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Ligand glucose 1-phosphate

Basic Ligand Information

Molecular Structure

Pathway Source

Pathways

BRENDA

glycogen metabolism, metabolism of disaccharids

KEGG

Acarbose and validamycin biosynthesis, Amino sugar and nucleotide sugar metabolism, Biosynthesis of cofactors, Biosynthesis of nucleotide sugars, Biosynthesis of plant secondary metabolites, Biosynthesis of secondary metabolites, Galactose metabolism, Glucagon signaling pathway, Glycerolipid metabolism, Glycolysis / Gluconeogenesis, Microbial metabolism in diverse environments, O-Antigen nucleotide sugar biosynthesis, Pentose and glucuronate interconversions, Polyketide sugar unit biosynthesis, Starch and sucrose metabolism, Streptomycin biosynthesis more

MetaCyc

CDP-4-dehydro-3,6-dideoxy-D-glucose biosynthesis, CDP-6-deoxy-D-gulose biosynthesis, chitin biosynthesis, D-galactose degradation I (Leloir pathway), dTDP-3-acetamido-3,6-dideoxy-alpha-D-glucose biosynthesis, dTDP-3-acetamido-alpha-D-fucose biosynthesis, dTDP-4-O-demethyl-beta-L-noviose biosynthesis, dTDP-6-deoxy-alpha-D-allose biosynthesis, dTDP-alpha-D-forosamine biosynthesis, dTDP-alpha-D-mycaminose biosynthesis, dTDP-alpha-D-olivose, dTDP-alpha-D-oliose and dTDP-alpha-D-mycarose biosynthesis, dTDP-alpha-D-ravidosamine and dTDP-4-acetyl-alpha-D-ravidosamine biosynthesis, dTDP-beta-D-fucofuranose biosynthesis, dTDP-beta-L-4-epi-vancosamine biosynthesis, dTDP-beta-L-digitoxose biosynthesis, dTDP-beta-L-megosamine biosynthesis, dTDP-beta-L-mycarose biosynthesis, dTDP-beta-L-olivose biosynthesis, dTDP-beta-L-rhamnose biosynthesis, dTDP-D-desosamine biosynthesis, dTDP-L-daunosamine biosynthesis, dTDP-N-acetylthomosamine biosynthesis, dTDP-N-acetylviosamine biosynthesis, dTDP-sibirosamine biosynthesis, extended VTC2 cycle, GDP-alpha-D-glucose biosynthesis, glucose and glucose-1-phosphate degradation, glucosylglycerol biosynthesis, glycogen biosynthesis I (from ADP-D-Glucose), glycogen biosynthesis III (from alpha-maltose 1-phosphate), glycogen degradation I, glycogen degradation II, laminaribiose degradation, stachyose degradation, starch biosynthesis, starch degradation III, starch degradation V, streptomycin biosynthesis, sucrose biosynthesis II, sucrose degradation II (sucrose synthase), sucrose degradation IV (sucrose phosphorylase), trehalose degradation V, type I lipoteichoic acid biosynthesis (S. aureus), UDP-alpha-D-glucose biosynthesis more

Show all BRENDA pathways known for glucose 1-phosphate

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Roles as Enzyme Ligand

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

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Show Natural Substrate (7 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.7.1.10

ATP + D-glucose 1-phosphate = ADP + D-glucose 1,6-bisphosphate

637087, 637088

-

2.7.1.106

3-phospho-D-glyceroyl phosphate + D-glucose 1-phosphate = 3-phospho-D-glycerate + D-glucose 1,6-bisphosphate

640349, 640348

-

2.7.7.33

CTP + D-glucose 1-phosphate = ?

643240, 643237, 643242

-

2.7.7.64

UTP + a monosaccharide 1-phosphate = diphosphate + UDP-monosaccharide

669277

-

2.7.7.64

UTP + D-glucose 1-phosphate = diphosphate + UDP-glucose

704709

-

2.7.7.64

2 entries

3.1.3.10

D-glucose 1-phosphate + H2O = D-glucose + phosphate

134576, 134577, 134578, 134579, 134582, 134580, 134584, 134585, 691563, 134583

-

3.1.3.8

D-glucose 1-phosphate + H2O = D-glucose + phosphate

666840

-

In Vivo Product in Enzyme-catalyzed Reactions (9 results)

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Show Natural Product (9 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.4.1.7

sucrose + phosphate = D-fructose + D-glucose 1-phosphate

0

-

2.7.1.62

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

0

-

2.7.7.28

GDP-glucose + diphosphate = GTP + D-glucose 1-phosphate

645219, 645220

-

2.7.7.28

IDP-glucose + diphosphate = ITP + D-glucose 1-phosphate

0, 645219

-

2.7.7.28

UDPglucose + diphosphate = UTP + D-glucose 1-phosphate

0

-

3.6.1.9

CDP-glucose + H2O = CMP + D-glucose-1-phosphate

246808, 246828

-

3.6.1.9

GDP-glucose + H2O = GMP + D-glucose-1-phosphate

246808

-

3.6.1.9

TDP-glucose + H2O = TMP + D-glucose-1-phosphate

246828, 246808

-

3.6.1.9

UDP-glucose + H2O = UMP + D-glucose-1-phosphate

208377, 208391, 246812, 246821, 246828, 208379, 246825, 246830, 246831, 246808

-

2.7.7.28

3 entries

3.6.1.9

4 entries

Substrate in Enzyme-catalyzed Reactions (73 results)

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Show Substrate (73 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.99.13

D-glucose 1-phosphate + acceptor = 3-keto-D-glucose 1-phosphate + reduced acceptor

389893, 389892

-

2.4.1.1

maltotetraose + D-glucose-1-phosphate = maltopentaose + phosphate

671424

-

2.4.1.1

(dextrin)n-1 + glucose 1-phosphate = (dextrin)n + phosphate

488294, 488300, 488266, 488246, 488252, 488295, 488240, 488258, 488259, 488243

-

2.4.1.1

(maltodextrin)n-1 + glucose 1-phosphate = (maltodextrin)n + phosphate

488264, 488254, 488239, 488267, 488256

-

2.4.1.1

amylopectin + glucose 1-phosphate = amylopectin + phosphate

488265, 488266, 488304, 488300, 488241, 488233, 488264, 488256, 488262, 488259, 488269, 488255, 488239, 488268

-

2.4.1.1

amylose + glucose 1-phosphate = amylose + phosphate

488274, 488261, 488233, 488259, 488262, 488239

-

2.4.1.1

debranched amylopectin + glucose 1-phosphate = debranched amylopectin + phosphate

488262

-

2.4.1.1

glycogen + glucose 1-phosphate = glycogen + phosphate

488300, 488294, 488238, 687257, 488281, 488283, 488288, 488253, 685551, 685629, 488247, 488278, 488284, 488285, 488287, 488297, 488265, 488266, 488304, 488274, 488254, 488275, 488249, 488289, 657863, 488295, 488236, 488233, 488279, 688279, 689907, 488264, 488259, 488243, 488251, 488268, 488248, 488256, 488258, 488240, 488242, 488246, 488252, 488245, 488262, 488239, 488244

-

2.4.1.1

granulose + glucose 1-phosphate = granulose + phosphate

488241

-

2.4.1.1

maltoheptadecaose + glucose 1-phosphate = maltooctadecaose + phosphate

488256

-

2.4.1.1

maltoheptaose + glucose 1-phosphate = maltooctaose + phosphate

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

-

2.4.1.1

maltohexaose + glucose 1-phosphate = maltoheptaose + phosphate

488294, 488254, 488264, 488256, 488295

-

2.4.1.1

maltooctaose + glucose 1-phosphate = maltononaose + phosphate

488264, 488256

-

2.4.1.1

maltopentaose + glucose 1-phosphate = maltohexaose + phosphate

488254, 488265, 488264, 488256, 488295, 488262, 488261

-

2.4.1.1

maltotetraose + glucose 1-phosphate = maltopentaose + phosphate

488294, 488254, 488264, 488295, 688445, 488256, 488239, 488262, 488297

-

2.4.1.1

maltotriose + glucose 1-phosphate = maltotetraose + phosphate

488294, 488264, 488295, 488303, 488259

-

2.4.1.1

starch + glucose 1-phosphate = starch + phosphate

488278, 488297, 488277, 684255, 657863, 488295, 488236, 488292, 488233, 688445, 488246, 488267, 488274, 488259, 488254, 488266, 488265, 488255, 488271, 488273, 488261, 488258, 488270, 488240, 488243

-

2.4.1.1

16 entries

2.4.1.20

1,5-anhydroglucitol + glucose-1-phosphate = ?

671874

-

2.4.1.7

glucose-1-phosphate + arsenate = glucose-1-arsenate + phosphate

637842, 637843

-

2.4.1.97

alpha-D-glucose + glucose 1-phosphate = phosphate + laminaribiose

757210

-

2.4.1.97

laminaribiose + glucose 1-phosphate = phosphate + laminarin

639634, 639635

-

2.4.1.97

laminaribiose + glucose 1-phosphate = phosphate + laminaritriose

757210

-

2.4.1.97

3 entries

2.7.1.10

ATP + D-glucose 1-phosphate = ADP + D-glucose 1,6-bisphosphate

637086, 637087, 637088

-

2.7.1.106

3-phospho-D-glyceroyl phosphate + D-glucose 1-phosphate = 3-phospho-D-glycerate + D-glucose 1,6-bisphosphate

640349, 640350, 640348

-

2.7.1.41

D-glucose 1-phosphate + D-glucose 1-phosphate = D-glucose + D-glucose 1,6-bisphosphate

641628, 641629, 641630

-

2.7.1.42

D-glucose 1-phosphate + 6-methyl-9-(D-1'-ribityl)-isoalloxazine = D-glucose + 6-methyl-9-(D-1'-ribityl)-isoalloxazine 5'-phosphate

636988

-

2.7.1.42

D-glucose 1-phosphate + araboflavin = D-glucose + araboflavin 5'-phosphate

636988

-

2.7.1.42

D-glucose 1-phosphate + isoriboflavin = D-glucose + isoriboflavin 5'-phosphate

636988

-

2.7.1.42

3 entries

2.7.1.61

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

636972, 636973

-

2.7.7.13

8-Azido-GTP + glucose 1-phosphate = 8-Azido-GDPglucose + diphosphate

642865

-

2.7.7.13

ITP + glucose 1-phosphate = IDP-glucose + diphosphate

642865

-

2.7.7.13

2 entries

2.7.7.24

D-glucose 1-phosphate + UTP = UDP-D-glucose + diphosphate

719642

-

2.7.7.30

GTP + D-glucose 1-phosphate = diphosphate + GDP-glucose

661161

-

2.7.7.33

CTP + D-glucose 1-phosphate = ?

643240, 643237, 643242

-

2.7.7.64

UTP + a monosaccharide 1-phosphate = diphosphate + UDP-monosaccharide

669277

-

2.7.7.64

D-glucose 1-phosphate + TTP = TTP-glucose + diphosphate

721524

-

2.7.7.64

D-glucose 1-phosphate + UTP = UDP-D-glucose + diphosphate

738819, 704709, 737817, 737765

-

2.7.7.64

D-glucose 1-phosphate + UTP = UDP-glucose + diphosphate

721524, 691365

-

2.7.7.64

UTP + D-glucose 1-phosphate = diphosphate + UDP-glucose

704709, 669277, 670505, 668028

-

2.7.7.64

5 entries

2.7.7.71

D-glucose 1-phosphate + GTP = GDP-D-glucose + diphosphate

760405

-

2.7.7.9

UTP + D-glucose-1-phosphate = diphosphate + UDP-glucose

663047

-

2.7.7.9

UTP + D-glucose-1-phosphate = UDP-glucose + diphosphate

663369, 663272, 661546, 660765

-

2.7.7.9

UTP + glucose-1-phosphate = UDP-glucose + diphosphate

662442

-

2.7.7.9

3 entries

2.7.7.91

ATP + D-glucose 1-phosphate = diphosphate + GDP-D-glucose

739226

-

3.1.3.1

D-glucose 1-phosphate + H2O = D-glucose + phosphate

654022, 679902, 749638, 677748, 679939

-

3.1.3.1

glucose 1-phosphate + H2O = glucose + phosphate

94572, 94586, 94573, 94609, 94616, 94619, 94613, 94634, 679942

-

3.1.3.1

2 entries

3.1.3.10

D-glucose 1-phosphate + H2O = D-glucose + phosphate

134576, 134577, 134578, 649158, 652437, 134579, 134582, 134583, 134580, 134581, 663741, 134584, 134585, 691563, 704914

-

3.1.3.11

D-glucose-1-phosphate + H2O = D-glucose + phosphate

651698

-

3.1.3.2

D-glucose 1-phosphate + H2O = D-glucose + phosphate

682436, 680990, 713973, 664662, 653161, 665560, 751234, 717266, 653439, 677425, 682668, 714280, 751942

-

3.1.3.2

D-glucose-1-phosphate + H2O = D-glucose + phosphate

691171

-

3.1.3.2

glucose 1-phosphate + H2O = glucose + phosphate

134750, 134766, 134744, 134774, 134755, 134787, 134709, 134736, 134745, 134740, 134752, 134765, 134804, 134760, 134724, 134769, 134691, 134747, 134702

-

3.1.3.2

3 entries

3.1.3.23

D-glucose 1-phosphate + H2O = D-glucose + phosphate

730458

-

3.1.3.25

D-glucose 1-phosphate + H2O = D-glucose + phosphate

677696

-

3.1.3.25

glucose 1-phosphate + H2O = ?

114224, 114232

-

3.1.3.26

D-glucose 1-phosphate + H2O = D-glucose + phosphate

709185, 650588, 652593

-

3.1.3.26

glucose 1-phosphate + H2O = glucose + phosphate

94796, 94803, 94801

-

3.1.3.25

2 entries

3.1.3.26

2 entries

3.1.3.37

glucose 1-phosphate + H2O = glucose + phosphate

134839

-

3.1.3.58

D-glucose-1-phosphate + H2O = D-glucose + phosphate

646416

-

3.1.3.60

D-glucose 1-phosphate + H2O = ?

646421

-

3.1.3.8

D-glucose 1-phosphate + H2O = D-glucose + phosphate

666840, 666841, 664984, 650588, 652593, 682302, 679925

-

3.1.3.8

glucose 1-phosphate + H2O = glucose + phosphate

114253

-

3.1.3.8

2 entries

3.6.1.1

D-glucose-1-phosphate + H2O = D-glucose + phosphate

209768, 209778

-

5.4.2.10

D-glucose 1-phosphate = D-glucose 6-phosphate

210871, 210869

-

5.4.2.2

D-glucose 1-phosphate + D-fructose 1,6-diphosphate = D-glucose 1,6-diphosphate + D-fructose 1-phosphate + D-fructose 6-phosphate

3284

-

5.4.2.2

D-glucose-1-phosphate = D-glucose-6-phosphate

3268, 661150, 662065, 662018

-

5.4.2.2

D-glucose-1-phosphate = glucose-6-phosphate

661880

-

5.4.2.2

Glucose 1-phosphate + 1,3-bisphosphoglycerate = Glucose 1,6-diphosphate + glycerate 3-phosphate

3284

-

5.4.2.3

D-glucose-1-phosphate = D-glucose-6-phosphate

661887

-

5.4.2.3

Glucose 1-phosphate = Glucose 6-phosphate

3300, 3302, 3296

-

5.4.2.2

4 entries

5.4.2.3

2 entries

5.4.2.7

Glucose 1-phosphate = ?

3346

-

5.4.2.8

D-glucose 1-phosphate = D-glucose 6-phosphate

682378, 680647

-

5.4.2.8

D-glucose-1-phosphate = D-glucose-6-phosphate

661150, 662065, 680647, 662018

-

5.4.2.8

Glucose 1-phosphate = Glucose 6-phosphate

3352, 3353

-

5.4.2.8

3 entries

Product in Enzyme-catalyzed Reactions (42 results)

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Show Product (42 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.4.1.1

starch + phosphate = starch + D-glucose 1-phosphate

0

-

2.4.1.1

amylopectin + phosphate = amylopectin + D-glucose-1-phosphate

0

-

2.4.1.1

amylose + phosphate = amylose + D-glucose-1-phosphate

0

-

2.4.1.1

starch + phosphate = starch + D-glucose-1-phosphate

0

-

2.4.1.1

amylose + phosphate = amylose + glucose 1-phosphate

488266, 488278, 488268

-

2.4.1.1

glycogen + phosphate = glycogen + glucose 1-phosphate

0

-

2.4.1.1

6 entries

2.4.1.20

cellobiose + phosphate = D-glucose 1-phosphate + D-glucose

0

-

2.4.1.49

phosphate + cellohexaose = cellopentaose + glucose 1-phosphate

489243, 489244

-

2.4.1.49

phosphate + cellopentaose = cellotetraose + glucose 1-phosphate

489243, 489245, 489244

-

2.4.1.49

phosphate + cellotetraose = cellotriose + glucose 1-phosphate

489243, 489245, 489244

-

2.4.1.49

phosphate + cellotriose = cellobiose + glucose 1-phosphate

489243, 489245, 489244

-

2.4.1.49

4 entries

2.4.1.7

sucrose + phosphate = D-fructose + D-glucose 1-phosphate

0

-

2.7.1.162

ATP + D-glucose = ADP + D-glucose 1-phosphate

0

-

2.7.1.62

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

636971, 0

-

2.7.7.12

UDP-glucose + D-galactose 1-phosphate = D-glucose 1-phosphate + UDP-galactose

0

-

2.7.7.13

GDP-glucose + diphosphate = D-glucose 1-phosphate + GTP

642865

-

2.7.7.23

diphosphate + UDP-glucose = UTP + D-glucose 1-phosphate

0, 643065

-

2.7.7.28

GDP-glucose + diphosphate = GTP + D-glucose 1-phosphate

645219, 645220

-

2.7.7.28

IDP-glucose + diphosphate = ITP + D-glucose 1-phosphate

0, 645219

-

2.7.7.28

UDPglucose + diphosphate = UTP + D-glucose 1-phosphate

0

-

2.7.7.37

dTDP-glucose + phosphate = dTDP + D-glucose 1-phosphate

0

-

2.7.7.37

UDP-glucose + phosphate = UDP + D-glucose 1-phosphate

0

-

2.7.7.28

3 entries

2.7.7.37

2 entries

2.7.7.64

diphosphate + UDP-D-glucose = UTP + D-glucose 1-phosphate

0

-

2.7.7.9

UDP-glucose + adenosine 5'-tetraphosphate = D-glucose-1-phosphate + adenosyl-5'-pentaphospho-5'-uridine

0

-

2.7.7.9

UDP-glucose + ATP = D-glucose-1-phosphate + adenosyl-5'-tetraphospho-5'-uridine

0

-

2.7.7.9

UDP-glucose + CTP = D-glucose-1-phosphate + cytidinyl-5'-tetraphospho-5'-uridine

0

-

2.7.7.9

UDP-glucose + GTP = D-glucose-1-phosphate + guanosyl-5'-tetraphospho-5'-uridine

0

-

2.7.7.9

UDP-glucose + guanosine 5'-tetraphosphate = D-glucose-1-phosphate + guanosyl-5'-pentaphospho-5'-uridine

0

-

2.7.7.9

UDP-glucose + tetrapolyphosphate = uridine-5'-pentaphosphate + D-glucose-1-phosphate

0

-

2.7.7.9

UDP-glucose + tripolyphosphate = uridine-5'-tetraphosphate + D-glucose-1-phosphate

0

-

2.7.7.9

7 entries

3.1.4.1

UDP-glucose + H2O = glucose-1-phosphate + 5'-UMP

0, 208393, 208379

-

3.6.1.21

ADP-Glc + H2O = AMP + Glc-1-phosphate

209943

-

3.6.1.21

GDP-Glc + H2O = GMP + Glc-1-phosphate

0

-

3.6.1.45

CDP-D-glucose = CMP + glucose 1-phosphate

0

-

3.6.1.45

GDP-glucose = GMP + glucose 1-phosphate

0

-

3.6.1.45

UDP-D-glucose = UMP + glucose 1-phosphate

209944, 0

-

3.6.1.9

CDP-glucose + H2O = CMP + D-glucose-1-phosphate

0, 246808, 246828

-

3.6.1.9

GDP-glucose + H2O = GMP + D-glucose-1-phosphate

246808, 246809

-

3.6.1.9

TDP-glucose + H2O = TMP + D-glucose-1-phosphate

246828, 246808

-

3.6.1.9

UDP-glucose + H2O = UMP + D-glucose-1-phosphate

208377, 208391, 246812, 246821, 0, 246828, 208379, 246825, 246830, 246831, 246808

-

3.6.1.9

uridine diphosphoglucose + H2O = UMP + D-glucose-1-phosphate

246809

-

3.6.1.21

2 entries

3.6.1.45

3 entries

3.6.1.9

5 entries

5.4.2.2

Glucose 6-phosphate = Glucose 1-phosphate

0, 3214, 3281

-

Activator in Enzyme-catalyzed Reactions (28 results)

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Show Activating Compound (28 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.2.1.9

-

726000

-

1.2.1.9

14fold activation at 0.1 mM D-glucose 1-phosphate

679719

-

1.2.1.9

activates. Activation follows an increase in affinity for glyceraldehyde-3-phosphate rather than an increase in maximum velocity

724471

-

1.2.1.9

activates. Activation follows an increase in maximum velocity rather than in affinity glyceraldehyde-3-phosphate

724471

-

1.2.1.9

activity increases by 1.4fold with increasing D-glucose 1-phosphate concentration from 0 to 0.1 mM. The enzyme shows K-type allosterism in which the positive cooperativity is abolished with concomitant activation by glucose 1-phosphate

725013

-

1.2.1.9

D-glucose 1-phosphate does not influence the affinity for DL-glyceraldehyde-3-phosphate; but increases the turnover severalfold

725013

-

1.2.1.90

-

727825

-

1.2.1.90

in contrast to other members of the ALDH superfamily, the enzyme from Thermoproteus tenax is regulated by a number of intermediates and metabolites. In the NAD+-dependent oxidation of D-glyceraldehyde 3-phosphate, D-glucose 1-phosphate, D-fructose 6-phosphate, AMP and ADP increase the affinity for the cosubstrate. In the NADP+-dependent reaction the presence of activators increases Vmax by a factor of 3. The crystal structure of the enzyme with the activating molecules reveal a common regulatory site able to accommodate the different activators

728132

-

1.2.1.9

6 entries

1.2.1.90

2 entries

2.3.3.8

activates

488221

-

2.4.1.1

production of a broad spectrum of MOSs (G4-G19) is stimulated both by phosphate and alpha-D-glucose 1-phosphate

718691

-

2.4.1.14

-

638661

-

2.4.1.14

slight activation

638637

-

2.4.1.14

2 entries

2.4.1.18

10 mM, activates

636950

-

2.7.1.19

activation

641031

-

2.7.1.40

not

641584

-

2.7.1.40

slight activation, not isozyme PKp

641576

-

2.7.1.90

no activation

642086

-

2.7.1.90

reverse reaction

642096

-

2.7.1.40

2 entries

2.7.1.90

2 entries

3.1.3.42

2 mM, 30°C, pH 7.8, 3.8fold activation

655957

-

3.1.3.51

activates

134915

-

4.1.1.31

-

748927

-

4.1.1.31

2 mM, 1.2fold increase of activity of PEPC2 at pH 7.3, activity of PEPC2 at pH 8 is nearly identical to activity without glucose 6-phosphate

656117

-

4.1.1.31

2 mM, 1.64fold increase of activity of PEPC1 at pH 7.3, 1.07fold increase in activity of PEPC1 at pH 8

656117

-

4.1.1.31

activates at pH 7 in absence of glycerol, but has no effect under other assay conditions

4318

-

4.1.1.31

activates at pH 7.8

4295

-

4.1.1.31

slight stimulation

656978

-

4.1.1.31

weak activation

4294

-

4.1.1.31

7 entries

5.1.3.2

stimulates

2315

-

Inhibitor in Enzyme-catalyzed Reactions (38 results)

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Show Inhibitors (38 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.200

about 55% inhibition at 20 mM

762130

-

1.1.1.263

25.5% inhibition at 50 mM

207965

-

1.1.1.363

a substrate-competitive inhibitor, that lowers the dissociation constant and maximum fluorescence quenching for NAD+ but not for NADP+

721400

-

2.3.1.157

-

756049

-

2.4.1.1

-

488266

-

2.4.1.1

above 2 mM; substrate inhibition

488238

-

2.4.1.1

completely reversible by 5'-AMP; kinetics

488242

-

2.4.1.1

kinetics

488245

-

2.4.1.1

not inhibited

488241, 488268

-

2.4.1.1

5 entries

2.4.1.11

-

672646

-

2.4.1.20

-

637868

-

2.4.1.20

substrate inhibition, competitive with cellobiose

637865

-

2.4.1.20

2 entries

2.4.1.242

-

672646

-

2.4.1.342

substrate inhibition above 4 mM

758608

-

2.4.99.16

slight inhibition

717816

-

2.7.1.197

-

641866

-

2.7.1.31

weak

641332

-

2.7.1.40

allosteric inhibitor with a 40% reduction in the Vmax

723520

-

2.7.7.13

10 mM, 50% inhibition

642873

-

2.7.7.13

inhibition of GDP-mannose phosphorolysis

642865

-

2.7.7.13

2 entries

2.7.7.9

2 mM, 14% inhibition

762316

-

2.7.9.1

72% activity sustained, effector concentration 5 mM, 55°C

676065

-

3.1.3.17

inhibits by binding to one subunit of phosphorylase a

94679

-

3.1.3.23

complete inhibition of hydrolysis of glucose 6-phosphate as long as glucose 1-phosphate to glucose 6-phosphate ratios are greater than 0.12

94723

-

3.1.4.45

-

730014

-

3.2.1.33

10 mM, 82% of initial activity

655909

-

4.1.1.31

95% residual activity at 2 mM

704531

-

4.1.2.13

-

4933, 4961

-

4.1.3.1

-

33151

-

4.2.1.3

-

650272

-

4.2.3.3

-

137612

-

5.1.3.2

partial inhibition of minor enzyme form, no effect on major enzyme form

2325

-

5.3.1.1

5 mM, 10% inhibition

2565

-

5.3.1.8

competitive

2624

-

5.4.2.2

-

649781

-

5.4.2.2

substrate inhibition above 0.5 mM

650262

-

5.4.2.2

2 entries

5.4.2.3

competitive inhibition

728329

-

5.4.2.8

substrate inhibition of reverse reaction

649449

-

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

2.4.1.1

0.001

-

wild-type, 37°C, pH 5.5

671424

2.4.1.1

0.0019

-

mutant N135S, 37°C, pH 5.5

671424

2.4.1.1

0.0023

-

mutant F39L, 37°C, pH 5.5

671424

2.4.1.1

0.0026

-

mutant T706I, 37°C, pH 5.5

671424

2.4.1.1

0.0036

-

mutant F39L/N135S/T706I, 37°C, pH 5.5

671424

2.4.1.1

0.0041

-

mutant N135S/T706I, 37°C, pH 5.5

671424

2.4.1.1

0.0042

-

mutant F39L/N135S, 37°C, pH 5.5

671424

2.4.1.1

0.0049

-

mutant F39L/T706I, 37°C, pH 5.5

671424

2.4.1.1

131

-

dextrin DP11 synthesis

488295

2.4.1.1

9 entries

2.7.7.30

0.32

-

pH 7.0, 37°C

661161

2.7.7.64

-999

-

Kcat/KM: 530000 1/M/sec, pH 7, 35°C

691365

2.7.7.64

0.008

-

pH 8.0, 37°C

738819

2.7.7.64

0.12

-

co-substrate: TTP, pH 7.6, 37°C

721524

2.7.7.64

26

-

co-substrate: UTP, pH 7.6, 37°C

721524

2.7.7.64

122

-

pH 7, 35°C

691365

2.7.7.64

191

-

forward reaction, pH 7.8, 25°C

704709

2.7.7.64

6 entries

2.7.7.71

0.0117

-

recombinant enzyme, pH 7.5, 37°C

760405

3.1.3.10

0.0393

-

-

134585

3.1.3.10

117

-

pH 6.5

652437

3.1.3.10

145

-

37°C, pH 5.0

663741

3.1.3.8

101

-

37°C, pH 4.5

666840

3.1.3.8

101

-

pH 5.5, 37°C

666841

5.4.2.10

0.0055

-

-

210871

5.4.2.10

0.0138

-

single-mutation S100T

210871

3.1.3.10

3 entries

3.1.3.8

2 entries

5.4.2.10

2 entries

5.4.2.2

50

-

-

3268

5.4.2.8

1.72

-

isoform alpha-PMM2, pH 6.5, 25°C

680647

5.4.2.8

2.85

-

isoform alpha-PMM1, pH 6.5, 25°C

680647

5.4.2.8

2 entries

K_M Value (115 results)

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Show KM Value (115 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.4.1.1

0.05

-

glucan synthesis

488241

2.4.1.1

0.12

-

glucan synthesis

488255

2.4.1.1

0.33

-

mutant T706I, 37°C, pH 5.5

671424

2.4.1.1

0.4

-

in the presence of Mg2+

488246

2.4.1.1

0.48

-

mutant F39L/N135S/T706I, 37°C, pH 5.5

671424

2.4.1.1

0.55

-

glucan synthesis

488241

2.4.1.1

0.56

-

mutant N135S/T706I, 37°C, pH 5.5

671424

2.4.1.1

0.57

-

wild-type, 37°C, pH 5.5

671424

2.4.1.1

0.59

-

mutant N135S, 37°C, pH 5.5

671424

2.4.1.1

0.62

-

mutant F39L/N135S, 37°C, pH 5.5

671424

2.4.1.1

0.66

-

starch synthesis

488259

2.4.1.1

0.72

-

chloroplast phosphorylase

488268

2.4.1.1

0.76

-

mutant F39L/T706I, 37°C, pH 5.5

671424

2.4.1.1

0.86

-

-

488291

2.4.1.1

0.92

-

cytoplasmic phosphorylase

488268

2.4.1.1

0.96

-

mutant F39L, 37°C, pH 5.5

671424

2.4.1.1

0.96

-

synthesis at pH 7.2

488266

2.4.1.1

1

-

-

488246

2.4.1.1

1

-

synthesis

488294

2.4.1.1

1

-

-

488238

2.4.1.1

1.04

-

dextrin DP11 synthesis

488295

2.4.1.1

1.19

-

at 3.1 mM starch

488292

2.4.1.1

1.2

-

-

488285

2.4.1.1

1.2

-

synthesis

488294

2.4.1.1

1.25

-

at 6.2 mM starch

488292

2.4.1.1

1.3

-

-

488254

2.4.1.1

1.38

-

at 18.6 mM starch

488292

2.4.1.1

1.4

-

starch synthesis, phosphorylase A

488258

2.4.1.1

1.51

-

stromal phosphorylase

488304

2.4.1.1

1.6

-

-

488247

2.4.1.1

1.7

-

phosphorylase a

488247

2.4.1.1

1.8

-

-

488277

2.4.1.1

2.2

-

maltose synthesis, phosphorylase A

488258

2.4.1.1

2.7

-

starch synthesis, phosphorylase C

488258

2.4.1.1

2.9

-

-

488254

2.4.1.1

3.3

-

starch synthesis, phosphorylase B

488258

2.4.1.1

3.4

-

glycogen synthesis

488240

2.4.1.1

3.4

-

glycogen synthesis

488240

2.4.1.1

3.56

-

phosphorylase a

488287

2.4.1.1

4

-

maltose synthesis, phosphorylase C

488258

2.4.1.1

4

-

phosphorylase I

488269

2.4.1.1

5

-

glycogen synthesis, phosphorylase A

488258

2.4.1.1

5.5

-

phosphorylase b

488285

2.4.1.1

5.5

-

phosphorylase II

488269

2.4.1.1

6

-

heart phosphorylase I and III

488283

2.4.1.1

8.3

-

-

488254

2.4.1.1

16

-

-

488249

2.4.1.1

18

-

phosphorylase ab

488287

2.4.1.1

20

-

phosphorylase ab

488287

2.4.1.1

49 entries

2.4.1.49

4.7

-

with cellobiose

489243

2.4.1.97

12

-

-

639634

2.7.1.106

0.009

-

25°C, pH 7.5, liver enzyme peak I

640349

2.7.1.106

0.059

-

25°C, pH 7.5, liver enzyme peak II

640349

2.7.1.106

0.09

-

23°C, pH 8, Mg2+- and Zn2+-enzyme in brain

640350

2.7.1.106

0.16

-

25°C, pH 7.5, erythrocyte enzyme

640349

2.7.1.106

4 entries

2.7.7.13

2.85

-

pH 7.5, 37°C, cosubstrate GTP

642865

2.7.7.23

5.8

-

pH 7.5, 37°C, 5 mM UTP

643065

2.7.7.28

2.6

-

-

645220

2.7.7.28

2.6

-

pH 7.8, 25°C

645219

2.7.7.28

2 entries

2.7.7.30

0.346

-

pH 7.0, 37°C

661161

2.7.7.64

0.13

-

cosubstrate UTP, S0.5 value, pH 8.0, 37°C

737765

2.7.7.64

0.177

-

co-substrate: UTP, pH 7.6, 37°C

721524

2.7.7.64

0.177

-

forward reaction, pH 7.6, 37°C

721524

2.7.7.64

0.23

-

pH 7, 35°C

691365

2.7.7.64

0.23

-

pH 8.0

670505

2.7.7.64

0.34

-

pH 7.0, 35°C

669277

2.7.7.64

0.36

-

cosubstrate TTP, S0.5 value, pH 8.0, 37°C

737765

2.7.7.64

1.49

-

pH 8.0, 37°C

738819

2.7.7.64

1.7

-

forward reaction, pH 7.8, 25°C

704709

2.7.7.64

1.706

-

forward reaction, pH 7.8, 25°C

704709

2.7.7.64

1.76

-

co-substrate: TTP, pH 7.6, 37°C

721524

2.7.7.64

11 entries

2.7.7.71

0.33

-

recombinant enzyme, pH 7.5, 37°C

760405

2.7.7.9

0.19

-

-

661546

2.7.7.9

0.83

-

-

663272

3.1.3.1

2.22

-

-

94634

3.1.3.1

4.8

-

-

94573, 94616

3.1.3.10

0.31

-

37°C, pH 5.0

663741

3.1.3.10

0.39

-

pH 6.5

652437

3.1.3.10

0.5

-

-

134576

3.1.3.10

4.8

-

-

134585

3.1.3.10

5.12

-

Vmax: 1.9 micromol/min/mg

704914

2.7.7.9

2 entries

3.1.3.1

2 entries

3.1.3.10

5 entries

3.1.3.2

24.4

-

-

134787

3.1.3.60

0.24

-

25°C, pH 5.6

646421

3.1.3.8

0.26

-

37°C, pH 4.5

666840

3.1.3.8

0.26

-

pH 5.5, 37°C

666841

3.1.3.8

0.28

-

at 62°C, in 50 mM sodium acetate buffer (pH 5)

679925

5.4.2.10

0.08

-

single mutation S100T

210871

5.4.2.10

0.65

-

-

210871

5.4.2.2

0.022

-

-

3268

5.4.2.2

0.0952

-

isoenzyme PH0923, 65°C

662065

5.4.2.2

0.127

-

isoenzyme PH0923S101A, 65°C

662065

5.4.2.2

3

-

90°C

662018

5.4.2.3

0.39

-

-

3300

5.4.2.3

0.54

-

pH 7.4, 26°C

661887

5.4.2.3

0.658

-

-

3296

5.4.2.8

0.0013

-

H308N/H329N double mutant

650233

5.4.2.8

0.0013

-

S108A mutant

650233

5.4.2.8

0.0024

-

S108A/H308N double mutant

650233

5.4.2.8

0.0027

-

K118L/H109Q double mutant

650233

5.4.2.8

0.0028

-

R20A mutant

650233

5.4.2.8

0.0034

-

S108D mutant

650233

5.4.2.8

0.0075

-

isoform alpha-PMM1, pH 6.5, 25°C

680647

5.4.2.8

0.008

-

H109Q mutant

650233

5.4.2.8

0.008

-

K118L mutant

650233

5.4.2.8

0.009

-

R247A mutant

650233

5.4.2.8

0.01

-

H308N mutant

650233

5.4.2.8

0.01

-

S108V mutant

650233

5.4.2.8

0.012

-

-

650233

5.4.2.8

0.0135

-

isoform alpha-PMM2, pH 6.5, 25°C

680647

5.4.2.8

0.016

-

H329N mutant

650233

5.4.2.8

0.022

-

-

3352

5.4.2.8

0.0654

-

30°C, pH 7.5

682378

5.4.2.8

0.0952

-

isoenzyme PH0923, 65°C

662065

5.4.2.8

0.127

-

isoenzyme PH0923S101A, 65°C

662065

5.4.2.8

3

-

90°C

662018

3.1.3.8

3 entries

5.4.2.10

2 entries

5.4.2.2

4 entries

5.4.2.3

3 entries

5.4.2.8

20 entries

K_i Value (10 results)

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Show KI Value (10 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.200

9.07

-

at pH 8.0 and 25°C

762130

2.4.1.1

0.1

-

-

488245, 488242

2.4.1.1

5.09

-

at pH 7.2

488266

2.4.1.1

2 entries

2.4.1.11

120

-

80°C, pH 5.0

672646

2.4.1.20

3.2

-

-

637865

2.4.1.242

120

-

-

672646

2.7.7.13

2.5

-

pH 7.5, 37°C

642865

4.2.1.3

0.81

-

mitochondrial enzyme, with isocitrate as substrate

650272

4.2.1.3

1.9

-

cytosolic enzyme, with isocitrate as substrate

650272

4.2.1.3

2 entries

5.4.2.2

3.3

-

25°C, pH 7.6, substrate inhibition at high concentrations

649781

IC₅₀ Value (2 results)

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Show IC50 Value (2 entries)

EC NUMBER

IC50 VALUE

IC50 VALUE MAXIMUM

COMMENTARY

LITERATURE

2.3.1.157

5

-

pH 7.5, 30°C

756049

5.4.2.3

0.0063

-

versus N-acetyl-D-glucosamine 6-phosphate, pH 7.3, 37°C

728329

References & Links

Literature References (287)

top print hide

Show Reference (287 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

2315

-

Purification and properties of UDP-galactose 4-epimerase from Bifidobacterium bifidum

1978

Lee, L.J.; Kimura, A.; Tochikura, T.

Agric. Biol. Chem.

42

731-737

2325

4348173

Two forms of UDPglucose-4-epimerase from mammalian liver

1973

Ray, M.; Bhaduri, A.

Biochim. Biophys. Acta

302

129-134

2565

-

Pea seed triose phosphate isomerase

1979

Tomlinson, J.D.; Turner, J.F.

Phytochemistry

18

1959-1962

2624

-

Aldose-ketose isomerases

1972

Noltmann, E.A.

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

6

271-354

3214

-

Phosphomutases

1972

Ray, W.J.; Peck, E.J.

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

6

407-477

3268

8050998

Purification and characterization of phosphomannomutase/phosphoglucomutase from Pseudomonas aeruginosa involved in biosynthesis of both alginate and lipopolysaccharide

1994

Ye, R.W.; Zielinski, N.A.; Chakrabarty, A.M.

J. Bacteriol.

176

4851-4877

3281

-

Phosphoglucomutase

1962

Najjar, V.A

The Enzymes, 2nd Ed (Boyer, P. D. , Lardy, H. , Myrbäck, K. , eds. )

6

161-178

3284

-

Multifunctional properties of beef liver phosphoglucomutase

1976

Hirose, M.; Ueda, M.; Chiba, H.

Agric. Biol. Chem.

40

2433-2439

3296

468829

Mechanism of phosphoacetylglucosamine mutase

1979

Cheng, P.W.; Carlson, D.M.

J. Biol. Chem.

254

8353-8357

3300

4996162

Purification and properties of phosphoglucosamine mutase

1971

Fernandez-Sorensen, A.; Carlson, D.M.

J. Biol. Chem.

246

3485-3493

3302

-

Phosphoacetylglucosamine mutase from pig submaxillary gland

1966

Carlson, D.M.

Methods Enzymol.

8

179-182

3346

6297594

Purification and characterization of phosphopentomutase from rat liver

1983

Barsky, D.L.; Hoffee, P.A.

Biochim. Biophys. Acta

743

162-171

3352

4062300

The synthesis of mannose 1-phosphate in brain

1985

Guha, S.K.; Rose, Z.B.

Arch. Biochem. Biophys.

243

168-173

3353

-

Phosphomannomutase activity in wild-type and alginate-producing strains of Pseudomonas aeruginosa

1986

Padgett, P.J.; Phibbs, P.V.

Curr. Microbiol.

14

187-192

4294

-

Purification and properties of phosphoenolpyruvate carboxylase from green leaves of maize

1979

Mares, J.; Barthova, J.; Leblova, S.

Collect. Czech. Chem. Commun.

44

1835-1840

4295

7397199

Kinetic analysis of effectors of phosphoenolpyruvate carboxylase from Bryophyllum fedtschenkoi

1980

Pays, A.G.G.; Jones, R.; Wilkins, M.B.; Fewson, C.A.; Malcolm, A.D.B.

Biochim. Biophys. Acta

614

151-162

4318

16667849

Metabolite regulation of partially purified soybean nodule phosphoenolpyruvate carboxylase

1990

Schuller, K.A.; Turpin, D.H.; Plaxton, W.C.

Plant Physiol.

94

1429-1435

4933

2996495

The purification and properties of human liver ketohexokinase. A role for ketohexokinase and fructose-bisphosphate aldolase in the metabolic production of oxalate from xylitol

1985

Bais, R.; James, H.M.; Rofe, A.M.; Conyers, A.J.

Biochem. J.

230

53-60

4961

2198022

Purification and characterization of cytosolic aldolase from carrot storage root

1990

Moorhead, G.B.G.; Plaxton, W.C.

Biochem. J.

269

133-139

33151

9011236

Purification and characterization of isocitrate lyase and malate synthase from fasting rat liver

1996

Popov, V.N.; Igamberdiev, A.U.; Volvenkin, S.V.

Biokhimiya

61

1898-1903

94572

-

E. coli alkaline phosphatase

1971

Reid, T.W.; Wilson, I.B.

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

4

373-415

94573

-

Mammalian alkaline phosphatases

1971

Fernley, H.N.

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

4

417-447

94586

-

Alkaline phosphatases

1961

Stadtman, T.C.

The Enzymes, 2nd Ed. (Boyer, P. D. , Lardy, H. , Myrbäck, K. , eds. )

5

55-71

94609

-

Extracellular alkaline phosphatase from marine bacteria: purification and properties of extracellular phosphatase from a marine Pseudomonas sp.

1980

Kobori, H.; Taga, N.

Can. J. Microbiol.

26

833-838

94613

413579

Properties of alkaline phosphatase of the halotolerant yeast Debaryomyces hansenii

1978

Adler, L.

Biochim. Biophys. Acta

522

113-121

94616

4970479

Studies on human placental alkaline phosphatase. II. Kinetic properties and studies on the apoenzyme

1968

Harkness, D.R.

Arch. Biochem. Biophys.

126

513-523

94619

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

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Multiple forms of alpha-glucan phosphorylase in banana fruits: properties and kinetics

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Purification and physicochemical properties of starch phosphorylase from young banana leaves

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Characterization of the spinach leaf phosphorylases

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Sweet corn phosphorylase: purification and properties

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Purification and properties of mesophyll and bundle sheath cell alpha-glucan phosphorylases from Zea mays L.

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Properties of alpha-glucan phosphorylase from pea chloroplasts

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Affinity purification and kinetics of pea cotyledon starch phosphorylases

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Kinetic properties of two starch phosphorylases from pea seeds

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Sweet potato starch phosphorylase-purification and characterization

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Purification and properties of potato phosphorylase isozymes

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Inhibition of -glucan phosphorylase by bisulfite competition at the phosphate binding site

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Kinetic properties of alpha-glucan phosphorylase from Indocibium guttattam

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Isolation and partial characterization of two forms of rat heart glycogen phosphorylase

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Comparative studies of phosphorylase isozymes from the rabbit

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Aromatic compounds as allosteric inhibitors of glycogen phosphorylase b

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Inhibition of alpha-glucan phosphorylase by alpha-D-glucopyranosyl fluoride

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Kinetic characterization of rabbit skeletal muscle phosphorylase ab hybrid

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Role of enzyme interactions in the regulation of glycolysis and gluconeogenesis. Purification and properties of the phospho- and dephospho-forms of glycogen phosphorylase from swine kidney

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Glycogen phosphorylase from flight muscle of the hawk moth, Manduca sexta: purification and properties of three interconvertible forms and the effect of flight on their interconversion

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Mechanism of regulation in yeast glycogen phosphorylase

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Purification and characterization of starch phosphorylase from Cuscuta reflexa filaments

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

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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

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