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Ligand maltoheptaose

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (4 results)

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Show Natural Substrate (4 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.2.1.1

maltoheptaose + H2O = maltose + D-glucose + ?

701883

-

3.2.1.20

maltoheptaose + 6 H2O = 7 alpha-D-glucose

667019, 666565

-

3.2.1.B8

linear maltoheptaose + H2O = maltose + D-glucose

710128

-

3.2.1.B8

maltoheptaose + H2O = maltose + D-glucose + ?

707349

-

3.2.1.B8

2 entries

In Vivo Product in Enzyme-catalyzed Reactions (2 results)

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Show Natural Product (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.2.1.1

starch + H2O = maltotriose + maltohexaose + maltoheptaose + maltose

0

-

3.2.1.1

4-nitrophenyl maltoheptaoside + H2O = 4-nitrophenol + maltoheptaoside

0

-

3.2.1.1

2 entries

Substrate in Enzyme-catalyzed Reactions (74 results)

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Show Substrate (74 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.3.10

D-maltoheptaose + O2 = ?

686372

-

1.1.99.29

D-maltoheptaose + acceptor = ?

686372

-

2.3.1.79

acetyl-CoA + maltoheptaose = CoA + acetyl-maltoheptaose

487512

-

2.4.1.1

maltoheptaose + alpha-D-glucose 1-phosphate = maltooctaose + phosphate

659735, 658355, 660145, 701969

-

2.4.1.1

maltoheptaose + glucose 1-phosphate = maltooctaose + phosphate

488264, 488239, 488256, 488295, 488267, 488254, 488261

-

2.4.1.1

maltoheptaose + phosphate = maltohexaose + alpha-D-glucose 1-phosphate

747687, 488294, 701969, 660145

-

2.4.1.1

3 entries

2.4.1.11

UDP-glucose + maltoheptaose = UDP + ?

756121

-

2.4.1.19

maltoheptaose + glycosyl acceptor = beta-cyclodextrin

488834, 488842

-

2.4.1.19

maltoheptaose + L-ascorbic acid = 2-O-alpha-D-glucopyranosyl-L-ascorbic acid

756523

-

2.4.1.19

2 entries

2.4.1.2

1,4-alpha-D-amyloheptaose + (1,6-alpha-D-glucopyranosyl)n = dextran

488875

-

2.4.1.21

ADP-alpha-D-glucose + maltoheptaose = ADP + maltooctaose

736158, 737088

-

2.4.1.248

maltoheptaose = cyclo-(-6)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-4)-alpha-D-Glc-(1-) + ?

698519

-

2.4.1.25

maltoheptaose + glycosyl acceptor = maltose + D-glucose + maltooligosaccharides

755955

-

2.4.1.25

maltoheptaose + maltoheptaose = ?

736255, 685153, 746947

-

2.4.1.25

maltoheptaose + maltoheptaose = D-glucose + maltooligosaccharides

660766

-

2.4.1.25

maltoheptaose + maltoheptaose = maltooligosaccharides

662665

-

2.4.1.25

maltoheptaose + maltopentaose = maltooligosaccharides

489000, 489010, 488995, 489005

-

2.4.1.25

maltoheptaose + maltotriose = maltononaose + D-glucose

488998

-

2.4.1.25

maltoheptaose = maltodextrin + D-glucose

748071

-

2.4.1.25

maltotheptaose + maltotriose = D-glucose + maltooligosaccharides

489011

-

2.4.1.25

maltotheptaose + maltotriose = maltodextrins

489011, 489001, 489010

-

2.4.1.25

9 entries

2.4.1.4

sucrose + maltoheptaose = ?

659439

-

2.4.1.B34

amylose V + maltoheptaose = ?

760023

-

2.4.1.B34

maltoheptaose + H2O = ?

721349, 760023

-

2.4.1.B34

maltoheptaose + H2O = D-glucose + maltotriose + maltohexaose

735514

-

2.4.1.B34

Maltoheptaose = ?

735534, 735717, 721349

-

2.4.1.B34

4 entries

2.4.99.B5

acarbose + maltoheptaose = acarviosyl-(1->4)-alpha-maltoheptaose + maltose

729911

-

3.2.1.1

maltodextrin G7 + H2O = maltodextrin G3 + maltodextrin G4

664980

-

3.2.1.1

maltoheptaose + 3 H2O = 2 maltose + maltotriose

729090

-

3.2.1.1

maltoheptaose + H2O = ?

718361, 701769

-

3.2.1.1

maltoheptaose + H2O = D-glucose + maltose + ?

752105

-

3.2.1.1

maltoheptaose + H2O = D-glucose + maltose + maltotriose

678799

-

3.2.1.1

maltoheptaose + H2O = maltohexaose + maltopentaose + maltotetraose + maltotriose + maltose

655467, 655083

-

3.2.1.1

maltoheptaose + H2O = maltooligosaccharides

750889

-

3.2.1.1

maltoheptaose + H2O = maltose + ?

749668

-

3.2.1.1

maltoheptaose + H2O = maltose + D-glucose + ?

701883

-

3.2.1.1

maltoheptaose + H2O = maltotriose + maltose + D-glucose

693604

-

3.2.1.1

maltoheptaose + H2O = more

393367, 393429, 393431, 393452, 393468, 393450, 136189, 393396, 393462

-

3.2.1.1

maltoheptaoside + H2O = ?

693670

-

3.2.1.1

12 entries

3.2.1.10

maltoheptaose + H2O = ?

654808

-

3.2.1.106

Maltoheptaose = ?

699548

-

3.2.1.116

maltoheptaose + H2O = maltotriose

731585, 646648

-

3.2.1.133

maltoheptaose + H2O = maltose + ?

678461

-

3.2.1.133

maltoheptaose + H2O = maltose + D-glucose + ?

664208

-

3.2.1.135

maltoheptaose + H2O = ?

703502

-

3.2.1.135

maltoheptaose + H2O = D-glucose + maltose + ?

646816, 393353

-

3.2.1.133

2 entries

3.2.1.135

2 entries

3.2.1.141

maltoheptaose + H2O = ?

692727, 680283

-

3.2.1.2

maltoheptaose + H2O = ?

208638, 208643, 208597, 208642, 656955

-

3.2.1.2

maltoheptaose + H2O = maltose + D-glucose + ?

678300

-

3.2.1.20

maltoheptaose + 6 H2O = 7 alpha-D-glucose

667019, 666565, 661611

-

3.2.1.20

maltoheptaose + H2O = ?

717984, 722938

-

3.2.1.20

maltoheptaose + H2O = beta-maltose + maltopentaose

393282

-

3.2.1.20

maltoheptaose + H2O = D-glucose + ?

708224

-

3.2.1.20

maltoheptaose + H2O = maltohexaose + D-glucose

393337, 393340, 393334, 657123, 656390, 393348, 393261, 393331, 393353, 393341, 655023

-

3.2.1.3

maltoheptaose + 6 H2O = 7 beta-D-glucose

728944

-

3.2.1.3

maltoheptaose + H2O = ?

136187, 136194, 136242, 136196, 136184, 136221, 136228, 136231, 136240, 136241, 136223, 136189

-

3.2.1.3

maltoheptaose + H2O = D-glucose + ?

707265

-

3.2.1.3

maltoheptaose + H2O = maltohexaose + D-glucose

663981, 654806, 664362, 657252

-

3.2.1.2

2 entries

3.2.1.20

5 entries

3.2.1.3

4 entries

3.2.1.41

maltoheptaose + H2O = maltotriose + maltose + D-glucose

136429, 136427

-

3.2.1.54

linear maltoheptaose + H2O = alpha-D-glucose + maltose

646818

-

3.2.1.54

maltoheptaose + H2O = ?

721338, 721746, 664779

-

3.2.1.54

maltoheptaose + H2O = D-glucose + maltose + ?

136617, 136620, 136615, 136611, 136618, 136619, 752112, 665437

-

3.2.1.54

maltoheptaose + H2O = maltose + D-glucose + ?

707248

-

3.2.1.54

maltoheptaose + H2O = maltotetraose + maltotriose

750233

-

3.2.1.54

5 entries

3.2.1.60

maltoheptaose + H2O = maltotetraose + maltotriose

136727, 136738

-

3.2.1.98

maltoheptaose + H2O = maltohexaose + maltotriose + maltose + D-glucose

752207

-

3.2.1.98

maltoheptaose + H2O = maltohexaose + maltotriose + maltotetraose + maltopentaose + maltose + D-glucose

664017

-

3.2.1.98

maltoheptaose + p-nitrophenyl alpha-glucoside = p-nitrophenyl alpha-maltoheptaoside + D-glucose

171731

-

3.2.1.B8

linear maltoheptaose + H2O = maltose + D-glucose

710128

-

3.2.1.B8

malto-heptaose + H2O = maltose + D-glucose

708926, 707349

-

3.2.1.B8

maltoheptaose + H2O = maltose + D-glucose + ?

707349

-

3.2.1.98

3 entries

3.2.1.B8

3 entries

4.2.2.13

Maltoheptaose = ?

5966, 650299

-

5.4.99.15

Maltoheptaose = ?

651359, 3488, 3486

-

5.4.99.15

maltoheptaose = alpha-maltopentaosyl trehalose

680274, 680309, 722996, 693473, 724948, 721858

-

5.4.99.15

2 entries

Product in Enzyme-catalyzed Reactions (28 results)

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Show Product (28 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.4.1.1

maltohexaose + alpha-D-glucose 1-phosphate = maltoheptaose + phosphate

0

-

2.4.1.1

maltohexaose + glucose 1-phosphate = maltoheptaose + phosphate

488294, 488254, 488264, 488256, 488295

-

2.4.1.1

2 entries

2.4.1.21

ADP-alpha-D-glucose + maltohexaose = ADP + maltoheptaose

0

-

2.4.1.25

maltopentaose + maltotriose = maltoheptaose + D-glucose

488998

-

2.4.1.25

maltotetraose + maltotriose = glucose + maltoheptaose + maltodecaose

488998

-

2.4.1.25

maltotriose + maltotriose = D-glucose + maltopentaose + maltoheptaose + maltononaose + maltoundecaose

488998

-

2.4.1.25

3 entries

2.4.1.4

sucrose + maltopentaose = D-fructose + maltohexaose + maltoheptaose

489140

-

3.2.1.1

2-chloro-4-nitrophenyl alpha-D-maltoheptaoside + H2O = 2-chloro-4-nitrophenol + alpha-D-maltoheptaose

0

-

3.2.1.1

beta-cyclodextrin + H2O = panose + maltoheptaose

0

-

3.2.1.1

cyclodextrin + H2O = panose + maltoheptaose

0

-

3.2.1.1

pullulan + H2O = panose + maltoheptaose

0

-

3.2.1.1

starch + H2O = maltotriose + maltohexaose + maltoheptaose + maltose

0

-

3.2.1.1

4-nitrophenyl maltoheptaoside + H2O = 4-nitrophenol + maltoheptaoside

0

-

3.2.1.135

pullulan + H2O = maltotriose + maltopentaose + maltohexaose + maltoheptaose

0

-

3.2.1.135

soluble and raw starch + H2O = maltose + maltotriose + maltotetraose + maltopentaose + maltohexaose + maltoheptaose + ?

0

-

3.2.1.1

6 entries

3.2.1.135

2 entries

3.2.1.141

maltoheptaosyltrehalose + H2O = maltoheptaose + alpha,alpha'-trehalose

0

-

3.2.1.3

maltooctaose + H2O = maltoheptaose + beta-D-glucose

0

-

3.2.1.33

Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-(Glc-alpha-1,6)Glc-alpha-1,4-Glc-alpha-1,4-Glc + H2O = Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc-alpha-1,4-Glc + D-glucose

0

-

3.2.1.41

4-nitrophenyl alpha-D-maltoheptaoside + H2O = 4-nitrophenol + alpha-D-maltoheptaose

0

-

3.2.1.54

beta-cyclodextrin + H2O = maltoheptaose

0

-

3.2.1.54

beta-cyclodextrin + H2O = maltose + maltotriose + maltotetraose + maltopentaose + maltoheptaose + glucose

0, 136615

-

3.2.1.54

beta-cyclodextrin + H2O = panose + maltoheptaose

0

-

3.2.1.54

cyclodextrin + H2O = panose + maltoheptaose

0

-

3.2.1.54

gamma-cyclodextrin + H2O = glucose + maltose + maltotriose + maltotetraose + maltopentaose + maltohexaose + maltoheptaose + maltooctaose

0, 136619

-

3.2.1.54

pullulan + H2O = panose + maltoheptaose

0

-

3.2.1.98

4-nitrophenyl alpha-maltoheptaoside + H2O = 4-nitrophenol + maltoheptaose

0

-

3.2.1.98

amylose + H2O = maltohexaose + maltoheptaose

0

-

3.2.1.98

amylose + H2O = maltohexaose + maltotriose + maltoheptaose

0

-

3.2.1.54

6 entries

3.2.1.98

3 entries

Activator in Enzyme-catalyzed Reactions (2 results)

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Show Activating Compound (2 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.4.1.25

stimulating effect of maltooligosaccharides on the conversion of amylose, 15 mM, relative activity 124%

489005

-

2.7.13.3

stimulates, stimulation pattern of MtrA is similar to that of MtrB

680813

-

Inhibitor in Enzyme-catalyzed Reactions (2 results)

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Show Inhibitors (2 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.4.1.18

40% inhibition at 15 mM

636939

-

3.2.1.3

-

728944

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (63 results)

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Show Turnover Number (63 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

2.4.1.1

2.3

-

pH 6.5, 37°C, recombinant enzyme, phosphorolysis reaction

659735

2.4.1.1

4.4

-

pH 6.5, 37°C, recombinant enzyme, synthesis reaction

659735

2.4.1.1

41.3

-

phosphorolysis

488295

2.4.1.1

312

-

synthesis

488295

2.4.1.25

1.99

-

pH 5.5, 70°C, mutant D249S

685153

2.4.1.25

8.7

-

pH 6.7, 80°C

660766

2.4.1.25

16

-

pH 6.6, 70°C

662665

2.4.1.25

159

-

pH 5.5, 70°C, mutant F366L

685153

2.4.1.25

213

-

pH 5.5, 70°C, wild-type enzyme

685153

3.2.1.1

2

-

30°C, pH 5.5

655467

3.2.1.1

5.6

-

30°C, pH 5.5

655467

3.2.1.1

25

-

in 50 mM sodium phosphate buffer (pH 6.5) at 75°C

701883

3.2.1.1

105

-

-

136189

3.2.1.1

573.8

-

pH 6.5, 40°C, recombinant enzyme

752105

3.2.1.1

679

-

-

393462

3.2.1.133

2

-

50°C, pH 6.0, mutant enzyme A290I

664208

3.2.1.133

42.5

-

50°C, pH 6.0, wild-type enzyme

664208

3.2.1.133

72.08

-

50°C, pH 6.0, mutant enzyme A290I

664208

3.2.1.133

384.1

-

50°C, pH 6.0, wild-type enzyme

664208

3.2.1.141

-999

-

-

680283

3.2.1.141

5

-

mutant enzyme Y328F, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation

692727

3.2.1.141

5.49

-

mutant enzyme F355Y, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation

692727

3.2.1.141

6.01

-

-

680283

3.2.1.141

6.01

-

wild-type enzyme, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation

692727

3.2.1.141

6.49

-

mutant enzyme A259S, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation

692727

3.2.1.141

6.49

-

mutant enzyme R356K, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation

692727

3.2.1.20

0.02

-

pH 4.0, 80°C

722938

3.2.1.20

3.42

-

-

393341

3.2.1.20

6.67

-

-

393334

3.2.1.20

10

-

pH 5.5, 42°C

667019

3.2.1.20

35.2

-

pH 6.8, 30°C, recombinant enzyme

657123

3.2.1.20

47.5

-

pH 4.5, 37°C

666565

3.2.1.20

146

-

-

393340

3.2.1.20

1020

-

pH 4.5, 35°C

661611

3.2.1.3

15.8

-

mutant enzyme S411D

136221

3.2.1.3

33

-

mutant enzyme S411C

136221

3.2.1.3

46.6

-

-

136196

3.2.1.3

54

-

recombinant glucoamylase

654806

3.2.1.3

54

-

wild-type enzyme

136228

3.2.1.3

57

-

mutant enzyme S119Y

136241

3.2.1.3

59.4

-

mutant enzyme S411A

136221

3.2.1.3

61.6

-

pH 6.5, 40°C, recombinant enzyme

664362

3.2.1.3

66

-

wild-type enzyme

136241

3.2.1.3

72

-

mutant enzyme G183K

136241

3.2.1.3

72.3

-

wild-type enzyme

136221

3.2.1.3

79

-

mutant enzyme S184H

136241

3.2.1.3

84

-

mutant enzyme S411G

136221

3.2.1.3

114

-

pH 5.0, 40°C

728944

3.2.1.3

221.3

-

45°C, pH 4.5

657252

3.2.1.3

343

-

pH 5.0, 75°C

707265

3.2.1.3

823

-

-

136187

3.2.1.54

1.63

-

pH 4.5, 85°C, mutant enzyme G415E

721746

3.2.1.54

55

-

pH 4.5, 85°C, mutant enzyme M439W/D440H

721338

3.2.1.54

93.3

-

pH 4.5, 85°C, wild-type enzyme

721746

3.2.1.54

160

-

pH 4.5, 85°C, wild-type enzyme

721338

3.2.1.54

170

-

pH 4.5, 85°C, mutant enzyme D440H

721338

2.4.1.1

4 entries

2.4.1.25

5 entries

3.2.1.1

6 entries

3.2.1.133

4 entries

3.2.1.141

7 entries

3.2.1.20

8 entries

3.2.1.3

17 entries

3.2.1.54

5 entries

3.2.1.B8

4.09

-

pH 6.5, 85°C, recombinant enzyme

707349

5.4.99.15

147

-

mutant F405S, pH 5.0, 60°C

680309

5.4.99.15

282

-

mutant Y409F, pH 5.0, 60°C

680274

5.4.99.15

363

-

mutant F405Y, pH 5.0, 60°C

680274, 680309

5.4.99.15

381

-

mutant F405M, pH 5.0, 60°C

680309

5.4.99.15

383

-

wild-type, pH 5.0, 60°C

680274, 680309

5.4.99.15

429

-

mutant F405W, pH 5.0, 60°C

680309

5.4.99.15

6 entries

K_M Value (109 results)

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Show KM Value (109 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.3.10

6.02

-

100 mM ethanolamine buffer, pH 10.5

686372

1.1.99.29

0.51

-

0.1 M ethanolamine buffer at pH 9.4

686372

2.4.1.1

0.08

-

stromal phosphorylase, synthesis

488304

2.4.1.1

0.1

-

stromal phosphorylase, phosphorolysis

488304

2.4.1.1

0.12

-

synthesis, isoenzyme P-2

488261

2.4.1.1

0.18

-

synthesis, isoenzyme P-2

488261

2.4.1.1

0.19

-

pH 6.5, 37°C, recombinant enzyme, phosphorolysis reaction

659735

2.4.1.1

0.2

-

phosphorolysis

488294

2.4.1.1

0.26

-

synthesis, isoenzyme P-1

488261

2.4.1.1

0.38

-

pH 6.5, 37°C, recombinant enzyme, synthesis reaction

659735

2.4.1.1

0.59

-

synthesis, isoenzyme P-1

488261

2.4.1.1

0.81

-

pH 7.5, 30°C, degradation reaction, cytosolic isozyme

660145

2.4.1.1

1.1

-

synthesis, isoenzyme P-1

488261

2.4.1.1

1.22

-

phosphorolysis

488256

2.4.1.1

1.7

-

degradation direction, cosubstrate: phosphate, pH 6.5, 30°C

747687

2.4.1.1

1.7

-

phosphorolysis, at 30°C

488294

2.4.1.1

2.2

-

synthesis

488256

2.4.1.1

3.6

-

degradation direction, cosubstrate: phosphate, pH 6.5, 70°C

747687

2.4.1.1

3.6

-

phosphorolysis, at 70°C

488294

2.4.1.1

3.72

-

phosphorolysis

488295

2.4.1.1

4.49

-

pH 7.5, 37°C, synthesis reaction, cytosolic isozyme

660145

2.4.1.1

5.9

-

phosphorolysis

488254

2.4.1.1

7.1

-

phosphorolysis

488254

2.4.1.1

31

-

synthesis

488254

2.4.1.1

33

-

synthesis

488254

2.4.1.1

39.86

-

synthesis

488295

2.4.1.1

24 entries

2.4.1.2

0.0017

-

-

488882

2.4.1.25

0.46

-

pH 7.0, 95°C

748071

2.4.1.25

1.5

-

pH 6.7, 80°C

660766

2.4.1.25

5.7

-

pH 6.6, 70°C

662665

3.2.1.1

0.21

-

30°C, pH 5.5

655467

3.2.1.1

0.22

-

30°C, pH 5.5

655467

3.2.1.1

0.51

-

-

393462

3.2.1.1

1.42

-

pH 6.5, 40°C, recombinant enzyme

752105

3.2.1.1

2.18

-

-

393431

3.2.1.1

2.7

-

-

136189

3.2.1.1

3.37

-

in 50 mM sodium phosphate buffer (pH 6.5) at 75°C

701883

3.2.1.133

1.5

-

kinetic parameters for C14-labelled maltooligosaccharides

678461

3.2.1.133

8.18

-

50°C, pH 6.0, mutant enzyme A290I

664208

3.2.1.133

9.21

-

50°C, pH 6.0, wild-type enzyme

664208

3.2.1.141

2.19

-

mutant enzyme A259S, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation

692727

3.2.1.141

2.19

-

mutant enzyme R356K, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation

692727

3.2.1.141

2.63

-

-

680283

3.2.1.141

2.63

-

wild-type enzyme, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation

692727

3.2.1.141

2.81

-

mutant enzyme F355Y, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation

692727

3.2.1.141

2.88

-

mutant enzyme Y328F, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation

692727

3.2.1.2

0.9

-

-

208642

3.2.1.2

1.83

-

mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S

208638

3.2.1.20

0.38

-

-

393337

3.2.1.20

0.39

-

pH 4.5, 37°C

666565

3.2.1.20

0.78

-

alpha-glucosidase I

393261

3.2.1.20

0.86

-

pH 5.5, 42°C

667019

3.2.1.20

1.1

-

alpha-glucosidase II

393261

3.2.1.20

3.27

-

-

708224

3.2.1.20

3.8

-

-

393282

3.2.1.20

4.9

-

pH 5.0, 37°C

655023

3.2.1.20

5.09

-

pH 4.0, 80°C

722938

3.2.1.20

5.3

-

-

393340

3.2.1.20

7.89

-

-

393334

3.2.1.20

15.1

-

pH 6.8, 30°C, recombinant enzyme

657123

3.2.1.20

21

-

-

393341

3.2.1.20

30

-

-

393348

3.2.1.20

76

-

pH 4.5, 35°C

661611

3.2.1.3

0.025

-

glucoamylase G2

136223

3.2.1.3

0.026

-

glucoamylase G1

136223

3.2.1.3

0.027

-

glucoamylase G3

136223

3.2.1.3

0.04

-

pH 5.0, 40°C

728944

3.2.1.3

0.058

-

glucoamylase G5

136223

3.2.1.3

0.059

-

glucoamylase G4

136223

3.2.1.3

0.07

-

mutant enzyme S411C

136221

3.2.1.3

0.083

-

wild-type enzyme

136221

3.2.1.3

0.09

-

-

136194

3.2.1.3

0.097

-

-

136184

3.2.1.3

0.1

-

enzyme form GII

136194

3.2.1.3

0.104

-

mutant enzyme S411A

136221

3.2.1.3

0.11

-

-

136196

3.2.1.3

0.11

-

enzyme form GI

136194

3.2.1.3

0.12

-

recombinant glucoamylase

654806

3.2.1.3

0.12

-

wild-type enzyme

136228

3.2.1.3

0.132

-

mutant enzyme S411G

136221

3.2.1.3

0.14

-

wild-type enzyme or mutant enzymes Gly183Lys or S184H

136241

3.2.1.3

0.148

-

mutant enzyme S411D

136221

3.2.1.3

0.15

-

-

136194

3.2.1.3

0.15

-

enzyme form GIII

136194

3.2.1.3

0.15

-

immobilized enzyme

136242

3.2.1.3

0.158

-

mutant enzyme S119Y

136241

3.2.1.3

0.61

-

45°C, pH 4.5

657252

3.2.1.3

2.21

-

pH 5.0, 75°C

707265

3.2.1.3

3.3

-

-

136189

3.2.1.3

4.15

-

-

136187

3.2.1.3

7.59

-

pH 6.5, 40°C, recombinant enzyme

664362

3.2.1.54

0.8

-

-

136615

3.2.1.54

0.91

-

-

136617

3.2.1.54

1.8

-

pH 4.5, 85°C, mutant enzyme M439W/D440H

721338

3.2.1.54

5.8

-

-

136620

3.2.1.54

9.07

-

pH 4.5, 85°C, wild-type enzyme

721746

3.2.1.54

9.77

-

pH 4.5, 85°C, mutant enzyme G415E

721746

3.2.1.54

13

-

pH 4.5, 85°C, mutant enzyme D440H

721338

3.2.1.54

14

-

pH 4.5, 85°C, wild-type enzyme

721338

2.4.1.25

3 entries

3.2.1.1

7 entries

3.2.1.133

3 entries

3.2.1.141

6 entries

3.2.1.2

2 entries

3.2.1.20

15 entries

3.2.1.3

28 entries

3.2.1.54

8 entries

3.2.1.B8

7.41

-

pH 6.5, 85°C, recombinant enzyme

707349

4.2.2.13

0.1

-

pH 5.0, 35°C

650299

5.4.99.15

0.9

-

-

3486

5.4.99.15

1.2

-

pH 5.5, 60°C

721858, 722996

5.4.99.15

2.84

-

mutant F405S, pH 5.0, 60°C

680309

5.4.99.15

3.38

-

mutant F405M, pH 5.0, 60°C

680309

5.4.99.15

3.8

-

mutant F405Y, pH 5.0, 60°C

680274, 680309

5.4.99.15

3.8

-

mutant Y409F, pH 5.0, 60°C

680274

5.4.99.15

3.88

-

wild-type, pH 5.0, 60°C

680274, 680309

5.4.99.15

5.71

-

mutant F405W, pH 5.0, 60°C

680309

5.4.99.15

8 entries

K_i Value (1 result)

top print hide

Show KI Value (1 entry)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

3.2.1.3

1.25

-

pH 5.0, 40°C

728944

References & Links

Literature References (157)

top print hide

Show Reference (157 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

3486

8611744

Purification and properties of a novel enzyme, maltooligosyl trehalose synthase, from Arthrobacter sp. Q36

1995

Nakada, T.; Maruta, K.; Tsusaki, K.; Kubota, M.; Chaen, H.; Sugimoto, T.; Kurimoto, M.; Tsujisaka, Y.

Biosci. Biotechnol. Biochem.

59

2210-2214

3488

9063973

Purification and characterization of thermostable maltooligosyl trehalose synthase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius

1996

Nakada, T.; Ikegami, S.; Chaen, H.; Kubota, M.; Fukuda, S.; Sugimoto, T.; Kurimoto, M.; Tsujisaka, Y.

Biosci. Biotechnol. Biochem.

60

263-266

5966

8461323

alpha-1,4-Glucan lyase, a new class of starch/glycogen degrading enzyme. I. Efficient purification and characterization from red seaweeds

1993

Yu, S.; Kenne, L.; Pedersen, M.

Biochim. Biophys. Acta

1156

313-320

136184

-

Effective purification of glucoamylase in Koji, a solid culture of Aspergillus oryzae on steamed rice, by affinity chromatography using an immobilized acarbose (BAY g-5421)

1988

Ono, K.; Shigeta, S.; Oka, S.

Agric. Biol. Chem.

52

1707-1714

136187

3124820

Purification and properties of an extracellular glucoamylase from a diastatic strain of Saccharomyces cerevisiae

1988

Kleinman, M.J.; Wilkinson, A.E.; Wright, I.P.; Evans, I.H.; Bevan, E.A.

Biochem. J.

249

163-170

136189

3106037

Purification and characterization of extracellular alpha-amylase and glucoamylase from the yeast Candida antarctica CBS 6678

1987

De Mot, R.; Verachtert, H.

Eur. J. Biochem.

164

643-654

136194

-

Kinetic and structural properties of the three forms of glucoamylase of Rhizopus delemar

1985

Abe, J.I.; Nagano, H.; Hizukuri, S.

J. Appl. Biochem.

7

235-247

136196

-

Purification and substrate specificity of glucoamylase of Paecilomyces varioti AHU 9417

1985

Takeda, Y.; Matsui, H.; Tanida, M.; Takao, S.; Chiba, S.

Agric. Biol. Chem.

49

1633-1641

136221

9681871

Protein engineering of Aspergillus awamori glucoamylase to increase its pH optimum

1998

Fang, T.Y.; Ford, C.

Protein Eng.

11

383-388

136223

9802217

Purification and properties of the raw-starch-digesting glucoamylases from Corticium rolfsii

1998

Nagasaka, Y.; Kurosawa, K.; Yokota, A.; Tomita, F.

Appl. Microbiol. Biotechnol.

50

323-330

136228

9521694

Enzymatic properties of the cysteinesulfinic acid derivative of the catalytic-base mutant Glu400->Cys of glucoamylase from Aspergillus awamori

1998

Fierobe, H.P.; Clarke, A.J.; Tull, D.; Svensson, B.

Biochemistry

37

3753-3759

136231

8679632

Mutational modulation of substrate bond-type specificity and thermostability of glucoamylase from Aspergillus awamori by replacement with short homologue active site sequences and thiol/disulfide engineering

1996

Fierobe, H.P.

Biochemistry

35

8696-8704

136240

9056481

Overexpression and characterization of Aspergillus awamori wild-type and mutant glucoamylase secreted by the methylotrophic yeast Pichia pastoris: comparison with wild-type recombinant glucoamylase produced using Saccharomyces cerevisiae and Aspergillus niger as hosts

1997

Fierobe, H.P.; Mirgorodskaya, E.; Frandsen, T.P.; Roepstorff, P.; Svensson, B.

Protein Expr. Purif.

9

159-170

136241

7716159

Protein engineering of the relative specificity of glucoamylase from Aspergillus awamori based on sequence similarities between starch degrading enzymes

1994

Sierks, M.R.; Svennson, B.

Protein Eng.

7

1479-1484

136242

1777117

Authenticity and reconstitution of immobilized enzymes: characterization and denaturation/renaturation of glucoamylase II

1991

Gottschalk, N.; Jaenicke, R.

Biotechnol. Appl. Biochem.

14

324-335

136427

-

Purification and properties of a thermostable pullulanase from Clostridium thermohydrosulfurogenes EM1 which hydrolyses both alpha-1,6 and alpha-1,4-glycosidic linkages

1990

Spreinat, A.; Antranikian, G.

Appl. Microbiol. Biotechnol.

33

511-518

136429

1444355

Purification and general biochemical properties of thermostable pullulanase from Bacillus stearothermophilus G-82

1992

Kambourova, M.S.; Emanuilova, E.I.

Appl. Biochem. Biotechnol.

33

193-203

136611

5649518

Pattern of action of the amylase and the cyclodextrinase of Bacillus macerans

1968

DePinto, J.A.; Campbell, L.L.

Arch. Biochem. Biophys.

125

253-258

136615

-

Purification and properties of cyclomaltodextrinase from alkalophilic Bacillus sp.

1991

Yoshida, A.; Iwasaki, Y.; Akiba, T.; Horikoshi, K.

J. Ferment. Bioeng.

71

226-229

136617

-

Reclassification of a thermostable alpha-glucosidase from Bacillus subtilis H-17 as a cyclomaltodextrinase

1992

Bradley, M.K.; Lindsay, J.A.

Enzyme Microb. Technol.

14

194-196

136618

1644767

Structure of the gene encoding cyclomaltodextrinase from Clostridium thermohydrosulfuricum 39E and characterization of the enzyme purified from Escherichia coli

1992

Podkovyrov, S.M.; Zeikus, J.G.

J. Bacteriol.

8

5400-5405

136619

-

Purification and characterization of a cyclodextrin-degrading enzyme from Flavobacterium sp.

1993

Bender, H.

Appl. Microbiol. Biotechnol.

39

714-719

136620

-

Purification and properties of the cyclodextrinase of Bacillus sphaericus ATCC 7055

1994

Galvin, N.M.; Kelly, C.T.; Fogarty, W.M.

Appl. Microbiol. Biotechnol.

42

46-50

136727

5123132

Isolation, purification, and characterization of a maltotetraose-producing amylase from Pseudomonas stutzeri

1971

Robyt, J.F.; Ackerman, R.J.

Arch. Biochem. Biophys.

145

105-114

136738

16535108

Purification and characterization of a maltotetraose-forming alkaline alpha-amylase from an alkalophilic Bacillus strain, GM8901

1995

Kim, T.U.; Gu, B.G.; Jeong, J.Y.; Byun, S.M.; Shin, Y.C.

Appl. Environ. Microbiol.

61

3105-3112

171731

1368529

Enzymatic synthesis of p-nitrophenyl alpha-maltoheptaoside by transglycosylation of maltohexaose-forming amylase

1990

Ogawa, K.; Uejima, O.; Nakakuki, T.; Usui, T.; Kainuma, K.

Agric. Biol. Chem.

54

581-586

208597

16667324

Purification and characterization of pea epicotyl beta-amylase

1990

Lizotte, P.A.; Henson, C.A.; Duke, S.H.

Plant Physiol.

92

615-621

208638

8690718

Construction of a plasmid used for the expression of a sevenfold-mutant barley beta-amylase with increased thermostability in Escherichia coli and properties of the sevenfold-mutant beta-amylase

1995

Yoshigi, N.; Okada, Y.; Maeba, H.; Sahara, H.; Tamaki, T.

J. Biochem.

118

562-567

208642

8987540

Cloning, sequencing, and expression of a beta-amylase gene from Bacillus cereus var. mycoides and characterization of its products

1996

Yamaguchi, T.; Matsumoto, Y.; Shirakawa, M.; Kibe, M.; Hibino, T.; Kozaki, S.; Takasaki, Y.; Nitta, Y.

Biosci. Biotechnol. Biochem.

60

1255-1259

208643

7765034

Expression in Escherichia coli of cDNA encoding barley beta-amylase and properties of recombinant beta-amylase

1994

Yoshigi, N.; Okada, Y.; Sahara, H.; Koshino, S.

Biosci. Biotechnol. Biochem.

58

1080-1086

393261

-

Low molecular-activity alpha-glucosidase from ungerminated rice seed

1988

Matsui, H.; Ito, H.; Chiba, S.

Agric. Biol. Chem.

52

1859-1860

393282

-

Purification and substrate specificity of sweet corn alpha-glucosidase

1981

Matsui, H.; Yazawa, I.; Chiba, S.

Agric. Biol. Chem.

45

887-894

393331

7814342

Purification and characterization of a maltase from the extremely thermophilic crenarchaeote Sulfolobus solfataricus

1995

Rolfsmeier, M.; Blum, P.

J. Bacteriol.

177

482-485

393334

-

Characterization of high pI alpha-glucosidase from germinated barley seeds: substrate specificity subsite affinities and active-site residues

1995

Im, H.; Henson, C.A.

Carbohydr. Res.

277

145-159

393337

-

Purification and properties of alpha-glucosidase from suspension-cultured sugar-beet cells

1991

Yamasaki, Y.; Konno, H.

Phytochemistry

30

2861-2863

393340

-

Substrate specificity and subsite affinities of crystalline alpha-glucosidase from Aspergillus niger

1991

Kita, A.; Matsui, H.; Somoto, A.; Kimura, A.; Takata, M.; Chiba, S.

Agric. Biol. Chem.

55

2327-2335

393341

-

An alpha-glucosidase from perimicrovillar membranes of Dysdercus peruvianus (hemiptera: pyrrhocoridae) midgut cells. Purification and properties

1995

Silva, C.P.; Terra, W.R.

Insect Biochem. Mol. Biol.

25

487-494

393348

2204617

Allosteric properties, substrate specificity and subsite affinities of honeybee alpha-glucosidase I

1990

Kimura, A.; Takewaki, S.; Matsui, H.; Kubota, M.; Chiba, S.

J. Biochem.

107

762-768

393353

1708385

Characterization of a neopullulanase and an alpha-glucosidase from Bacteroides thetaiotaomicron 95-1

1991

Smith, K.A.; Salyers, A.A.

J. Bacteriol.

173

2962-2968

393367

16667384

Characterization of alpha-amylase from shoots and cotyledons of pea (Pisum sativum L.) seedlings

1990

Beers, E.P.; Duke, S.H.

Plant Physiol.

92

1154-1163

393396

-

alpha-Amylase. UV-method with maltoheptaose

1984

Rauscher, E.

Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )

4

152-157

393429

8226989

The purification and characterization of an extremely thermostable alpha-amylase from the hyperthermophilic archaebacterium Pyrococcus furiosus

1993

Laderman, K.A.; Davis, B.R.; Krutzsch, H.C.; Lewis, M.S.; Griko, Y.V.; Privalov, P.L.; Anfinsen, C.B.

J. Biol. Chem.

268

24394-24401

393431

9726872

Enzymatic properties of a novel liquefying alpha-amylase from an alkaliphilic Bacillus isolate and entire nucleotide and amino acid sequences

1998

Igarashi, K.; Hatada, Y.; Hagihara, H.; Saeki, K.; Takaiwa, M.; Uemura, T.; Ara, K.; Ozaki, K.; Kawai, S.; Kobayashi, T.; Ito, S.

Appl. Environ. Microbiol.

64

3282-3289

393450

27396998

Three Different Types of ?-Amylases from Aspergillus awamori KT-11: Their Purifications, Properties, and Specificities.

1998

Anindyawati, T.; Melliawati, R.; Ito, K.; Iizuka, M.; Minamiura, N.

Biosci. Biotechnol. Biochem.

62

1351-1357

393452

-

Characteristics of a chimeric enzyme engineered from two rice alpha-amylase isozymes

1996

Terashima, M.; Kawai, M.; Kumagai, M.H.; Rodriguez, R.L.; Katoh, S.

Appl. Microbiol. Biotechnol.

45

607-611

393462

-

Ostrich, pancreatic alpha-amylase: kinetic properties, amino terminal sequence and subsite structure

1994

Oosthuizen, V.; Naude, R.J.; Oelofsen, W.; Muramoto, K.; Kamiya, H.

Int. J. Biochem.

26

1313-1321

393468

8958075

Modification of alpha-amylase functions by protein engineering

1996

Terashima, M.; Katoh, S.

Ann. N. Y. Acad. Sci.

799

65-69

487512

12731863

The structure and specificity of Escherichia coli maltose acetyltransferase give new insight into the LacA family of acyltransferases

2003

Lo Leggio, L.; Dal Degan, F.; Poulsen, P.; Moeller Andersen, S.; Larsen, S.

Biochemistry

42

5225-5235

488239

12945

1,4-alpha-Glucan phosphorylase from Klebsiella pneumoniae purification, subunit structure and amino acid composition

1976

Linder, D.; Kurz, G.; Bender, H.; Wallenfels, K.

Eur. J. Biochem.

70

291-303

488254

-

Yeast glycogen phosphorylase: kinetic properties compared with muscle and potato enzymes

1988

Tanabe, S.; Kobayashi, M.; Matsuda, K.

Agric. Biol. Chem.

52

757-764

488256

-

Characterization of Chlorella phosphorylase: the glucan specificity and effect of temperature

1983

Nakamura, Y.; Imamura, M.

Phytochemistry

22

2395-2399

488261

-

Purification and some properties of two phosphorylases from Typha latifolia pollen

1988

Iwata, T.; Funagama, T.; Hara, A.

Agric. Biol. Chem.

52

407-412

488264

4730475

Sweet corn phosphorylase: purification and properties

1973

Lee, E.Y.C.; Braun, J.J.

Arch. Biochem. Biophys.

156

276-286

488267

-

Non-chloroplast alpha-1,4-glucan phosphorylase from pea leaves: characterization and in situ localization by indirect immunofluorescence

1986

Conrads, J.; Van Berkel, J.; Schächtele, C.; Steup, M.

Biochim. Biophys. Acta

882

452-463

488294

8706700

Purification and characterization of an alpha-glucan phosphorylase from the thermophilic bacterium Thermus thermophilus

1996

Boeck, B.; Schinzel, R.

Eur. J. Biochem.

239

150-155

488295

9307027

alpha-1,4-D-Glucan phosphorylase of gram-positive Corynebacterium callunae: isolation, biochemical properties and molecular shape of the enzyme from solution X-ray scattering

1997

Weinhausel, A.; Griessler, R.; Krebs, A.; Zipper, P.; Haltrich, D.; Kulbe, K.D.; Nidetzky, B.

Biochem. J.

326

773-783

488304

11361132

Purification and characterization of the maize amyloplast stromal 112-kDa starch phosphorylase

2001

Mu, H.H.; Yu, Y.; Wasserman, B.P.; Carman, G.M.

Arch. Biochem. Biophys.

388

155-164

488834

-

Purification and properties of cyclomaltodextrin glucanotransferase from an alkalophilic Bacillus

1988

Maekelae, M.; Mattsson, P.; Schinina, M.E.; Korpela, T.

Biotechnol. Appl. Biochem.

10

414-427

488842

1532314

Cyclomaltodextrin glucanotransferase from Bacillus circulans E 192. I. Purification and characterization of the enzyme

1992

Bovetto, L.J.; Backer, D.P.; Villette, J.R.; Sicard, P.J.; Bouquelet, S.J.L.

Biotechnol. Appl. Biochem.

15

48-58

488875

14917661

The biological synthesis of dextran from dextrins

1953

Hehre, E.J.

J. Biol. Chem.

192

161-174

488882

-

Functional characteristics of a bacterial dextrin dextranase from Acetobacter capsulatum ATCC 11894

2001

Suzuki, M.; Unno, T.; Okada, G.

J. Appl. Glycosci.

48

143-151

488995

4972097

The isolation and mode of action of a bacterial glucanosyltransferase

1968

Pazur, J.H.; Okada, S.

J. Biol. Chem.

243

4732-4738

488998

758954

Starch metabolism in Pseudomonas stutzeri. II. Purification and properties of a dextrin glycosyl-transferase (D-enzyme) and amylomaltase

1979

Schmidt, J.; John, M.

Biochim. Biophys. Acta

566

100-114

489000

16665877

Characterization of D-enzyme (4-alpha-glucanotransferase) in Arabidopsis leaf

1988

Lin, T.P.; Preiss, J.

Plant Physiol.

86

260-265

489001

16666985

Characterization of pea chloroplast D-enzyme (4-alpha-D-glucanotransferase)

1989

Kakefuda, G.; Duke, S.H.

Plant Physiol.

91

136-143

489005

1628664

Purification and characterization of a novel thermostable 4-alpha-glucanotransferase of Thermotoga maritima cloned in Escherichia coli

1992

Liebl, W.; Feil, R.; Gabelsberger, J.; Kellermann, J.; Schleifer, K.H.

Eur. J. Biochem.

207

81-88

489010

9310375

4-alpha-glucanotransferase from the hyperthermophilic archaeon Thermococcus litoralis. Enzyme purification and characterization, and gene cloning, sequencing and expression in Escherichia coli

1997

Jeon, B.S.; Taguchi, H.; Sakai, H.; Ohshima, T.; Wakagi, T.; Matsuzawa, H.

Eur. J. Biochem.

248

171-178

489011

-

Cloning and expression of the 4-alpha-glucanotransferase gene from the hyperthermophilic archaeon Pyrococcus sp. KOD1, and characterization of the enzyme

1997

Tachibana, Y.; Fujiwara, S.; Takagi, M.; Imanaka, T.

J. Ferment. Bioeng.

83

540-548

489140

-

Studies on a recombinant amylosucrase

1995

Remaud-Simeon, M.; Albaret, F.; Canard, B.; Varlet, I.; Colonna, P.; Willemot, R.M.; Monsan, P.

Prog. Biotechnol.

10

313-320

636939

5288588

Studies of glycogen branching enzyme. Preparation and properties of alpha-1,4-glucan- alpha-1,4-glucan 6-glycosyltransferase and its action on the characteristic polysaccharide of the liver of children with Type IV glycogen storage disease

1971

Gibson, W.B.; Illingworth Brown, B.; Brown, D.H.

Biochemistry

10

4253-4262

646648

1592801

Haloalkaliphilic maltotriose-forming alpha-amylase from the archaebacterium Natronococcus sp. strain Ah-36

1992

Kobayashi, T.; Kanai, H.; Hayashi, T.; Akiba, T.; Akaboshi, R.; Horikoshi, K.

J. Bacteriol.

174

3439-3444

646816

11916682

Bacillus stearothermophilus neopullulanase selective hydrolysis of amylose to maltose in the presence of amylopectin

2002

Kamasaka, H.; Sugimoto, K.; Takata, H.; Nishimura, T.; Kuriki, T.

Appl. Environ. Microbiol.

68

1658-1664

646818

10825529

Structure, specificity and function of cyclomaltodextrinase, a multispecific enzyme of the alpha-amylase family

2000

Park, K.H.; Kim, T.J.; Cheong, T.K.; Kim, J.W.; Oh, B.H.; Svensson, B.

Biochim. Biophys. Acta

1478

165-185

650299

10564758

Characterization of exo-(1,4)-alpha glucan lyase from red alga Gracilaria chorda. Activation, inactivation and the kinetic properties of the enzyme

1999

Yoshinaga, K.; Fujisue, M.; Abe, J.; Hanashiro, I.; Takeda, Y.; Muroya, K.; Hizukuri, S.

Biochim. Biophys. Acta

1472

447-454

651359

11164309

Characterization of the maltooligosyl trehalose synthase from the thermophilic archaeon Sulfolobus acidocaldarius

2001

Gueguen, Y.; Rolland, J.L.; Schroeck, S.; Flament, D.; Defretin, S.; Saniez, M.H.; Dietrich, J.

FEMS Microbiol. Lett.

194

201-206

654806

11150611

Glucoamylase: structure/function relationships, and protein engineering

2000

Sauer, J.; Sigurskjold, B.W.; Christensen, U.; Frandsen, T.P.; Mirgorodskaya, E.; Harrison, M.; Roepstorff, P.; Svensson, B.

Biochim. Biophys. Acta

1543

275-293

654808

11341943

Comparison of sucrase-free isomaltase with sucrase-isomaltase purified from the house musk shrew Suncus murinus

2001

Takesue, Y.; Yokota, K.; Oda, S.; Takesue, S.

Biochim. Biophys. Acta

1544

341-349

655023

12506981

Purification and characterization of a novel fungal alpha-glucosidase from Mortierella alliacea with high starch-hydrolytic activity

2002

Tanaka, Y.; Aki, T.; Hidaka, Y.; Furuya, Y.; Kawamoto, S.; Shigeta, S.; Ono, K.; Suzuki, O.

Biosci. Biotechnol. Biochem.

66

2415-2423

655083

-

Production and characterization of extracellular alpha-amylases from the thermophilic fungus Thermomyces lanuginosus (wild and mutant strains)

2000

Petrova, S.D.; Ilieva, S.Z.; Bakalova, N.G.; Atev, A.P.; Bhat, M.K.; Kolev, D.N.

Biotechnol. Lett.

22

1619-1624

655467

14511369

On the mechanism of alpha-amylase

2003

Oudjeriouat, N.; Moreau, Y.; Santimone, M.; Svensson, B.; Marchis-Mouren, G.; Desseaux, V.

Eur. J. Biochem.

270

3871-3879

656390

11001140

Purification and specificity of two alpha-glucosidase isoforms of the parasitic protist Trichomonas vaginalis

2000

Ter Kuile, B.H.; Hrdy, I.; Sanchez, L.B.; Muller, M.

J. Eukaryot. Microbiol.

47

440-442

656955

14561508

beta-Amylase in germinating millet seeds

2003

Yamasaki, Y.

Phytochemistry

64

935-939

657123

11469591

Copy-DNA cloning and characterisation of a potato alpha-glucosidase: expression in Escherichia coli and effects of down-regulation in transgenic potato

2001

Taylor, M.A.; Ross, H.A.; McRae, D.; Wright, F.; Viola, R.; Davies, H.V.

Planta

213

258-264

657252

12356463

Cloning, heterologous expression, and enzymatic characterization of a thermostable glucoamylase from Talaromyces emersonii

2002

Nielsen, B.R.; Lehmbeck, J.; Frandsen, T.P.

Protein Expr. Purif.

26

1-8

658355

-

Purification and characterization of a cytosolic starch phosphorylase from etiolated rice seedlings

2004

Hsu, J.H.; Yang, C.C.; Su, J.C.; Lee, P.D.

Bot. Bull. Acad. Sin.

45

187-196

659439

14570882

Molecular basis of the amylose-like polymer formation catalyzed by Neisseria polysaccharea amylosucrase

2004

Albenne, C.; Skov, L.K.; Mirza, O.; Gajhede, M.; Feller, G.; D'Amico, S.; Andre, G.; Potocki-Veronese, G.; van der Veen, B.A.; Monsan, P.; Remaud-Simeon, M.

J. Biol. Chem.

279

726-734

659735

-

Characterization of a hyperthermostable glycogen phosphorylase from Aquifex aeolicus expressed in Escherichia coli

2003

Bhuiyan, S.H.; Rus'd, A.A.; Kitaoka, M.; Hayashi, K.

J. Mol. Catal. B

22

173-180

660145

15564531

The relation of starch phosphorylases to starch metabolism in wheat

2004

Schupp, N.; Ziegler, P.

Plant Cell Physiol.

45

1471-1484

660766

16151092

Amylomaltase of Pyrobaculum aerophilum IM2 produces thermoreversible starch gels

2005

Kaper, T.; Talik, B.; Ettema, T.J.; Bos, H.; van der Maarel, M.J.; Dijkhuizen, L.

Appl. Environ. Microbiol.

71

5098-5106

661611

-

Purification and characterization of the hyper-glycosylated extracellular alpha-glucosidase from Schizosaccharomyces pombe

2005

Okuyama, M.; Tanimoto, Y.; Ito, T.; Anzai, A.; Mori, H.; Kimura, A.; Matsui, H.; Chiba, S.

Enzyme Microb. Technol.

37

472-480

662665

-

A cycloamylose-forming hyperthermostable 4-alpha-glucanotransferase of Aquifex aeolicus expressed in Escherichia coli

2003

Bhuiyan, S.H.; Kitaoka, M.; Hayashi, K.

J. Mol. Catal. B

22

45-53

663981

16509822

The family 21 carbohydrate-binding module of glucoamylase from Rhizopus oryzae consists of two sites playing distinct roles in ligand binding

2006

Chou, W.I.; Pai, T.W.; Liu, S.H.; Hsiung, B.K.; Chang, M.D.

Biochem. J.

396

469-477

664017

15518553

Biochemical and crystallographic analyses of maltohexaose-producing amylase from alkalophilic Bacillus sp. 707

2004

Kanai, R.; Haga, K.; Akiba, T.; Yamane, K.; Harata, K.

Biochemistry

43

14047-14056

664208

15975859

Mutagenesis of Ala290, which modulates substrate subsite affinity at the catalytic interface of dimeric ThMA

2005

Park, S.; Cha, H.; Kang, H.; Shim, J.; Woo, E.; Kim, J.; Park, K.

Biochim. Biophys. Acta

1751

170-177

664362

14981306

Purification, characterization, and subsite affinities of Thermoactinomyces vulgaris R-47 maltooligosaccharide-metabolizing enzyme homologous to glucoamylases

2004

Ichikawa, K.; Tonozuka, T.; Uotsu-Tomita, R.; Akeboshi, H.; Nishikawa, A.; Sakano, Y.

Biosci. Biotechnol. Biochem.

68

413-420

664779

-

Purification and characterization of cyclodextrinase from Paenibacillus sp. A11

2005

Kaulpiboon, J.; Pongsawasdi, P.

Enzyme Microb. Technol.

36

168-175

664980

15043869

Cloning and expression of Lipomyces starkeyi alpha-amylase in Escherichia coli and determination of some of its properties

2004

Kang, H.K.; Lee, J.H.; Kim, D.; Day, D.F.; Robyt, J.F.; Park, K.H.; Moon, T.W.

FEMS Microbiol. Lett.

233

53-64

665437

15469727

Expression of cyclodextrinase gene from Paenibacillus sp. A11 in Escherichia coli and characterization of the purified cyclodextrinase

2004

Kaulpiboon, J.; Pongsawasdi, P.

J. Biochem. Mol. Biol.

37

408-415

666565

15845403

Purification and characterization of an alpha-glucosidase from germinating millet seeds

2005

Yamasaki, Y.; Fujimoto, M.; Kariya, J.; Konno, H.

Phytochemistry

66

851-857

667019

16491468

Purification and biochemical characterization of an alpha-glucosidase from Xanthophyllomyces dendrorhous

2006

Marin, D.; Linde, D.; Lobato, M.F.

Yeast

23

117-125

678300

17223700

Kinetic and structural analysis of enzyme sliding on a substrate: multiple attack in beta-amylase

2007

Ishikawa, K.; Nakatani, H.; Katsuya, Y.; Fukazawa, C.

Biochemistry

46

792-798

678461

17468058

Molecular cloning and biochemical characterization of the first archaeal maltogenic amylase from the hyperthermophilic archaeon Thermoplasma volcanium GSS1

2007

Kim, J.W.; Kim, Y.H.; Lee, H.S.; Yang, S.J.; Kim, Y.W.; Lee, M.H.; Kim, J.W.; Seo, N.S.; Park, C.S.; Park, K.H.

Biochim. Biophys. Acta

1774

661-669

678799

17690465

Purification, biochemical characterization, and gene cloning of a new extracellular thermotolerant and glucose tolerant maltooligosaccharide-forming alpha-amylase from an endophytic ascomycete Fusicoccum sp. BCC4124

2007

Champreda, V.; Kanokratana, P.; Sriprang, R.; Tanapongpipat, S.; Eurwilaichitr, L.

Biosci. Biotechnol. Biochem.

71

2010-2020

680274

19127729

Mutations on aromatic residues of the active site to alter selectivity of the Sulfolobus solfataricus maltooligosyltrehalose synthase

2006

Fang, T.; Tseng, W.; Chung, Y.; Pan, C.

J. Agric. Food Chem.

54

3585-3590

680283

16968069

Expression, purification, and characterization of the maltooligosyltrehalose trehalohydrolase from the thermophilic archaeon Sulfolobus solfataricus ATCC 35092

2006

Fang, T.Y.; Tseng, W.C.; Guo, M.S.; Shih, T.Y.; Hung, X.G.

J. Agric. Food Chem.

54

7105-7112

680309

17567140

Protein engineering of Sulfolobus solfataricus maltooligosyltrehalose synthase to alter its selectivity

2007

Fang, T.Y.; Tseng, W.C.; Pan, C.H.; Chun, Y.T.; Wang, M.Y.

J. Agric. Food Chem.

55

5588-5594

680813

17650500

Osmosensing properties of the histidine protein kinase MtrB from Corynebacterium glutamicum

2007

Moeker, N.; Reihlen, P.; Kraemer, R.; Morbach, S.

J. Biol. Chem.

282

27666-27677

685153

17407266

Identification of acceptor substrate binding subsites +2 and +3 in the amylomaltase from Thermus thermophilus HB8

2007

Kaper, T.; Leemhuis, H.; Uitdehaag, J.C.; van der Veen, B.A.; Dijkstra, B.W.; van der Maarel, M.J.; Dijkhuizen, L.

Biochemistry

46

5261-5269

686372

-

Amperometric biosensors for detection of sugars based on the electrical wiring of different pyranose oxidases and pyranose dehydrogenases with osmium redox polymer on graphite electrodes

2007

Tasca, F.; Timur, S.; Ludwig, R.; Haltrich, D.; Volc, J.; Antiochia, R.; Gorton, L.

Electroanalysis

19

294-302

692727

18563901

Identification of the essential catalytic residues and selectivity-related residues of maltooligosyltrehalose trehalohydrolase from the thermophilic archaeon Sulfolobus solfataricus ATCC 35092

2008

Fang, T.Y.; Tseng, W.C.; Shih, T.Y.; Wang, M.Y.

J. Agric. Food Chem.

56

5628-5633

693473

18594890

Production of a thermophilic maltooligosyl-trehalose synthase in Lactococcus lactis

2008

Cimini, D.; De Rosa, M.; Panariello, A.; Morelli, V.; Schiraldi, C.

J. Ind. Microbiol. Biotechnol.

35

1079-1083

693604

18467868

Effects of calcium ion concentration on starch hydrolysis of barley alpha-amylase isozymes

2008

Yuk, J.B.; Choi, S.H.; Lee, T.H.; Jang, M.U.; Park, J.M.; Yi, A.R.; Svensson, B.; Kim, T.J.

J. Microbiol. Biotechnol.

18

730-734

693670

18951906

Probing the role of aromatic residues at the secondary saccharide-binding sites of human salivary alpha-amylase in substrate hydrolysis and bacterial binding

2008

Ragunath, C.; Manuel, S.G.; Venkataraman, V.; Sait, H.B.; Kasinathan, C.; Ramasubbu, N.

J. Mol. Biol.

384

1232-1248

698519

-

A novel glucanotransferase that produces a cyclomaltopentaose cyclized by an alpha-1,6-linkage

2007

Watanabe, H.; Nishimoto, T.; Chaen, H.; Fukuda, S.

J. Appl. Glycosci.

54

109-118

699548

18586271

Structural insights into the substrate specificity and function of Escherichia coli K12 YgjK, a glucosidase belonging to the glycoside hydrolase family 63

2008

Kurakata, Y.; Uechi, A.; Yoshida, H.; Kamitori, S.; Sakano, Y.; Nishikawa, A.; Tonozuka, T.

J. Mol. Biol.

381

116-128

701769

20108054

A Novel alpha-amylase from Bacillus mojavensis A21: Purification and biochemical characterization

2010

Hmidet, N.; Maalej, H.; Haddar, A.; Nasri, M.

Appl. Biochem. Biotechnol.

162

1018-1030

701883

19834705

Characterization of an exo-acting intracellular alpha-amylase from the hyperthermophilic bacterium Thermotoga neapolitana

2010

Park, K.M.; Jun, S.Y.; Choi, K.H.; Park, K.H.; Park, C.S.; Cha, J.

Appl. Microbiol. Biotechnol.

86

555-566

701969

19054743

Recombinant production and biochemical characterization of a hyperthermostable alpha-glucan/maltodextrin phosphorylase from Pyrococcus furiosus

2008

Mizanur, R.M.; Griffin, A.K.; Pohl, N.L.

Archaea

2

169-176

703502

-

Purification and characterization of a novel amylopullulanase that converts pullulan to glucose, maltose, and maltotriose and starch to glucose and maltose

2010

Zareian, S.; Khajeh, K.; Ranjbar, B.; Dabirmanesh, B.; Ghollasi, M.; Mollania, N.

Enzyme Microb. Technol.

46

57-63

707248

19707756

Characterization of a recombinant amylolytic enzyme of hyperthermophilic archaeon Thermofilum pendens with extremely thermostable maltogenic amylase activity

2010

Li, X.; Li, D.; Yin, Y.; Park, K.H.

Appl. Microbiol. Biotechnol.

85

1821-1830

707265

20155355

Cloning, expression, and characterization of a thermostable glucoamylase from Thermoanaerobacter tengcongensis MB4

2010

Zheng, Y.; Xue, Y.; Zhang, Y.; Zhou, C.; Schwaneberg, U.; Ma, Y.

Appl. Microbiol. Biotechnol.

87

225-233

707349

12127967

A novel amylolytic enzyme from Thermotoga maritima, resembling cyclodextrinase and alpha-glucosidase, that liberates glucose from the reducing end of the substrates

2002

Lee, M.; Kim, Y.-W.; Kim, T.-J.; Park, C.-S.; Kim, J.-W.; Moon, T.-W.; Park, K.-H.

Biochem. Biophys. Res. Commun.

295

818-825

708224

19766731

Purification and partial characterization of a midgut membrane-bound alpha-glucosidase from Quesada gigas (Hemiptera: Cicadidae)

2010

Fonseca, F.V.; Silva, J.R.; Samuels, R.I.; DaMatta, R.A.; Terra, W.R.; Silva, C.P.

Comp. Biochem. Physiol. B

155

20-25

708926

19465663

Role of maltogenic amylase and pullulanase in maltodextrin and glycogen metabolism of Bacillus subtilis 168

2009

Shim, J.H.; Park, J.T.; Hong, J.S.; Kim, K.W.; Kim, M.J.; Auh, J.H.; Kim, Y.W.; Park, C.S.; Boos, W.; Kim, J.W.; Park, K.H.

J. Bacteriol.

191

4835-4844

710128

20385261

Overexpression and characterization of an extremely thermostable maltogenic amylase, with an optimal temperature of 100 degrees C, from the hyperthermophilic archaeon Staphylothermus marinus

2010

Li, D.; Park, J.T.; Li, X.; Kim, S.; Lee, S.; Shim, J.H.; Park, S.H.; Cha, J.; Lee, B.H.; Kim, J.W.; Park, K.H.

New Biotechnol.

27

300-307

717984

20799086

Purification and characterization of the alpha-glucosidase produced by thermophilic fungus Thermoascus aurantiacus CBMAI 756

2010

Carvalho, A.F.; Boscolo, M.; da Silva, R.; Ferreira, H.; Gomes, E.

J. Microbiol.

48

452-459

718361

20552260

Gene sequence, bioinformatics and enzymatic characterization of alpha-amylase from Saccharomycopsis fibuligera KZ

2010

Hostinova, E.; Janecek, S.; Gasperik, J.

Protein J.

29

355-364

721338

17630303

Changes in the catalytic properties of Pyrococcus furiosus thermostable amylase by mutagenesis of the substrate binding sites

2007

Yang, S.J.; Min, B.C.; Kim, Y.W.; Jang, S.M.; Lee, B.H.; Park, K.H.

Appl. Environ. Microbiol.

73

5607-5612

721349

21948833

4,6-alpha-Glucanotransferase, a novel enzyme that structurally and functionally provides an evolutionary link between glycoside hydrolase enzyme families 13 and 70

2011

Kralj, S.; Grijpstra, P.; van Leeuwen, S.S.; Leemhuis, H.; Dobruchowska, J.M.; van der Kaaij, R.M.; Malik, A.; Oetari, A.; Kamerling, J.P.; Dijkhuizen, L.

Appl. Environ. Microbiol.

77

8154-8163

721746

22902546

A novel domain arrangement in a monomeric cyclodextrin-hydrolyzing enzyme from the hyperthermophile Pyrococcus furiosus

2013

Park, J.T.; Song, H.N.; Jung, T.Y.; Lee, M.H.; Park, S.G.; Woo, E.J.; Park, K.H.

Biochim. Biophys. Acta

1834

380-386

721858

27281155

Reaction mechanism of a new glycosyltrehalose-producing enzyme isolated from the hyperthermophilic archaeum, Sulfolobus solfataricus KM1

1996

Kato, M.; Miura, Y.; Kettoku, M.; Shindo, K.; Iwamatsu, A.; Kobayashi, K.

Biosci. Biotechnol. Biochem.

60

921-924

722938

23314368

Enzymatic properties of a thermostable alpha-glucosidase from acidothermophilic crenarchaeon Sulfolobus tokodaii strain 7

2013

Park, J.E.; Park, S.H.; Woo, J.Y.; Hwang, H.S.; Cha, J.; Lee, H.

J. Microbiol. Biotechnol.

23

56-63

722996

-

Trehalose production with a new enzymatic system from Sulfolobus solfataricus KM1

1999

Kato, M.

J. Mol. Catal. B

6

223-233

724948

15150700

Characterization of the trehalosyl dextrin-forming enzyme from the thermophilic archaeon Sulfolobus solfataricus ATCC 35092

2004

Fang, T.Y.; Hung, X.G.; Shih, T.Y.; Tseng, W.C.

Extremophiles

8

335-343

728944

24468405

Glucoamylase of Caulobacter crescentus CB15: Cloning and expression in Escherichia coli and functional identification

2014

Sakaguchi, M.; Matsushima, Y.; Nankumo, T.; Seino, J.; Miyakawa, S.; Honda, S.; Sugahara, Y.; Oyama, F.; Kawakita, M.

AMB Express

4

5

729090

25038927

An exceptionally cold-adapted alpha-amylase from a metagenomic library of a cold and alkaline environment

2015

Vester, J.; Glaring, M.; Stougaard, P.

Appl. Microbiol. Biotechnol.

99

717-727

729911

11443082

Identification, cloning, expression, and characterization of the extracellular acarbose-modifying glycosyltransferase, AcbD, from Actinoplanes sp. strain SE50

2001

Hemker, M.; Stratmann, A.; Goeke, K.; Schröder, W.; Lenz, J.; Piepersberg, W.; Pape, H.

J. Bacteriol.

183

4484-4492

731585

24345719

Characterization and mechanism of action of Microbacterium imperiale glucan 1,4-alpha-maltotriohydrolase

2014

Wu, C.; Zhou, X.; Xu, Y.; Li, H.; Tian, Y.; Xu, X.; Jin, Z.

Carbohydr. Res.

384

46-50

735514

26590275

The Exiguobacterium sibiricum 255-15 GtfC enzyme represents a novel glycoside hydrolase 70 subfamily of 4,6-alpha-glucanotransferase enzymes

2016

Gangoiti, J.; Pijning, T.; Dijkhuizen, L.

Appl. Environ. Microbiol.

82

756-766

735534

22361861

4,6-alpha-Glucanotransferase activity occurs more widespread in Lactobacillus strains and constitutes a separate GH70 subfamily

2013

Leemhuis, H.; Dijkman, W.; Dobruchowska, J.; Pijning, T.; Grijpstra, P.; Kralj, S.; Kamerling, J.; Dijkhuizen, L.

Appl. Microbiol. Biotechnol.

97

181-193

735717

26868718

The Gram-negative bacterium Azotobacter chroococcum NCIMB 8003 employs a new glycoside hydrolase family 70 4,6-alpha-glucanotransferase enzyme (GtfD) to synthesize a reuteran like polymer from maltodextrins and starch

2016

Gangoiti, J.; van Leeuwen, S.S.; Vafiadi, C.; Dijkhuizen, L.

Biochim. Biophys. Acta

1860

1224-1236

736158

26858729

In vitro biochemical characterization of all barley endosperm starch synthases

2015

Cuesta-Seijo, J.A.; Nielsen, M.M.; Ruzanski, C.; Krucewicz, K.; Beeren, S.R.; Rydhal, M.G.; Yoshimura, Y.; Striebeck, A.; Motawia, M.S.; Willats, W.G.; Palcic, M.M.

Front. Plant Sci.

6

1265

736255

26875536

Mutagenesis for improvement of activity and thermostability of amylomaltase from Corynebacterium glutamicum

2016

Nimpiboon, P.; Kaulpiboon, J.; Krusong, K.; Nakamura, S.; Kidokoro, S.; Pongsawasdi, P.

Int. J. Biol. Macromol.

86

820-828

737088

26367870

The role of cysteine residues in redox regulation and protein stability of Arabidopsis thaliana starch synthase 1

2015

Skryhan, K.; Cuesta-Seijo, J.A.; Nielsen, M.M.; Marri, L.; Mellor, S.B.; Glaring, M.A.; Jensen, P.E.; Palcic, M.M.; Blennow, A.

PLoS ONE

10

e0136997

746947

-

Acceptor specificity of 4-alpha-glucanotransferase of Thermotoga maritima

1994

Huber, W.; Liebl, W.

Biocatal. Biotransform.

11

105-115

747687

8706700

Purification and characterisation of an alpha-glucan phosphorylase from the thermophilic bacterium Thermus thermophilus

1996

Boeck, B.; Schinzel, R.

Eur. J. Biochem.

239

150-155

748071

10348846

Maltose metabolism in the hyperthermophilic archaeon Thermococcus litoralis Purification and characterization of key enzymes

1999

Xavier, K.; Peist, R.; Kossmann, M.; Boos, W.; Santos, H.

J. Bacteriol.

181

3358-3367

749668

29752267

Novel maltogenic amylase CoMA from Corallococcus sp. strain EGB catalyzes the conversion of maltooligosaccharides and soluble starch to maltose

2018

Zhou, J.; Li, Z.; Zhang, H.; Wu, J.; Ye, X.; Dong, W.; Jiang, M.; Huang, Y.; Cui, Z.

Appl. Environ. Microbiol.

84

e00152-18

750233

30732782

Preparation of malto-oligosaccharides with specific degree of polymerization by a novel cyclodextrinase from Palaeococcus pacificus

2019

Ji, H.; Bai, Y.; Li, X.; Wang, J.; Xu, X.; Jin, Z.

Carbohydr. Polym.

210

64-72

750889

26979859

Characterization and application of BiLA, a psychrophilic alpha-amylase from Bifidobacterium longum

2016

Lee, H.W.; Jeon, H.Y.; Choi, H.J.; Kim, N.R.; Choung, W.J.; Koo, Y.S.; Ko, D.S.; You, S.; Shim, J.H.

J. Agric. Food Chem.

64

2709-2718

752105

27108054

Purification and characterization of a novel intracellular alpha-amylase with a wide variety of substrates hydrolysis and transglycosylation activity from Paenibacillus sp. SSG-1

2018

Xu, Q.; Cao, Y.; Li, X.; Liu, L.; Qin, S.; Wang, Y.; Cao, Y.; Xu, H.; Qiao, D.

Protein Expr. Purif.

144

62-70

752112

30149121

Recombinant expression, purification, and characterization of a cyclodextrinase from Massilia timonae

2019

Santos, F.C.D.; Barbosa-Tessmann, I.P.

Protein Expr. Purif.

154

74-84

752207

27808246

Characterization of the starch-acting MaAmyB enzyme from Microbacterium aurum B8.A representing the novel subfamily GH13_42 with an unusual, multi-domain organization

2016

Valk, V.; van der Kaaij, R.M.; Dijkhuizen, L.

Sci. Rep.

6

36100

755955

28522291

Y418 in 410s loop is required for high transglucosylation activity and large-ring cyclodextrin production of amylomaltase from Corynebacterium glutamicum

2017

Tumhom, S.; Krusong, K.; Pongsawasdi, P.

Biochem. Biophys. Res. Commun.

488

516-521

756121

28465215

Glycogen synthase from the parabasalian parasite Trichomonas vaginalis An unusual member of the starch/glycogen synthase family

2017

Wilson, W.A.; Pradhan, P.; Madhan, N.; Gist, G.C.; Brittingham, A.

Biochimie

138

90-101

756523

30563366

Current studies on the enzymatic preparation 2-O-alpha-D-glucopyranosyl-L-ascorbic acid with cyclodextrin glycosyltransferase

2019

Tao, X.; Su, L.; Wu, J.

Crit. Rev. Biotechnol.

39

249-257

760023

28399167

Characterization of the Paenibacillus beijingensis DSM 24997 GtfD and its glucan polymer products representing a new glycoside hydrolase 70 subfamily of 4,6-alpha-glucanotransferase enzymes

2017

Gangoiti, J.; Lamothe, L.; van Leeuwen, S.S.; Vafiadi, C.; Dijkhuizen, L.

PLoS ONE

12

e0172622