication

746961

5.3.1.8

19.4

-

pH 7.6, presence of 5 mM Mg2+

671785

5.3.1.8

20

-

pH 7.1, 25°C

661119

5.3.1.8

31

-

mutant enzyme E67A, pH 7.0, 80°C

714372

5.3.1.8

37

-

mutant enzyme Q48A, pH 7.0, 80°C

714372

5.3.1.8

54

-

mutant enzyme H50A, pH 7.0, 80°C

714372

5.3.1.8

70

-

mutant enzyme R142A, pH 7.0, 80°C

714372

5.3.1.8

75

-

mutant enzyme H122A, pH 7.0, 80°C

714372

5.3.1.8

121

-

selenomethionine-labelled enzyme

2825

5.3.1.8

162

-

wild-type enzyme

2825

5.3.1.8

1371

-

wild type enzyme, pH 7.0, 80°C

714372

5.3.1.8

23550

-

wild type enzyme, at pH 7.0 and 70°C

726723

5.3.1.8

55120

-

mutant enzyme L129F, at pH 7.0 and 70°C

726723

5.3.1.8

85720

-

mutant enzyme N90A/L129F, at pH 7.0 and 70°C

726723

5.3.1.8

106000

-

pH 7.5, 70°C

749059

5.3.1.8

112100

-

mutant enzyme W17Q/N90A/L129F, at pH 7.0 and 70°C

726723

2.5.1.132

3 entries

2.5.1.57

3 entries

3.1.3.23

4 entries

5.3.1.8

28 entries

K_M Value (74 results)

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Show KM Value (74 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.224

5.9

-

enzyme purified from leaves

348006

1.1.1.224

8.6

-

enzyme purified from flowering spikes

348006

1.1.1.224

10.1

-

recombinant enzyme

348005

1.1.1.224

13.6

-

enzyme purified from leaves

348005

1.1.1.224

15.8

-

-

348002

2.5.1.132

1.4

-

pH 7.5, 25°C

738039

2.5.1.132

2.5

5

mutant enzyme M42L, at pH 7.5 and 37°C

671868

2.5.1.132

2.62

-

wild type enzyme, at pH 7.5 and 37°C

671868

2.5.1.132

3.66

-

pH 7.0, 25°C

736395

2.5.1.57

2.5

5

mutant enzyme M42L, at 37°C

671868

2.5.1.57

2.62

-

in 50 mM bicine pH 7.5 at 37°C

671716

2.5.1.57

2.62

-

wild type enzyme, at 37°C

671868

1.1.1.224

5 entries

2.5.1.132

4 entries

2.5.1.57

3 entries

3.1.3.10

9

-

Vmax: 2.6 micromol/min/mg

704914

3.1.3.23

4.9

-

wild type enzyme, in 20 mM Tris-HCl(pH 7.0), 5 mM MgCl2, at 32°C

730667

3.1.3.23

5

-

mutant enzyme I68M, in 20 mM Tris-HCl(pH 7.0), 5 mM MgCl2, at 32°C

730667

3.1.3.23

5.5

-

mutant enzyme K71R, in 20 mM Tris-HCl(pH 7.0), 5 mM MgCl2, at 32°C

730667

3.1.3.23

6.7

-

mutant enzyme A69M, in 20 mM Tris-HCl(pH 7.0), 5 mM MgCl2, at 32°C

730667

5.3.1.8

0.0413

-

pH 7.5, 25°C

693149

5.3.1.8

0.06

-

pH 7.4, 80°C

661679

5.3.1.8

0.121

-

pH 7.1, 25°C

661119

5.3.1.8

0.13

-

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

747781

5.3.1.8

0.17

-

-

2828

5.3.1.8

0.18

-

mutant enzyme E132A, pH 7.0, 80°C

714372

5.3.1.8

0.18

-

mutant enzyme E67A, pH 7.0, 80°C

714372

5.3.1.8

0.2

-

Hepes buffer

2825

5.3.1.8

0.21

-

wild type enzyme, pH 7.0, 80°C

714372

5.3.1.8

0.23

-

recombinant enzyme

2826

5.3.1.8

0.25

-

80°C, pH 7.4

662220

5.3.1.8

0.25

-

wild-type enzyme

2826, 2828

5.3.1.8

0.27

-

mutant enzyme H122A, pH 7.0, 80°C

714372

5.3.1.8

0.33

-

mutant enzyme H50A, pH 7.0, 80°C

714372

5.3.1.8

0.354

-

in 50 mM HEPES buffer, pH 7.1, at 25°C

727158

5.3.1.8

0.372

-

pH 7.5, 25°C

693149

5.3.1.8

0.53

-

mutant enzyme Q48A, pH 7.0, 80°C

714372

5.3.1.8

0.65

-

-

2828

5.3.1.8

0.73

-

-

2810

5.3.1.8

0.8

-

selenomethionine-labelled enzyme, Hepes buffer

2825

5.3.1.8

0.85

-

mutant enzyme W13A, pH 7.0, 80°C

714372

5.3.1.8

0.89

-

pH 7.5, 30°C

748577

5.3.1.8

1

-

Tris/HCl buffer

2825

5.3.1.8

1.1

-

80°C, pH 7.4

662220

5.3.1.8

1.18

-

wild-type, pH 7.0, 25°C

692361

5.3.1.8

1.21

-

22°C, pH 7.4

661902

5.3.1.8

1.24

-

-

2828

5.3.1.8

1.29

-

mutant enzyme R142A, pH 7.0, 80°C

714372

5.3.1.8

1.35

-

-

2624

5.3.1.8

1.6

-

enzyme from developing seeds

2813

5.3.1.8

1.625

-

pH 7.5, 30°C

749318

5.3.1.8

1.9

-

enzyme from germinating seeds

2813

5.3.1.8

2

-

-

2827

5.3.1.8

2.5

-

pH 7.1, 25°C

661119

5.3.1.8

3.03

-

bifunctional enzyme: phosphomannose isomerase-guanosine 5'-diphospho-D-mannose pyrophosphorylase

2824

5.3.1.8

3.808

-

pH 7.5, 30°C

749318

5.3.1.8

4

-

selenomethionine-labelled enzyme, Tris/HCl buffer

2825

5.3.1.8

6.462

-

pH 7.5, 30°C

749318

5.3.1.8

7.62

-

pH 7.5, 70°C

749059

5.3.1.8

8

9

mutant enzyme N90A/L129F, at pH 7.0 and 70°C

726723

5.3.1.8

9

-

pH 7.6, presence of 5 mM Mg2+

671785

5.3.1.8

9.01

-

pH 7.6, 5 mM Mg2+, temperature not specified in the publication

746961

5.3.1.8

9.04

-

mutant E410A, pH 7.0, 25°C

692361

5.3.1.8

12.28

-

mutant R479A, pH 7.0, 25°C

692361

5.3.1.8

12.36

-

mutant E458A, pH 7.0, 25°C

692361

5.3.1.8

12.4

-

30°C, pH 7.6

690577

5.3.1.8

12.9

-

mutant N433A, pH 7.0, 25°C

692361

5.3.1.8

15.9

-

mutant R373A, pH 7.0, 25°C

692361

5.3.1.8

16.26

-

mutant H411A, pH 7.0, 25°C

692361

5.3.1.8

23.12

-

mutant R472A, pH 7.0, 25°C

692361

5.3.1.8

100

-

mutant enzyme W17Q/N90A/L129F, at pH 7.0 and 70°C

726723

5.3.1.8

149

-

wild type enzyme, at pH 7.0 and 70°C

726723

5.3.1.8

243

-

mutant enzyme L129F, at pH 7.0 and 70°C

726723

5.3.1.9

0.25

-

80°C, pH 7.4

662220

5.3.1.9

1.1

-

80°C, pH 7.4

662220

5.4.2.8

0.074

-

in presence of glucose 1,6-diphosphate

3352

5.4.2.8

0.3

0.5

-

3288

3.1.3.23

4 entries

5.3.1.8

53 entries

5.3.1.9

2 entries

5.4.2.8

2 entries

K_i Value (3 results)

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Show KI Value (3 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.7.1.7

12.5

-

pH 8.4, 37°C, noncompetitive versus MgATP2-

641893

2.7.1.7

22.5

-

pH 8.4, 37°C, competitive versus mannose

641893

2.7.1.7

2 entries

5.3.1.9

2.3

-

50°C, pH 7.5, D-fructose 6-phosphate as substrate

651319

IC₅₀ Value (1 result)

top print hide

Show IC50 Value (1 entry)

EC NUMBER

IC50 VALUE

IC50 VALUE MAXIMUM

COMMENTARY

LITERATURE

1.1.1.140

0.0075

-

potent inhibitor, IC50: 0.0075 mM

669655

References & Links

Literature References (128)

top print hide

Show Reference (128 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

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2816

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1993

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1994

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2818

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Mechanism of irreversible inactivation of phosphomannose isomerase by silver ions and flamazine

1995

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Biochemistry

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2819

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A novel Saccharomyces cerevisiae secretory mutant possesses a thermolabile phosphomannose isomerase

1991

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2820

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Crystallization and preliminary X-ray analysis of Candida albicans phosphomannose isomerase

1994

Tolley, S.; Davies, G.; Hubbard, R.E.; Smith, D.J.; Proudfoot, A.E.I.; Payton, M.A.; Cleasby, A.; Wonacott, A.; Wells, T.N.C.

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2821

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Inhibition of phosphomannose isomerase by fructose 1-phosphate: an explanation for defective N-glycosylation in hereditary fructose intolerance

1996

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Pediatr. Res.

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2822

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The X-ray crystal structure of phosphomannose isomerase from Candida albicans at 1.7 A resolution

1996

Cleasby, A.; Wonacott, A.; Skarzynski, T.; Hubbard, R.E.; Davies, G.J.; Proudfoot, A.E.I.; Bernard, A.R.; Payton, M.A.; Wells, T.N.C.

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2823

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Identification of amino acid residues involved in the activity of phosphomannose isomerase-guanosine 5'-diphospho-D-mannose pyrophosphorylase. A bifunctional enzyme in the alginate biosynthetic pathway of Pseudomonas aeruginosa

1994

May, T.B.; Shinabarger, D.; Boyd, A.; Chakrabarty, A.M.

J. Biol. Chem.

269

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2824

1846611

Purification and characterization of phosphomannose isomerase-guanosine diphospho-D-mannose pyrophosphorylase. A bifunctional enzyme in the alginate biosynthetic pathway of Pseudomonas aeruginosa

1991

Shinabarger, D.; Berry, A.; May, T.B.; Rothmel, R.; Fialho, A.; Chakrabarty, A.M.

J. Biol. Chem.

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2825

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Selenomethionine labelling phosphomannose isomerase changes its kinetic properties

1995

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2826

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3288

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3330

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1965

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3349

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3352

4062300

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Glycobiology

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829-834

3357

8922954

Expression, purification and characterization of recombinant phosphomannomutase and GDP-alpha-D-mannose pyrophosphorylase from Salmonella enterica, group B, for the synthesis of GDP-alpha-D-mannose from D-mannose

1996

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3358

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3359

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The reaction mechanism of phosphomannomutase in plants

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Characterization and regulation of the Pseudomonas aeruginosa algC gene encoding phosphomannomutase

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7786023

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16661614

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348003

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Mannitol metabolism in celery stressed by excess macronutrients

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348005

9112783

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348006

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348007

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348008

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6331331

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636972

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Acyl phosphate:hexose phosphotransferase (hexose phosphate:hexose phosphotransferase)

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392-396

636973

6033450

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11886840

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Glycobiology

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73-83

640232

-

Eigenschaften der Hexokinase aus der SCP Hefe Candida maltosa H

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641481

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D-fructose (D-mannose) kinase

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641483

1658003

Purification and properties of fructokinase I from Lactococcus lactis. Localization of scrK on the sucrose-nisin transposon Tn5306

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641892

4635821

Identification and properties of an inducible mannokinase from Streptomyces violaceoruber

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641893

6289902

Identification and kinetic studies of an inducible mannokinase from a Streptomyces strain

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641894

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645378

8940156

Bovine UDP-N-acetylglucosamine:lysosomal-enzyme N-acetylglucosamine-1-phosphotransferase. II. Enzymatic characterization and identification of the catalytic subunit

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646416

2993253

Characterization of a membrane-regulated sugar phosphate phosphohydrolase from Lactobacillus casei

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951-956

648219

236465

Glucosaminephosphate isomerase from house flies

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649729

11879177

The glucose-6-phosphatase system

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362

513-532

651319

12560104

Characterization of the cupin-type phosphoglucose isomerase from the hyperthermophilic archaeon Thermococcus litoralis

2003

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FEBS Lett.

535

200-204

652190

11533028

The phosphoglucose isomerase from the hyperthermophilic archaeon Pyrococcus furiosus is a unique glycolytic enzyme that belongs to the cupin superfamily

2001

Verhees, C.H.; Huynen, M.A.; Ward, D.E.; Schiltz, E.; De Vos, W.M.; van der Oost, J.

J. Biol. Chem.

276

40926-40932

652215

11084042

The role of phosphomannose isomerase in Leishmania mexicana glycoconjugate synthesis and virulence

2001

Garami, A.; Ilg, T.

J. Biol. Chem.

276

6566-6575

652287

12058031

Human mannose 6-phosphate-uncovering enzyme is synthesized as a proenzyme that is activated by the endoprotease furin

2002

Do, H.; Lee, W.S.; Ghosh, P.; Hollowell, T.; Canfield, W.; Kornfeld, S.

J. Biol. Chem.

277

29737-29744

655643

15808744

Enzyme genomics: Application of general enzymatic screens to discover new enzymes

2005

Kuznetsova, E.; Proudfoot, M.; Sanders, S.A.; Reinking, J.; Savchenko, A.; Arrowsmith, C.H.; Edwards, A.M.; Yakunin, A.F.

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263-279

656972

-

Expression of a celery mannose 6-phosphate reductase in Arabidopsis thaliana enhances salt tolerance and induces biosynthesis of both mannitol and a glucosyl-mannitol dimer

2003

Zhifang, G.; Loescher, W.H.

Plant Cell Environ.

26

275-283

661119

15005628

Inhibition of type I and type II phosphomannose isomerases by the reaction intermediate analogue 5-phospho-D-arabinonohydroxamic acid supports a catalytic role for the metal cofactor

2004

Roux, C.; Lee, J.H.; Jeffery, C.J.; Salmon, L.

Biochemistry

43

2926-2934

661679

15290326

Bifunctional phosphoglucose/phosphomannose isomerase from the hyperthermophilic archaeon Pyrobaculum aerophilum

2004

Hansen, T.; Urbanke, C.; Schonheit, P.

Extremophiles

8

507-512

661902

-

Kinetic measurements of phosphoglucose isomerase and phosphomannose isomerase by direct analysis of phosphorylated aldose-ketose isomers using tandem mass spectrometry

2005

Gao, H.; Chen, Y.; Leary, J.A.

Int. J. Mass Spectrom.

240

291-299

662220

14551194

Bifunctional phosphoglucose/phosphomannose isomerases from the Archaea Aeropyrum pernix and Thermoplasma acidophilum constitute a novel enzyme family within the phosphoglucose isomerase superfamily

2004

Hansen, T.; Wendorff, D.; Schonheit, P.

J. Biol. Chem.

279

2262-2272

669655

16791965

Preliminary studies on the inhibition of D-sorbitol-6-phosphate 2-dehydrogenase from Escherichia coli with substrate analogues

2006

Roux, C.; Salmon, L.; Verchere-Beaur, C.

J. Enzyme Inhib. Med. Chem.

21

187-192

671716

16274664

Cloning, expression, and characterization of sialic acid synthases

2005

Hao, J.; Balagurumoorthy, P.; Sarilla, S.; Sundaramoorthy, M.

Biochem. Biophys. Res. Commun.

338

1507-1514

671785

17184737

The Burkholderia cepacia bceA gene encodes a protein with phosphomannose isomerase and GDP-D-mannose pyrophosphorylase activities

2007

Sousa, S.A.; Moreira, L.M.; Wopperer, J.; Eberl, L.; Sa-Correia, I.; Leitao, J.H.

Biochem. Biophys. Res. Commun.

353

200-206

671868

16503877

Elimination of 2-keto-3-deoxy-D-glycero-D-galacto-nonulosonic acid 9-phosphate synthase activity from human N-acetylneuraminic acid 9-phosphate synthase by a single mutation

2006

Hao, J.; Vann, W.F.; Hinderlich, S.; Sundaramoorthy, M.

Biochem. J.

397

195-201

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