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Ligand 2'-deoxyadenosine

Basic Ligand Information

Molecular Structure

Show all BRENDA pathways known for 2'-deoxyadenosine

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (20 results)

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Show Natural Substrate (20 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.3.39

2'-deoxyadenosine + 2 O2 + H2O = 2'-deoxy-9-riburonosyladenine + 2 H2O2

287628

-

2.7.1.113

ATP + 2'-deoxyadenosine = ADP + 2'-deoxyadenosine 5'-phosphate

661034, 661728, 671890, 661453, 661731, 663023, 662882

-

2.7.1.113

UTP + 2'-deoxyadenosine = UDP + 2'-deoxyadenosine 5'-phosphate

661453

-

2.7.1.113

2 entries

2.7.1.145

ATP + 2'-deoxyadenosine = ADP + 2'-deoxyadenosine 5'-phosphate

661702, 662967, 738781, 661072, 661453

-

2.7.1.74

ATP + 2'-deoxyadenosine = ADP + 2'-deoxyadenosine 5'-phosphate

662988, 661731, 663023, 702271, 674748, 671911

2zi3, 3D-view

2.7.1.74

ATP + 2'-deoxyadenosine = ADP + 2'-deoxyadenosine 5'-phosphate

662988, 661731, 663023, 702271, 674748, 671911

2zi6, 3D-view

2.7.1.74

NTP + 2'-deoxyadenosine = NDP + 2'-deoxyadenosine 5'-phosphate

671043, 672149

2zi3, 3D-view

2.7.1.74

NTP + 2'-deoxyadenosine = NDP + 2'-deoxyadenosine 5'-phosphate

671043, 672149

2zi6, 3D-view

2.7.1.74

UTP + 2'-deoxyadenosine = UDP + 2'-deoxyadenosine 5'-phosphate

662988, 663023, 674748, 671911

2zi3, 3D-view

2.7.1.74

UTP + 2'-deoxyadenosine = UDP + 2'-deoxyadenosine 5'-phosphate

662988, 663023, 674748, 671911

2zi6, 3D-view

2.7.1.74

ATP + deoxyadenosine = ADP + dAMP

723029, 721556, 722913

2zi3, 3D-view

2.7.1.74

ATP + deoxyadenosine = ADP + dAMP

723029, 721556, 722913

2zi6, 3D-view

2.7.1.74

UTP + deoxyadenosine = UDP + dAMP

721556, 722913

2zi3, 3D-view

2.7.1.74

UTP + deoxyadenosine = UDP + dAMP

721556, 722913

2zi6, 3D-view

2.7.1.76

ATP + 2'-deoxyadenosine = ADP + 2'-deoxyadenosine 5'-phosphate

662985, 660855

-

2.7.1.76

ATP + 2'-deoxyadenosine = ADP + dAMP

739204, 759008, 759073

-

2.7.1.76

ATP + deoxyadenosine = ADP + 5'-dAMP

641937, 641977, 640567, 641984

-

2.7.1.76

ATP + deoxyadenosine = ADP + dAMP

675444

-

2.7.1.74

10 entries

2.7.1.76

4 entries

3.2.2.7

2'-deoxyadenosine + H2O = 6-aminopurine + 2-deoxy-D-ribofuranose

137099, 137109, 137102, 137112, 137113, 137111

-

3.5.4.4

2'-deoxyadenosine + H2O = 2'-deoxyinosine + NH3

667032, 686549, 700148, 667870

3iar, 3D-view

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

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Show Natural Product (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.4.2.6

2'-deoxy-D-ribosyl-uracil + adenine = 2'-deoxy-D-ribosyl-adenine + uracil

0

1s2g, 3D-view

Substrate in Enzyme-catalyzed Reactions (102 results)

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Show Substrate (102 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.3.28

2'-deoxyadenosine + O2 = 9-(2-deoxy-beta-D-erythro-pentofuranuronosyl)-9H-purin-6-amine + H2O

287612

-

1.1.3.39

2'-deoxyadenosine + 2 O2 + H2O = 2'-deoxy-9-riburonosyladenine + 2 H2O2

287628

-

2.4.2.1

2'-deoxyadenosine + phosphate = 2-deoxy-alpha-D-ribose 1-phosphate + adenine

721902

-

2.4.2.1

2'-deoxyadenosine + phosphate = adenine + 2-deoxy-alpha-D-ribose 1-phosphate

726781, 727477, 721902, 686625, 722135, 736776

-

2.4.2.1

deoxyadenosine + phosphate = alpha-D-ribose 1-phosphate + adenine

489660, 489711, 489670, 489703, 489688, 489661, 489669, 489668, 489671, 489672

-

2.4.2.28

2'-deoxyadenosine + phosphate = adenine + 2'-deoxy-D-ribose 1-phosphate

760012

-

2.4.2.28

2'-deoxyadenosine + phosphate = adenine + 2-deoxy-D-ribose 1-phosphate

637534, 637545, 637533

-

2.4.2.28

deoxyadenosine + phosphate = adenine + deoxy-D-ribose 1-phosphate

736501

-

2.4.2.6

2'-deoxyadenosine + 5-chlorouracil = 2'-deoxy-D-ribosyl-5-chlorouracil + adenine

673396, 721340, 721371

1s2g, 3D-view

2.4.2.6

2'-deoxyadenosine + 5-fluorouracil = 2'-deoxy-5-fluorouridine + adenine

673396

1s2g, 3D-view

2.4.2.6

2'-deoxyadenosine + 5-fluorouracil = 2'-deoxy-D-ribosyl-5-fluorouracil + adenine

722820

1s2g, 3D-view

2.4.2.6

2'-deoxyadenosine + cytosine = 2'-deoxycytidine + adenine

705990, 721371

1s2g, 3D-view

2.4.2.6

2'-deoxyadenosine + guanine = 2'-deoxyguanosine + adenine

758681, 759065

1s2g, 3D-view

2.4.2.6

2'-deoxyadenosine + hypoxanthine = 2'-deoxyinosine + adenine

759065

1s2g, 3D-view

2.4.2.6

2'-deoxyadenosine + thymine = 2'-deoxythymidine + adenine

705990

1s2g, 3D-view

2.4.2.6

5-fluorouracil + 2'-deoxyadenosine = 5-fluoro-2'-deoxyuridine + adenine

758927

1s2g, 3D-view

2.4.2.6

5-iodouracil + 2'-deoxyadenosine = 5-iodo-2'-deoxyuridine + adenine

758927

1s2g, 3D-view

2.4.2.6

cytosine + deoxyadenosine = deoxycytidine + adenine

691053

1s2g, 3D-view

2.4.2.6

deoxyadenosine + 2-amino 6-methylmercaptopurine = adenine + 9-(2-deoxy-beta-D-ribofuranosyl)-2-amino-6-methylmercaptopurine

638050

1s2g, 3D-view

2.4.2.6

deoxyadenosine + 2-amino-6-hydroxy 8-mercaptopurine = adenine + ?

638050

1s2g, 3D-view

2.4.2.6

deoxyadenosine + 2-aminobenzimidazole = adenine + ?

638050

1s2g, 3D-view

2.4.2.6

deoxyadenosine + 2-hydroxybenzimidazole = adenine + ?

638050

1s2g, 3D-view

2.4.2.6

deoxyadenosine + 2-thiouracil = adenine + deoxy-2-thiouridine

638050

1s2g, 3D-view

2.4.2.6

deoxyadenosine + 4-amino-5-imidazole carboxamide = adenine + ?

638050

1s2g, 3D-view

2.4.2.6

deoxyadenosine + 5-fluorouracil = adenine + deoxy-5-fluorouridine

638050

1s2g, 3D-view

2.4.2.6

deoxyadenosine + 5-iodouracil = adenine + deoxy-5-iodouridine

638050

1s2g, 3D-view

2.4.2.6

deoxyadenosine + 6-azathymine = adenine + deoxy-6-deazathymidine

638050

1s2g, 3D-view

2.4.2.6

deoxyadenosine + 6-chloroguanine = adenine + 2'-deoxy-6-chloroguanosine

638050

1s2g, 3D-view

2.4.2.6

deoxyadenosine + 6-chloropurine = adenine + 9-(2-deoxy-beta-D-ribofuranosyl)-6-chloropurine

638050

1s2g, 3D-view

2.4.2.6

deoxyadenosine + 6-dimethylaminopurine = adenine + 9-(2-deoxy-beta-D-ribofuranosyl)-6-dimethylaminopurine

638050

1s2g, 3D-view

2.4.2.6

deoxyadenosine + 6-methylpurine = adenine + 9-(2-deoxy-beta-D-ribofuranosyl)-6-methylpurine

638050

1s2g, 3D-view

2.4.2.6

deoxyadenosine + adenine = adenine + deoxyadenosine

638045

1s2g, 3D-view

2.4.2.6

deoxyadenosine + cytosine = adenine + deoxycytidine

638040, 638045, 638051

1s2g, 3D-view

2.4.2.6

deoxyadenosine + ethyl 4-amino-1H-imidazole-5-carboxylate = adenine + ethyl 4-amino-1-(2-deoxy-b-D-erythro-pentofuranosyl)-1H-imidazole-5-carboxylate

638050

1s2g, 3D-view

2.4.2.6

deoxyadenosine + hypoxanthine = adenine + deoxyinosine + 7-(beta-D-2'-deoxyribufuranosyl)hypoxanthine

638041, 638040

1s2g, 3D-view

2.4.2.6

deoxyadenosine + thymine = adenine + thymidine

638040

1s2g, 3D-view

2.4.2.6

deoxyadenosine + uracil = adenine + deoxyuridine

638040

1s2g, 3D-view

2.4.2.6

deoxyadenosine + xanthine = adenine + deoxyxanthosine

638040

1s2g, 3D-view

2.4.2.6

hypoxanthine + deoxyadenosine = deoxyinosine + adenine

691053

1s2g, 3D-view

2.4.2.6

thymine + deoxyadenosine = thymidine + adenine

691053

1s2g, 3D-view

2.4.2.6

uracil + deoxyadenosine = deoxyuridine + adenine

691053

1s2g, 3D-view

2.4.2.1

3 entries

2.4.2.28

3 entries

2.4.2.6

33 entries

2.7.1.11

ADP + 2'-deoxyadenosine = AMP + ?

761560

-

2.7.1.113

ATP + 2'-deoxyadenosine = ADP + 2'-deoxyadenosine 5'-phosphate

661034, 661728, 662882, 671890, 661453, 661731, 663023

-

2.7.1.113

GTP + 2'-deoxyadenosine = GDP + 2'-deoxyadenosine 5'-phosphate

640561

-

2.7.1.113

UTP + 2'-deoxyadenosine = UDP + 2'-deoxyadenosine 5'-phosphate

661453, 663023

-

2.7.1.113

ATP + deoxyadenosine = ADP + dAMP

762058, 640555, 640553, 640561, 640558, 675444

-

2.7.1.145

2'-deoxy-2'-fluoroadenosine 3'-triphosphate + 2'-deoxyadenosine = 2'-deoxy-2'-fluoroadenosine 3'-diphosphate + 2'-deoxyadenosine 5'-phosphate

662985

-

2.7.1.145

2'-deoxyadenosine + ATP = 2'-deoxyadenosine 5'-phosphate + ADP

636844, 675450, 636842, 636840, 636839, 694476

-

2.7.1.145

adenosine-2'-deoxy-3'-triphosphate + 2'-deoxyadenosine = adenosine-2'-deoxy-3'-diphosphate + 2'-deoxyadenosine 5'-phosphate

662985

-

2.7.1.145

adenosine-3'-deoxy-2'-triphosphate + 2'-deoxyadenosine = adenosine-3'-deoxy-2'-diphosphate + 2'-deoxyadenosine 5'-phosphate

662985

-

2.7.1.145

ATP + 2'-deoxyadenosine = ADP + 2'-deoxyadenosine 5'-phosphate

660855, 661583, 661629, 661702, 662985, 662967, 738781, 661072, 661453, 662607, 662990

-

2.7.1.146

ADP + 2'-deoxyadenosine = AMP + ?

761560

-

2.7.1.146

ADP + 2'-deoxyadenosine = AMP + dAMP

761560

-

2.7.1.20

ATP + 2'-deoxy-adenosine = ?

641084, 685030

-

2.7.1.20

ATP + 2'-deoxy-adenosine = ADP + 2'-deoxy-AMP

641083, 641084, 641089, 641090, 641091, 641092, 641115, 641086, 641078, 671849, 685030

-

2.7.1.20

ATP + deoxyadenosine = ADP + deoxyadenosine 5'-phosphate

687787

-

2.7.1.113

4 entries

2.7.1.145

5 entries

2.7.1.146

2 entries

2.7.1.20

3 entries

2.7.1.21

ATP + deoxyadenosine = ADP + dAMP

722758

-

2.7.1.74

ATP + 2'-deoxyadenosine = ADP + 2'-deoxyadenosine 5'-phosphate

662988, 704730, 661453, 661731, 663023, 672137, 690954, 692364, 693554, 702271, 674748, 671911

2zi3, 3D-view

2.7.1.74

ATP + 2'-deoxyadenosine = ADP + 2'-deoxyadenosine 5'-phosphate

662988, 704730, 661453, 661731, 663023, 672137, 690954, 692364, 693554, 702271, 674748, 671911

2zi6, 3D-view

2.7.1.74

NTP + 2'-deoxyadenosine = NDP + 2'-deoxyadenosine 5'-phosphate

671043, 672149

2zi3, 3D-view

2.7.1.74

NTP + 2'-deoxyadenosine = NDP + 2'-deoxyadenosine 5'-phosphate

671043, 672149

2zi6, 3D-view

2.7.1.74

UTP + 2'-deoxyadenosine = UDP + 2'-deoxyadenosine 5'-phosphate

662988, 661453, 663023, 693554, 674748, 671911

2zi3, 3D-view

2.7.1.74

UTP + 2'-deoxyadenosine = UDP + 2'-deoxyadenosine 5'-phosphate

662988, 661453, 663023, 693554, 674748, 671911

2zi6, 3D-view

2.7.1.74

ATP + deoxyadenosine = ADP + dAMP

723029, 721556, 722913, 737347, 762058

2zi3, 3D-view

2.7.1.74

ATP + deoxyadenosine = ADP + dAMP

723029, 721556, 722913, 737347, 762058

2zi6, 3D-view

2.7.1.74

NTP + deoxyadenosine = NDP + dAMP

641953, 722221, 641079, 641937, 641941, 641942, 641943, 641944, 641947, 641965, 641967, 641931, 641936, 640566, 641950, 641938

2zi3, 3D-view

2.7.1.74

NTP + deoxyadenosine = NDP + dAMP

641953, 722221, 641079, 641937, 641941, 641942, 641943, 641944, 641947, 641965, 641967, 641931, 641936, 640566, 641950, 641938

2zi6, 3D-view

2.7.1.74

UTP + deoxyadenosine = UDP + dAMP

721556, 722913, 737347

2zi3, 3D-view

2.7.1.74

UTP + deoxyadenosine = UDP + dAMP

721556, 722913, 737347

2zi6, 3D-view

2.7.1.76

2'-deoxyadenosine-3'-fluoro-3'-triphosphate + 2'-deoxyadenosine = 2'-deoxyadenosine-3'-fluoro-3'-diphosphate + 2'-deoxyadenosine 5'-phosphate

662985

-

2.7.1.76

2'-deoxyadenosine-3'-fluoroara-3'-triphosphate + 2'-deoxyadenosine = 2'-deoxyadenosine-3'-fluoroara-3'-diphosphate + 2'-deoxyadenosine 5'-phosphate

662985

-

2.7.1.76

2'-deoxyadenosine-3'-triphosphate + 2'-deoxyadenosine = 2'-deoxyadenosine-3'-diphosphate + 2'-deoxyadenosine 5'-phosphate

662985

-

2.7.1.76

3'-deoxyadenosine 2'-triphosphate + 2'-deoxyadenosine = 3'-deoxyadenosine-2'-diphosphate + 2'-deoxyadenosine 5'-phosphate

662985

-

2.7.1.76

3'-deoxyadenosine-3'-fluoro-2'-triphosphate + 2'-deoxyadenosine = 3'-deoxyadenosine-3'-fluoro-2'-diphosphate + 2'-deoxyadenosine 5'-phosphate

662985

-

2.7.1.76

3'-deoxyadenosine-3'-fluoroxylo-2'-triphosphate + 2'-deoxyadenosine = 3'-deoxyadenosine-3'-fluoroxylo-2'-diphosphate + 2'-deoxyadenosine 5'-phosphate

662985

-

2.7.1.76

ATP + 2'-deoxyadenosine = ADP + 2'-deoxyadenosine 5'-phosphate

662985, 660855, 675444, 674219, 690459, 675428

-

2.7.1.76

ATP + 2'-deoxyadenosine = ADP + dAMP

739204, 759008, 759073, 640565

-

2.7.1.76

CTP + 2'-deoxyadenosine = CDP + 2'-deoxyadenosine 5'-phosphate

675444

-

2.7.1.76

GTP + 2'-deoxyadenosine = GDP + 2'-deoxyadenosine 5'-phosphate

640561, 675444

-

2.7.1.76

UTP + 2'-deoxyadenosine = UDP + 2'-deoxyadenosine 5'-phosphate

675444

-

2.7.1.76

ATP + deoxyadenosine = ADP + 5'-dAMP

641937, 641977, 640567, 641984

-

2.7.1.76

ATP + deoxyadenosine = ADP + dAMP

641984, 641937, 641089, 641977, 641981, 676722, 641988, 641980, 672159, 640567, 674219, 675444, 675428, 641974, 641976, 641950, 641987, 640566

-

2.7.1.76

CTP + deoxyadenosine = CDP + dAMP

641988, 672159, 675428

-

2.7.1.76

dATP + deoxyadenosine = dADP + dAMP

675428

-

2.7.1.76

dCTP + deoxyadenosine = dCDP + dAMP

675428

-

2.7.1.76

dTTP + deoxyadenosine = dTDP + dAMP

641981, 675428

-

2.7.1.76

GTP + deoxyadenosine = GDP + dAMP

641981, 641988

-

2.7.1.76

TTP + deoxyadenosine = TDP + dAMP

641988, 672159

-

2.7.1.76

UTP + deoxyadenosine = UDP + dAMP

641988, 672159, 641981, 675428

-

2.7.1.77

4-nitrophenyl phosphate + 2'-deoxyadenosine = 2'-deoxyadenosine 5'-phosphate + 2'-deoxyadenosine 3'-phosphate + 4-nitrophenol

642003, 641993

-

2.7.1.77

4-nitrophenyl phosphate + 2'-deoxyadenosine = 4-nitrophenol + 2'-deoxyadenosine 5'-phosphate

641994, 641995

-

2.7.1.77

phenyl phosphate + deoxyadenosine = dAMP + phenol

641990, 641991

-

2.7.1.74

12 entries

2.7.1.76

20 entries

2.7.1.77

3 entries

2.7.1.B20

ATP + 2'-deoxyadenosine = ADP + 2'-deoxyadenosine 5'-phosphate

697882

-

3.1.3.2

p-nitrophenyl phosphate + 2'-deoxyadenosine = ?

134701

-

3.2.2.1

2'-deoxyadenosine + H2O = D-ribose + ?

326380

-

3.2.2.7

2'-deoxyadenosine + H2O = 6-aminopurine + 2-deoxy-D-ribofuranose

137099, 137109, 137102, 137112, 137113, 137111

-

3.2.2.7

2'-deoxyadenosine + H2O = 6-aminopurine + 2-deoxy-D-ribose

752110

-

3.5.4.17

2'-deoxyadenosine + H2O = 2'-deoxyinosine + NH3

246709, 246710, 246708

-

3.5.4.17

deoxyadenosine + H2O = deoxyinosine + NH3

246706

-

3.2.2.7

2 entries

3.5.4.17

2 entries

3.5.4.18

deoxyadenosine + H2O = deoxyinosine + NH3

172176

-

3.5.4.4

2'-deoxyadenosine + H2O = 2'-deoxyinosine + NH3

209637, 209624, 209605, 209615, 209617, 209621, 209622, 209625, 209633, 667870, 667032, 686549, 209619, 209608, 209620, 209635, 719525, 209616, 209623, 720969, 209627, 209628, 209609, 697984, 209630, 686577, 719423, 712583, 700148, 655272, 655265, 686612

3iar, 3D-view

3.5.4.40

2'-deoxyadenosine + H2O = ?

727029

-

Product in Enzyme-catalyzed Reactions (34 results)

top print hide

Show Product (34 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.4.2.1

adenine + deoxyribose 1-phosphate = deoxyadenosine + phosphate

0

-

2.4.2.6

2'-deoxy-D-ribosyl-uracil + adenine = 2'-deoxy-D-ribosyl-adenine + uracil

0

1s2g, 3D-view

2.4.2.6

thymidine + adenine = 2'-deoxy-D-ribosyl-adenine + thymine

0

1s2g, 3D-view

2.4.2.6

2'-deoxycytidine + adenine = 2'-deoxyadenosine + cytosine

0

1s2g, 3D-view

2.4.2.6

2'-deoxycytidine + adenosine = 2'-deoxyadenosine + cytosine

0

1s2g, 3D-view

2.4.2.6

2'-deoxyguanosine + adenine = 2'-deoxyadenosine + guanine

0

1s2g, 3D-view

2.4.2.6

2'-deoxyinosine + adenine = 2'-deoxyadenosine + hypoxanthine

0

1s2g, 3D-view

2.4.2.6

2'-deoxythymidine + adenine = 2'-deoxyadenosine + thymine

0

1s2g, 3D-view

2.4.2.6

2'-deoxyuridine + adenine = 2'-deoxyadenosine + uracil

0

1s2g, 3D-view

2.4.2.6

2'-deoxyuridine + adenine = uracil + 2'-deoxyadenosine

0

1s2g, 3D-view

2.4.2.6

2-fluoro-2'-deoxyinosine + adenine = 2'-deoxyadenosine + 2-fluoroinosine

0

1s2g, 3D-view

2.4.2.6

thymidine + adenine = 2'-deoxyadenosine + thymine

0

1s2g, 3D-view

2.4.2.6

thymidine + adenine = thymine + 2'-deoxyadenosine

0, 638048

1s2g, 3D-view

2.4.2.6

adenine + deoxycytidine = deoxyadenosine + cytosine

0

1s2g, 3D-view

2.4.2.6

adenine + deoxyguanosine = deoxyadenosine + guanine

0

1s2g, 3D-view

2.4.2.6

adenine + deoxyinosine = deoxyadenosine + hypoxanthine

0

1s2g, 3D-view

2.4.2.6

adenine + deoxyuridine = deoxyadenosine + uracil

0

1s2g, 3D-view

2.4.2.6

adenine + thymidine = deoxyadenosine + thymine

0

1s2g, 3D-view

2.4.2.6

deoxyadenosine + adenine = adenine + deoxyadenosine

0

1s2g, 3D-view

2.4.2.6

deoxycytidine + adenine = cytosine + deoxyadenosine

0, 638040, 638042

1s2g, 3D-view

2.4.2.6

deoxyguanosine + adenine = guanine + deoxyadenosine

0

1s2g, 3D-view

2.4.2.6

deoxyinosine + adenine = hypoxanthine + deoxyadenosine

638040, 638042, 0

1s2g, 3D-view

2.4.2.6

deoxyuridine + adenine = deoxyadenosine + uracil

0

1s2g, 3D-view

2.4.2.6

22 entries

2.7.4.18

2'-deoxy-adenosine 5'-phosphate + trans-farnesyl diphosphate = 2'-deoxyadenosine + trans-farnesyl triphosphate

0

-

3.1.13.3

dApG + H2O = 2'-deoxyadenosine + GMP

0

-

3.1.3.2

dAMP + H2O = 2'-deoxyadenosine + phosphate

0

-

3.1.3.2

5'-dAMP + H2O = deoxyadenosine + phosphate

0

-

3.1.3.2

dAMP + H2O = deoxyadenosine + phosphate

0

-

3.1.3.5

5'-dAMP + H2O = deoxyadenosine + phosphate

0, 95037, 95074, 95035, 95042, 95045, 95054, 95058, 95051, 95021, 95065, 95028, 95033

-

3.1.3.5

dAMP + H2O = deoxyadenosine + phosphate

652095

-

3.1.3.2

3 entries

3.1.3.5

2 entries

3.1.3.89

5'-dAMP + H2O = deoxyadenosine + phosphate

0

-

3.1.5.B1

dATP + H2O = deoxyadenosine + triphosphate

0

-

3.1.5.B1

dATP + H2O = deoxyadeonsine + triphosphate

0

-

3.1.5.B1

2 entries

3.5.1.11

N6-phenylacetyl-2'-deoxyadenosine + H2O = phenylacetic acid + 2'-deoxyadenosine

650570, 653284

-

Activator in Enzyme-catalyzed Reactions (2 results)

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Show Activating Compound (2 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.7.1.74

activation, deoxycytidine as substrate, mitochondrial isozyme

641938

2zi3, 3D-view

2.7.1.74

activation, deoxycytidine as substrate, mitochondrial isozyme

641938

2zi6, 3D-view

2.7.1.74

2 entries

Inhibitor in Enzyme-catalyzed Reactions (44 results)

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Show Inhibitors (44 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.1.1.20

-

657792

-

2.4.2.1

-

489693

-

2.4.2.4

20% inactivation at 1 mM

638450

-

2.4.2.6

-

638042

1s2g, 3D-view

2.4.2.6

linear competitive inhibition of deoxycytidine

638045

1s2g, 3D-view

2.4.2.6

linear competitive inhibition of deoxyinosine and linear non-competitive inhibition of adenine

638044

1s2g, 3D-view

2.4.2.6

3 entries

2.5.1.17

weak inhibition

659058

-

2.7.1.113

-

640553

-

2.7.1.113

0.07 mM, 9% inhibition

640549

-

2.7.1.113

weak inhibition

640552

-

2.7.1.113

3 entries

2.7.1.145

reaction with thymidine or 2'-deoxyguanosine

636840

-

2.7.1.20

10-90% inhibition at 0.1 mM

685030

-

2.7.1.20

-

671849

-

2.7.1.20

no inhibition

641106

-

2.7.1.20

substrate inhibition

641083

-

2.7.1.20

-

641096, 641097

-

2.7.1.74

-

641079

2zi3, 3D-view

2.7.1.74

-

641079

2zi6, 3D-view

2.7.1.74

cytosine arabinoside or deoxyguanosine as substrate

641931

2zi3, 3D-view

2.7.1.74

cytosine arabinoside or deoxyguanosine as substrate

641931

2zi6, 3D-view

2.7.1.74

cytosolic isozyme I, weak

641938

2zi3, 3D-view

2.7.1.74

cytosolic isozyme I, weak

641938

2zi6, 3D-view

2.7.1.74

cytosolic isozyme I, weak; deoxycytidine; kinetics

641950

2zi3, 3D-view

2.7.1.74

cytosolic isozyme I, weak; deoxycytidine; kinetics

641950

2zi6, 3D-view

2.7.1.74

deoxycytidine

641942, 641943

2zi3, 3D-view

2.7.1.74

deoxycytidine

641942, 641943

2zi6, 3D-view

2.7.1.74

not

641930

2zi3, 3D-view

2.7.1.74

not

641930

2zi6, 3D-view

2.7.1.20

5 entries

2.7.1.74

12 entries

2.7.1.76

substrate ribavirin

641976

-

3.1.3.5

-

95051

-

3.13.2.1

-

137125, 137126, 137127, 137142, 137144, 137145, 137147

-

3.13.2.1

irreversible

137121

-

3.13.2.1

reversible

137126

-

3.13.2.1

time course of PaSAHase inactivation by 2'-deoxyadenosine, influence of K+ and Rb+ ions, overview

755488

-

3.13.2.1

-

137137

-

3.13.2.1

5 entries

3.2.2.1

-

137116, 714225

-

3.2.2.7

Ki: 0.05 mM

137111

-

3.2.2.7

one third inhibition at 0.5 mM

137107

-

3.5.4.5

-

209661

-

3.5.4.5

3.0 mM, 32% inhibition

209644

-

3.5.4.5

competitive inhibition

209655, 209658, 209660

-

3.2.2.7

2 entries

3.5.4.5

3 entries

4.6.1.1

-

34760, 34796, 715176

-

4.6.1.19

-

134494

-

6.3.5.2

-

1362

-

3D Structure of Enzyme-Ligand-Complex (PDB) (22 results)

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Show 3D Structure of Enzyme-Ligand-Complex (PDB) (22 entries)

EC NUMBER

ENZYME 3D STRUCTURE

2.3.2.6

2z3m, 3D-view

2.4.2.6

1s2g, 3D-view

2.5.1.63

2c5h, 3D-view

2.7.1.74

2zi3, 3D-view

2.7.1.74

2zi6, 3D-view

2.7.1.74

2zi3, 3D-view

2.7.1.74

2zi6, 3D-view

2.7.1.74

2zi3, 3D-view

2.7.1.74

2zi6, 3D-view

2.7.1.74

2zi3, 3D-view

2.7.1.74

2zi6, 3D-view

2.7.1.74

2zi3, 3D-view

2.7.1.74

2zi6, 3D-view

2.7.1.74

2zi3, 3D-view

2.7.1.74

2zi6, 3D-view

2.7.1.74

2zi3, 3D-view

2.7.1.74

2zi6, 3D-view

2.7.1.74

2zi3, 3D-view

2.7.1.74

2zi6, 3D-view

2.7.1.74

16 entries

2.7.7.7

3si8, 3D-view

3.3.1.1

5m67, 3D-view

3.5.4.4

3iar, 3D-view

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (62 results)

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Show Turnover Number (62 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

2.4.2.28

9.6

-

at pH 7.4 and 37°C

736501

2.4.2.28

48.44

-

mutant enzyme S12T, at pH 7.4 and 25°C

760012

2.4.2.28

80.03

-

mutant enzyme Q289L, at pH 7.4 and 25°C

760012

2.4.2.28

224.3

-

wild type enzyme, at pH 7.4 and 25°C

760012

2.4.2.28

299.2

-

mutant enzyme S12T/N87T/Q289L, at pH 7.4 and 25°C

760012

2.4.2.28

372.8

-

mutant enzyme S12T/N87T, at pH 7.4 and 25°C

760012

2.4.2.28

441.2

-

mutant enzyme N87T, at pH 7.4 and 25°C

760012

2.7.1.113

0.0047

-

-

675444

2.7.1.113

0.3

-

at pH 8.0, temperature not specified in the publication

762058

2.7.1.145

0.021

-

pH 8.0, recombinant enzyme

662967

2.7.1.145

0.084

-

recombinant mutant A110D

661583

2.7.1.145

0.4

-

recombinant mutant N64D

661702

2.7.1.145

0.828

-

mutant enzyme N45D/N64D

636844

2.7.1.145

1.1

-

recombinant mutant V84S

661583

2.7.1.145

1.36

-

recombinant mutant V84M

661583

2.7.1.145

1.83

-

recombinant mutant N45D

661702

2.7.1.145

1.88

-

recombinant mutant M88R

661583

2.7.1.145

3.2

-

recombinant mutant V84S/M88R/A110D

661583

2.7.1.145

3.5

-

recombinant mutant V84A/M88R/A110D

661583

2.7.1.145

3.7

-

recombinant mutant V84A

661583

2.7.1.145

6.9

-

recombinant mutant M88R/A110D

661583

2.7.1.145

18

19

pH 8.0, 22°C

636840

2.7.1.145

20.6

-

pH 7.8, 22°C, recombinant enzyme

636844, 636842

2.7.1.145

20.6

-

recombinant wild-type enzyme

661583

2.7.1.20

1

-

25fold reduction

641115

2.7.1.20

4.2

-

pH 7.6, 37°C

687787

2.7.1.20

5.25

-

wild-type enzyme

671849

2.4.2.28

7 entries

2.7.1.113

2 entries

2.7.1.145

15 entries

2.7.1.20

3 entries

2.7.1.21

0.047

-

full-length enzyme, at pH 7.8 and 37°C

722758

2.7.1.74

0.31

-

residues 65-79 deletion mutant with UTP as cosubstrate

672149

2.7.1.74

0.33

-

wild type enzyme with UTP as cosubstrate

672149

2.7.1.74

0.37

-

cosubstrate UTP, pH 7.5, 37°C

693554

2.7.1.74

0.69

-

mutant S74E, pH 7.5, 25°C

692364

2.7.1.74

0.77

-

wild-type, pH 7.5, 25°C

692364

2.7.1.74

0.9

-

mutant S74Q, pH 7.5, 25°C

692364

2.7.1.74

1

-

mutant S74D, pH 7.5, 25°C

692364

2.7.1.74

1.08

-

mutant D47E/R104Q/D133G/N163I/F242L, pH 7.5, 30°C

690954

2.7.1.74

1.12

-

mutant S74A, pH 7.5, 25°C

692364

2.7.1.74

1.7

-

wild type enzyme with ATP as cosubstrate

672149

2.7.1.74

1.75

-

mutant R104Q/D133G, pH 7.5, 30°C

690954

2.7.1.74

2

-

mutant R104Q/D133N, pH 7.5, 30°C

690954

2.7.1.74

2.1

-

cosubstrate ATP, pH 7.5, 37°C

693554

2.7.1.74

2.13

-

wild type enzyme, in 100 mM Tris, pH 7.5, 100 mM KCl, 10 mM MgCl2 and 1 mM ATP, at 37°C

702271

2.7.1.74

2.67

-

mutant A100V/R104M/D133T, pH 7.5, 37°C

690954

2.7.1.74

2.71

-

mutant R104M/D133A, pH 7.5, 37°C

690954

2.7.1.74

2.73

-

at pH 8.0, temperature not specified in the publication

762058

2.7.1.74

2.8

-

residues 65-79 deletion mutant with ATP as cosubstrate

672149

2.7.1.74

3.1

-

wild-type, pH 7.5, 30°C

690954

2.7.1.74

3.1

-

wild-type, pH 7.5, 37°C

690954

2.7.1.74

3.37

-

mutant A100V/R104M/D133S, pH 7.5, 37°C

690954

2.7.1.74

3.4

-

mutant A100V/R104M/D133A, pH 7.5, 37°C

690954

2.7.1.74

3.47

-

mutant R104M/D133N, pH 7.5, 37°C

690954

2.7.1.74

4.07

-

at pH 8.0, temperature not specified in the publication

762058

2.7.1.74

4.14

-

mutant R104M/D133T, pH 7.5, 37°C

690954

2.7.1.74

4.51

-

mutant enzyme R104M/D133A, in 100 mM Tris, pH 7.5, 100 mM KCl, 10 mM MgCl2 and 1 mM ATP, at 37°C

702271

2.7.1.74

4.85

-

mutant R104M/D133S, pH 7.5, 37°C

690954

2.7.1.74

5.72

-

mutant enzyme R104L/D133A, in 100 mM Tris, pH 7.5, 100 mM KCl, 10 mM MgCl2 and 1 mM ATP, at 37°C

702271

2.7.1.76

1.22

-

in 50 mM Tris/HCl, pH 8.0, 10 mM dithiothreitol, 2.5 mM ATP, 2.5 mM MgCl2, 3 mg/ml of bovine serum albumin and 0.5 mM CHAPS

674219

2.7.1.76

1.48

-

pH 7.6, 37°C, recombinant enzyme

641988

2.7.1.76

1.82

-

pH 8.0

690459

2.7.1.76

3.7

-

-

675444

2.7.1.76

3.7

-

-

675444

2.7.1.74

28 entries

2.7.1.76

5 entries

3.5.4.40

0.72

-

wild type enzyme, at pH 7.5 and at 30°C

727029

K_M Value (130 results)

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Show KM Value (130 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.3.39

0.02

-

-

287628

2.4.2.1

0.145

-

-

489670

2.4.2.1

0.19

-

-

489672

2.4.2.28

0.00099

-

mutant enzyme S12T, at pH 7.4 and 25°C

760012

2.4.2.28

0.00302

-

mutant enzyme Q289L, at pH 7.4 and 25°C

760012

2.4.2.28

0.00389

-

mutant enzyme S12T/N87T, at pH 7.4 and 25°C

760012

2.4.2.28

0.00397

-

wild type enzyme, at pH 7.4 and 25°C

760012

2.4.2.28

0.00652

-

mutant enzyme S12T/N87T/Q289L, at pH 7.4 and 25°C

760012

2.4.2.28

0.0083

-

at pH 7.4 and 37°C

736501

2.4.2.28

0.01033

-

mutant enzyme N87T, at pH 7.4 and 25°C

760012

2.4.2.6

0.092

-

reaction with adenine

638045

2.4.2.6

0.1

-

reaction with cytosine

638051

2.4.2.6

0.12

-

-

638042

2.4.2.6

0.12

-

reaction with cytosine

638045

2.4.2.6

0.45

-

-

638042

2.7.1.113

0.0026

-

patient with double mutation N46S/L266, pH 7.4, 37°C

671890

2.7.1.113

0.0035

-

father (L266R), pH 7.4, 37°C

671890

2.7.1.113

0.0041

-

brother (N46S), pH 7.4, 37°C

671890

2.7.1.113

0.0053

-

mother (N46S), pH 7.4, 37°C

671890

2.7.1.113

0.0068

-

control group, pH 7.4, 37°C

671890

2.7.1.113

0.206

-

-

675444

2.7.1.113

0.414

-

pH 7.6, recombinant mutant E227K

661728

2.7.1.113

0.467

-

pH 7.6, recombinant wild-type enzyme

661728

2.7.1.113

0.467

-

pH 7.6, wild-type enzyme

662882

2.7.1.113

0.47

-

pH 7.6, recombinant mitochondrial deoxyguanosine kinase

640555

2.7.1.113

0.5

-

pH 7.6, mutant L250S

662882

2.7.1.113

0.63

-

pH 6.0, 37°C

640553

2.7.1.113

2.689

-

at pH 8.0, temperature not specified in the publication

762058

2.7.1.145

0.0181

-

pH 8.0, recombinant enzyme

662967

2.7.1.145

0.109

-

pH 8.0, 22°C

636840

2.7.1.145

0.119

-

recombinant mutant N45D

661702

2.7.1.145

0.15

-

recombinant mutant V84S

661583

2.7.1.145

0.153

-

recombinant mutant V84A/M88R/A110D

661583

2.7.1.145

0.225

-

pH 7.8, 22°C, recombinant enzyme

636842

2.7.1.145

0.225

-

recombinant wild-type enzyme

661583

2.7.1.145

0.239

-

recombinant mutant A110D

661583

2.7.1.145

0.36

-

recombinant mutant M88R/A110D

661583

2.7.1.145

0.373

-

pH 7.6, 37°C, recombinant wild-type enzyme

661629

2.7.1.145

0.373

-

pH 8, 37°C

636841

2.7.1.145

0.388

-

recombinant mutant V84S/M88R/A110D

661583

2.7.1.145

0.501

-

-

662607

2.7.1.145

0.625

-

pH 7.6, 37°C, recombinant mutant Q81N

661629

2.7.1.145

0.7

-

recombinant mutant V84A

661583

2.7.1.145

0.852

-

recombinant mutant V84M

661583

2.7.1.145

2.088

-

recombinant mutant M88R

661583

2.7.1.145

2.1

-

-

662607

2.7.1.145

3.16

-

mutant enzyme N45D/N64D

636844

2.7.1.145

3.82

-

recombinant mutant N64D

661702

2.7.1.20

0.077

-

wild-type enzyme

671849

2.7.1.20

0.11

-

pH 7.6, 37°C

687787

2.7.1.20

0.18

-

pH 5.8, 25ºC

641078

2.7.1.20

0.36

0.67

-

641089

2.7.1.20

0.36

0.67

pH 7.5, 30ºC

641090

2.7.1.20

0.36

0.67

-

641084

2.7.1.20

0.66

-

pH 8.0, 37ºC

641115

2.4.2.1

2 entries

2.4.2.28

7 entries

2.4.2.6

5 entries

2.7.1.113

13 entries

2.7.1.145

20 entries

2.7.1.20

7 entries

2.7.1.21

8.4

-

full-length enzyme, at pH 7.8 and 37°C

722758

2.7.1.74

0.0085

-

cosubstrate UTP, pH 7.5, 37°C

693554

2.7.1.74

0.013

-

wild type enzyme with UTP as cosubstrate

672149

2.7.1.74

0.019

-

cosubstrate UTP, 37°C, pH 7.6

641953

2.7.1.74

0.053

-

residues 65-79 deletion mutant with UTP as cosubstrate

672149

2.7.1.74

0.081

-

wild-type, pH 7.5, 30°C

690954

2.7.1.74

0.081

-

wild-type, pH 7.5, 37°C

690954

2.7.1.74

0.091

-

mutant D47E/R104Q/D133G/N163I/F242L, pH 7.5, 30°C

690954

2.7.1.74

0.093

-

at pH 8.0, temperature not specified in the publication

762058

2.7.1.74

0.1

-

wild type enzyme with ATP as cosubstrate

672149

2.7.1.74

0.1146

-

wild type enzyme, in 100 mM Tris, pH 7.5, 100 mM KCl, 10 mM MgCl2 and 1 mM ATP, at 37°C

702271

2.7.1.74

0.115

-

cosubstrate ATP, pH 7.5, 37°C

693554

2.7.1.74

0.1169

-

wild-type, pH 7.5, 25°C

692364

2.7.1.74

0.12

-

pH 8.0, 37°C

641943

2.7.1.74

0.15

-

cosubstrate UTP, 37°C, pH 7.6

641953

2.7.1.74

0.15

-

pH 8.0

641079

2.7.1.74

0.1623

-

mutant enzyme R104L/D133A, in 100 mM Tris, pH 7.5, 100 mM KCl, 10 mM MgCl2 and 1 mM ATP, at 37°C

702271

2.7.1.74

0.231

-

mutant R104Q/D133G, pH 7.5, 30°C

690954

2.7.1.74

0.398

-

mutant R104M/D133S, pH 7.5, 37°C

690954

2.7.1.74

0.412

-

mutant R104M/D133A, pH 7.5, 37°C

690954

2.7.1.74

0.415

-

residues 65-79 deletion mutant with ATP as cosubstrate

672149

2.7.1.74

0.452

-

mutant R104M/D133N, pH 7.5, 37°C

690954

2.7.1.74

0.48

-

cosubstrate ATP, 37°C, pH 7.6

641953

2.7.1.74

0.5

-

37°C, pH 7.0

641941, 641942

2.7.1.74

0.518

-

mutant S74E, pH 7.5, 25°C

692364

2.7.1.74

0.532

-

mutant R104Q/D133N, pH 7.5, 30°C

690954

2.7.1.74

0.55

-

cosubstrate ATP, 37°C, pH 7.6

641953

2.7.1.74

0.553

-

at pH 8.0, temperature not specified in the publication

762058

2.7.1.74

0.598

-

mutant A100V/R104M/D133A, pH 7.5, 37°C

690954

2.7.1.74

0.691

-

mutant R104M/D133T, pH 7.5, 37°C

690954

2.7.1.74

0.843

-

mutant A100V/R104M/D133S, pH 7.5, 37°C

690954

2.7.1.74

0.89

-

37°C, pH 7.5

641944

2.7.1.74

1.04

-

mutant enzyme R104M/D133A, in 100 mM Tris, pH 7.5, 100 mM KCl, 10 mM MgCl2 and 1 mM ATP, at 37°C

702271

2.7.1.74

1.437

-

mutant A100V/R104M/D133T, pH 7.5, 37°C

690954

2.7.1.76

0.0028

-

pH 8.0, 20°C, recombinant dAK

640565

2.7.1.76

0.0049

-

pH 7.4, 37°C, CCRF-CEM leukemia cells

641987

2.7.1.76

0.0075

-

pH 8.0, 20°C, R79K mutant dAK

640565

2.7.1.76

0.01

-

with ATP as phosphoryl donor, at room temperature in 0.01 M HEPES (pH 7.4) containing 0.15 M NaCl and 0.002 M MgCl2

672159

2.7.1.76

0.012

-

pH 7.6, 37°C, recombinant enzyme

641988

2.7.1.76

0.018

-

with CTP as phosphoryl donor, at room temperature in 0.01 M HEPES (pH 7.4) containing 0.15 M NaCl and 0.002 M MgCl2

672159

2.7.1.76

0.0227

-

-

675444

2.7.1.76

0.0227

-

-

675444

2.7.1.76

0.029

-

pH 7.4, 37°C, erythrocyte

641987

2.7.1.76

0.0292

-

pH 8.0

690459

2.7.1.76

0.0332

-

-

674219

2.7.1.76

0.0332

-

in 50 mM Tris/HCl, pH 8.0, 10 mM dithiothreitol, 2.5 mM ATP, 2.5 mM MgCl2, 3 mg/ml of bovine serum albumin and 0.5 mM CHAPS

674219

2.7.1.76

0.5

-

pH 7.5, 37°C

641976

2.7.1.76

5

-

pH 7.8, 37°C

641974

2.7.1.77

0.0059

-

pH 7.5, 37°C, reaction with 4-nitrophenyl phosphate

642003

2.7.1.77

0.087

-

pH 5.0, reaction with AMP

641994

2.7.1.74

33 entries

2.7.1.76

14 entries

2.7.1.77

2 entries

2.7.1.B20

1.1

-

pH 7.0, 37°C

697882

3.2.2.1

0.042

-

-

326380

3.2.2.7

0.12

-

in MES buffer, pH 5.4

137111

3.5.4.17

0.071

-

-

246708

3.5.4.17

0.27

-

pH 4.0, at 25°C

246710

3.5.4.4

0.004

-

-

209608

3.5.4.4

0.016

-

-

209637

3.5.4.4

0.034

-

-

209622

3.5.4.4

0.034

-

pH 7.4, 37°C

719423

3.5.4.4

0.039

-

kidney cortex large isozyme

667032

3.5.4.4

0.04

-

-

209624

3.5.4.4

0.04

-

pleural fluid large isozyme

667032

3.5.4.4

0.042

-

blood serum large isozyme

667032

3.5.4.4

0.05

0.07

-

209621

3.5.4.4

0.052

-

-

209633

3.5.4.4

0.053

-

-

209617

3.5.4.4

0.057

-

-

209617

3.5.4.4

0.135

-

spleen small isozyme

667032

3.5.4.4

0.189

-

lung small isozyme

667032

3.5.4.4

0.2

-

-

209630

3.5.4.4

0.22

-

-

209627

3.5.4.4

0.333

-

-

655272

3.5.4.4

0.4

-

-

209616

3.5.4.4

0.56

-

37°C, pH not specified in the publication

720969

3.5.4.17

2 entries

3.5.4.4

19 entries

3.5.4.40

0.037

-

wild type enzyme, at pH 7.5 and at 30°C

727029

K_i Value (10 results)

top print hide

Show KI Value (10 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.1.1.20

0.38

-

pH 8.6

657792

2.4.2.6

0.092

-

-

638042, 638045

2.4.2.6

0.43

-

-

638042

2.4.2.6

2 entries

2.7.1.113

0.34

-

pH 8.0, 37°C

640552

2.7.1.145

0.02

-

pH 8.0, 22°C, reaction with thymidine

636840

2.7.1.145

0.16

-

pH 8.0, 22°C, reaction with 2'-deoxyguanosine

636840

2.7.1.145

2 entries

2.7.1.20

0.01575

-

wild-type enzyme

671849

2.7.1.76

0.97

-

pH 7.5, 37°C, substrate ribavirin

641976

3.2.2.1

0.182

-

at pH 7.0 and 35°C

714225

3.2.2.7

0.05

-

-

137111

IC₅₀ Value (1 result)

top print hide

Show IC50 Value (1 entry)

EC NUMBER

IC50 VALUE

IC50 VALUE MAXIMUM

COMMENTARY

LITERATURE

4.6.1.1

0.07

-

in 10 mM Tris-HCl pH 7.5, at 30°C

715176

References & Links

Literature References (235)

top print hide

Show Reference (235 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

1362

164459

Guanosine monophosphate synthetase from Escherichia coli B-96. Inhibition by nucleosides

1975

Spector, T.; Beacham III, L.M.

J. Biol. Chem.

250

3101-3107

34760

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Adenylate cyclase form the phytopathogenic fungus Alternaria solani

1985

Jayaswal, R.K.; Bressan, R.A.; Handa, A.K.

FEMS Microbiol. Lett.

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313-318

34796

9346923

The catalytic mechanism of mammalian adenylyl cyclase. Equilibrium binding and kinetic analysis of P-site inhibition

1997

Dessauer, C.W.; Gilman, A.G.

J. Biol. Chem.

272

27787-27795

95021

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Manganese-dependent production, and properties, of 5'-nucleotidase by alkalophilic Bacillus No. A-59

1989

Ikura, Y.; Horikoshi, K.

Agric. Biol. Chem.

53

645-649

95028

2822031

Purification, characterization and cellular localization of 5'-nucleotidase from Torpedo electric organ

1987

Grondal, E.J.M.; Zimmermann, H.

Biochem. J.

245

805-810

95033

-

Purification and properties of 5'-nucleotidase from cod muscle

1986

Yamamoto, H.; Tomioka, K.; Kawai, H.; Endo, K.

Agric. Biol. Chem.

50

1123-1129

95035

3001058

Human placental cytoplasmic 5'-nucleotidase. Kinetic properties and inhibition

1986

Madrid-Marina, V.; Fox, I.H.

J. Biol. Chem.

261

444-452

95037

2986711

Isolation and kinetic properties of 5'-nucleotidase from guinea-pig skeletal muscle

1985

Camici, M.; Fini, C.; Ipata, P.L.

Biochim. Biophys. Acta

840

6-12

95042

6271180

5'-Nucleotidase from rat heart

1981

Naito, Y.; Lowenstein, J.M.

Biochemistry

20

5188-5194

95045

6260203

Purification and some properties of cytosol 5'-nucleotidase from rat liver

1981

Itoh, R.

Biochim. Biophys. Acta

657

402-410

95051

-

A 5'-nucleotidase from Neurospora crassa

1974

Olson, A.C.; Fraser, M.J.

Biochim. Biophys. Acta

334

156-167

95054

-

Nucleotide phosphomonoesterases

1971

Drummond, G.I.; Yamamoto, M.

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

4

337-354

95058

9636049

Nucleotide and nucleoside analogues as inhibitors of cytosolic 5'-nucleotidase I from heart

1998

Garvey, E.P.; Lowen, G.T.; Almond, M.R.

Biochemistry

37

9043-9051

95065

2344353

Partial purification and properties of an AMP-specific 5'-nucleotidase from pigeon heart

1990

Skladanowski, A.C.; Newby, A.C.

Biochem. J.

268

117-122

95074

9675234

Biochemical properties of 5'-nucleotidase from mouse skeletal muscle

1998

Martinez-Martinez, A.; Flores-Flores, C.; Campoy, F.J.; Munoz-Delgado, E.; Fini, C.; Vidal, C.J.

Biochim. Biophys. Acta

1386

16-28

134494

965365

Further studies on the specificity of the minor ribonuclease from Aspergillus saitoi

1976

Irie, M.; Ohgi, K.

J. Biochem.

80

39-43

134701

3049613

Periplasmic nonspecific acid phosphatase II from Salmonella typhimurium LT2. Crystallization, detergent reactivation, and phosphotransferase activity

1988

Uerkvitz, W.

J. Biol. Chem.

263

15823-15830

137099

-

Isolation and characterization of adenosine nucleosidase from yellow lupin (Lupinus luteus)

2000

Abusamhadneh, E.; McDonald, N.E.; Kline, P.C.

Plant Sci.

153

25-32

137102

-

Nucleic acid degrading enzymes of barley malt. III. Adenosine nucleosidase from malted barley

1986

Lee, W.J.; Pyler, R.E.

J. Am. Soc. Brew. Chem.

44

86-90

137107

16662043

Metabolism of cytokinin: Deribosylation of cytokinin ribonucleoside by adenosine nucleosidase from wheat germ cells

1981

Chen, C.M.; Kristopeit, S.M.

Plant Physiol.

68

1020-1023

137109

-

Purification and properties of adenosine nucleosidases from tea leaves

1979

Imagawa, H.; Yamano, H.; Inoue, K.; Takino, Y.

Agric. Biol. Chem.

43

2337-2342

137111

861230

Purification and characterization of adenosine nucleosidase from barley leaves

1977

Guranowski, A.; Schneider, Z.

Biochim. Biophys. Acta

482

145-158

137112

-

Purification and properties of N-ribosyladenine ribohydrolase from potato leaves

1972

Clark, M.C.; Page, O.T.; Fisher, M.G.

Phytochemistry

11

3413-3419

137113

14085386

An adenosine hydrolase from Brussels sprouts

1963

Mazelis, M.; Creveling, R.K.

J. Biol. Chem.

238

3358-3361

137116

468819

Nucleosidases from Leishmania donovani. Pyrimidine ribonucleosidase, purine ribonucleosidase, and a novel purine 2-deoxyribonucleosidase

1979

Koszalka, G.W.; Krenitsky, T.A.

J. Biol. Chem.

254

8185-8193

137121

3657555

Adenosylhomocysteinase (bovine)

1987

Chiang, P.K.

Methods Enzymol.

143

377-383

137125

2987197

Purification and characterization of S-adenosylhomocysteine hydrolase from mouse mastocytoma P-815 cells. Evidence for cell cycle-specific fluctuation of the enzyme activity

1985

Ichikawa, A.; Sato, S.; Tomita, K.

J. Biochem.

97

189-197

137126

6091559

Purification of S-adenosyl-L-homocysteine hydrolase from Dictyostelium discoideum: Reversible inactivation by cAMP and 2 -deoxyadenosine

1984

Hohman, R.J.; Guitton, M.C.; Veron, M.

Arch. Biochem. Biophys.

233

785-795

137127

6428887

Occurrence of S-adenosylhomocysteine hydrolase in prokaryote cells. Characterization of the enzyme from Alcaligenes faecalis and role of the enzyme in the activated methyl cycle

1984

Shimizu, S.; Shiozaki, S.; Ohshiro, T.; Yamada, H.

Eur. J. Biochem.

141

385-392

137137

4562409

Partial purification and characterization of S-adenosylhomocysteine hydrolase isolated from Saccharomyces cerevisiae

1972

Knudsen, R.C.; Yall, I.

J. Bacteriol.

112

569-575

137142

8093102

Effects of novel anti-viral adenosine analogues on the activity of S-adenosylhomocysteine hydrolase from human liver

1994

Fabianowska-Majewska, K.; Duley, J.A.; Simmonds, H.A.

Biochem. Pharmacol.

48

897-903

137144

8874802

Inhibition studies of S-adenosylhomocysteine hydrolase purified from Acinetobacter calcoaceticus ULA-501

1996

Impagnatiello, A.; Franceschini, N.; Oratore, A.; Bozzi, A.

Biochimie

78

267-272

137145

-

Adenosine analogues as inhibitors or inactivators of S-adenosylhomocysteine hydrolase from bovine pancreas

1993

Bozzi, A.; Parisi, M.; Martini, F.

J. Enzyme Inhib.

7

159-167

137147

8871889

S-adenosylhomocysteine-hydrolase from bovine kidney: Enzymatic and binding properties

1996

Kloor, D.; Kurz, J.; Fuchs, S.; Faust, B.; Osswald, H.

Kidney Blood Press. Res.

19

100-108

172176

-

Purine, purine nucleoside, and purine nucleotide aminohydrolases

1971

Zielke, C.L.; Suelter, C.H.

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

4

47-78

209605

4625871

Multiple forms of human adenosine deaminase. 1. Purification and characterization of two molecular species

1972

Akedo, H.; Nishihara, H.; Shinkai, K.; Komatsu, K.; Ishikawa, S.

Biochim. Biophys. Acta

276

257-271

209608

-

Purification and some properties of calf thymus adenosine deaminase

1974

Rossi, C.A.; Lucacchini, A.

Biochem. Soc. Trans.

2

1313-1315

209609

1168529

Purification and some properties of the soluble and membrane-bound adenosine deaminases of Micrococcus sodonensis ATCC 11880 and their distribution within the family Micrococcaceae

1975

Pickard, M.A.

Can. J. Biochem.

53

344-353

209615

3606997

Immunoaffinity purification and fluorescence studies of human adenosine deaminase

1987

Philips, A.V.; Robbins, D.J.; Coleman, M.S.

Biochemistry

26

2893-2903

209616

3096380

Purification, stability and kinetic properties of highly purified adenosine deaminase from Bacillus cereus NCIB 8122

1986

Gabellieri, E.; Bernini, S.; Piras, L.; Cioni, P.; Balestreri, E.; Cercignani, G.; Felicioli, R.

Biochim. Biophys. Acta

884

490-496

209617

6363411

Human malaria parasite adenosine deaminase

1984

Daddona, P.E.; Wiesmann, W.P.; Lambros, C.; Kelley, W.N.; Webster, H.K.

J. Biol. Chem.

259

1472-1475

209619

6815190

Adenosine deaminase from deoxycoformycin-sensitive and -resistent rat hepatoma cells

1982

Hunt, S.W.3rd.; Hoffee, P.A.

J. Biol. Chem.

257

14239-14244

209620

-

A simple conventional method for the purification of bovine spleen adenosine deaminase in high yield: Physical properties

1981

Lewis, A.S.; McCalla, C.; Murphy, L.

J. Appl. Biochem.

3

378-386

209621

6975278

Human adenosine deaminase: Properties and turnover in cultured T and B lymphoblasts

1981

Daddona, P.E.

J. Biol. Chem.

256

12496-12501

209622

6947796

Purification, characterization and radioimmunoassay of adenosine deaminase from human leukaemic granulocytes

1981

Wiginton, D.A.; Coleman, M.S.; Hutton, J.J.

Biochem. J.

195

389-397

209623

7212927

Adenosine deaminase from Azotobacter vinelandii. Purification and properties

1980

Tsukada, T.; Yoshino, M.

Arch. Microbiol.

128

228-232

209624

357905

Adenosine deaminase from Escherichia coli

1978

Nygaard, P.

Methods Enzymol.

51

508-512

209625

1705781

Slight differences between adenosine deaminase from different species. An immunochemical study

1990

Centelles, J.J.; Franco, R.

Arch. Int. Physiol. Biochim.

98

421-431

209627

-

Purification and characterization of extracellular adenosine deaminase from a Streptomyces sp.

1991

Jun, H.K.; Kim, T.S.; Sakai, T.

J. Ferment. Bioeng.

71

6-11

209628

-

Purification and characterization of adenosine deaminase from Klebsiella sp. LF 1202

1991

Ling, F.; Inoue, Y.; Kimura, A.

J. Ferment. Bioeng.

71

89-92

209630

7986382

Purification and charaterization of an extracellular adenosine deaminase from Nocardioides sp. J-326TK

1994

Jun, H.K.; Yeeh, Y.

Biotechnol. Appl. Biochem.

20

265-277

209633

9891839

Inhibition studies on membrane adenosine deaminase from human placenta

1998

Lupidi, G.; Marmocchi, F.; Cristalli, G.

Biochem. Mol. Biol. Int.

46

1071-1080

209635

10666580

Crystallization and preliminary analysis of bovine adenosine deaminase

1999

Kinoshita, T.; Nishio, N.; Sato, A.; Murata, M.

Acta Crystallogr. Sect. D

55

2031-2032

209637

10718633

Purification and characterization of intestinal adenosine deaminase from mice

2000

Singh, L.S.; Sharma, R.

Mol. Cell. Biochem.

204

127-134

209644

4202859

The purification and properties of cytidine deaminase from Escherichia coli

1973

Hosono, H.; Kuno, S.

J. Biochem.

74

797-803

209655

3910086

Cytidine deaminase from Escherichia coli B. Purification and enzymatic and molecular properties

1985

Vita, A.; Amici, A.; Cacciamani, T.; Lanciotti, M.; Magni, G.

Biochemistry

24

6020-6024

209658

-

Further properties of cytidine deaminase and uridine phosphorylase from E. coli B

1986

Vita, A.; Amici, A.; Lanciotti, M.; Cacciamani, T.; Magni, G.

Ital. J. Biochem.

35

145A-147A

209660

-

Purification and properties of Escherichia coli cytidine deaminase by amplification of the cdd gene

1991

Kwon, T.K.; Lee, S.Y.; Kim, J.G.; Song, B.H.; Hong, S.D.

Mol. Cells

1

281-286

209661

1929398

Purification of human cytidine deaminase: Molecular and enzymatic characterization and inhibition by synthetic pyrimidine analogs

1991

Cacciamani, T.; Vita, A.; Cristalli, G.; Vincenzetti, S.; Natalini, P.; Ruggieri, S.; Amici, A.; Magni, G.

Arch. Biochem. Biophys.

290

285-292

246706

5773435

A non-specific adenine nucleotide deaminase from Desulfovibrio desulfuricans

1969

Yates, M.G.

Biochim. Biophys. Acta

171

299-310

246708

-

Distribution of adenosine (phosphate) deaminases with unusual substrate specificity in marine mollusc

1998

Uchida, H.; Chen, Y.X.; Nagai, H.; Fujisaki, Y.; Harihara, K.; Saka, N.; Kugisaki, Y.; Nomura, A.

Comp. Biochem. Physiol. B

119

227-233

246709

-

Recognition of ribose moiety by adenosine (phosphate) deaminase from squid liver

1995

Uchida, H.; Narita, Y.; Masuda, A.; Chen, Y.X.; Nomura, A.

Biosci. Biotechnol. Biochem.

59

2120-2122

246710

-

Purification and some properties of adenosine (phosphate) deaminase from the liver of the squid Todarodes pacificus

1995

Uchida, H.; Narita, Y.; Masuda, A.; Matsui, Y.; Chen, Y.X.; Takahashi, I.; Maeda, S.; Nomura, A.

Biosci. Biotechnol. Biochem.

59

1276-1280

287612

-

Properties of a new enzyme, nucleoside oxidase, from Pseudomonas maltophilia LB-86

1989

Isono, Y.; Sudo, T.; Hoshino, M.

Agric. Biol. Chem.

53

1671-1677

287628

16535726

Nuceloside oxidase, a hydrogen peroxide-forming oxidase, from Flavobacterium meningosepticum

1997

Koga, S.; Ogawa, J.; Cheng, L.Y.; Choi, Y.M.; Yamada, H.; Shimizu, S.

Appl. Environ. Microbiol.

63

4282-4286

326380

8702965

Purine-specific nucleoside N-ribohydrolase from Trypanosoma brucei brucei

1996

Parkin, D.W.

J. Biol. Chem.

271

21713-21719

489660

4570469

Purification and properties of purine nucleoside phosphorylase from Salmonella typhimurium

1973

Robertson, B.C.; Hoffee, P.A.

J. Biol. Chem.

248

2040-2043

489661

99174

Two purine nucleoside phosphorylases in Bacillus subtilis. Purification and some properties of the adenosine-specific phosphorylase

1978

Jensen, K.J.

Biochim. Biophys. Acta

525

346-356

489668

-

Properties of nucleoside phosphorylase from Enterobacter aerogenes

1985

Utagawa, T.; Morisawa, H.; Yamanaka, S.; Yamazaki, A.; Yoshinaga, F.; Hirose, Y.

Agric. Biol. Chem.

49

3239-3246

489669

-

Properties of purine nucleoside phosphorylase from Enterobacter cloacae

1981

Machida, Y.; Nakanishi, T.

Agric. Biol. Chem.

45

1801-1807

489670

7211

Purification and characterization of a purine-nucleoside phosphorylase from bovine thyroid

1976

Moyer, T.P.; Fischer, A.G.

Arch. Biochem. Biophys.

174

622-629

489671

1368721

Purifications and properties of orotidine-phosphorolyzing enzyme and purine nucleoside phosphorylase from Erwinia carotovora AJ 2992

1991

Shirae, H.; Yokozeki, K.

Agric. Biol. Chem.

55

1849-1857

489672

-

Purification and characterization of second thermostable purine nucleoside phosphorylase in Bacillus stearothermophilus JTS 859

1989

Hori, N.; Watanabe, M.; Yamazaki, Y.; Mikami, Y.

Agric. Biol. Chem.

53

3219-3224

489688

235429

Purine nucleoside phosphorylase from Escherichia coli and Salmonella typhimurium. Purification and some properties

1975

Jensen, K.F.; Nygaard, P.

Eur. J. Biochem.

51

253-265

489693

3042752

Purification and properties of inosine-guanosine phosphorylase from Escherichia coli K-12

1988

Koszalka, G.W.; Vanhooke, J.; Short, S.A.; Hall, W.W.

J. Bacteriol.

170

3493-3498

489703

9614697

Purification and partial characterization of purine nucleoside phosphorylase from Serratia marcescens

1998

Choi, H.S.

Biosci. Biotechnol. Biochem.

62

667-671

489711

11337031

Purine nucleoside phosphorylases: properties, functions, and clinical aspects

2000

Bzowska, A.; Kulikowska, E.; Shugar, D.

Pharmacol. Ther.

88

349-425

636839

9598112

The single deoxynucleoside kinase in Drosophila melanogaster, Dm-dNK, is multifunctional and differs from the mammalian deoxynucleoside kinases

1998

Munch-Petersen, B.; Piskur, J.; Sondergaard, L.

Adv. Exp. Med. Biol.

431

465-469

636840

9461577

Four deoxynucleoside kinase activities from Drosophila melanogaster are contained within a single monomeric enzyme, a new multifunctional deoxynucleoside kinase

1998

Munch-Petersen, B.; Piskur, J.; Sondergaard, L.

J. Biol. Chem.

273

3926-3931

636841

10446143

Cloning and characterization of the multisubstrate deoxyribonucleoside kinase of Drosophila melanogaster

1999

Johansson, M.; van Rompay, A.R.; Degreve, B.; Balzarini, J.; Karlsson, A.

J. Biol. Chem.

274

23814-23819

636842

10692477

Functional expression of a multisubstrate deoxyribonucleoside kinase from Drosophila melanogaster and its C-terminal deletion mutants

2000

Munch-Petersen, B.; Knecht, W.; Lenz, C.; Sondergaard, L.; Piskur, J.

J. Biol. Chem.

275

6673-6679

636844

10966789

Identification of residues involved in the specificity and regulation of the highly efficient multisubstrate deoxyribonucleoside kinase from Drosophila melanogaster

2000

Knecht, W.; Munch-Petersen, B.; Piskur, J.

J. Mol. Biol.

301

827-837

637533

3125430

Substrate specificities of 5'-deoxy-5'-methylthioadenosine phosphorylase from Trypanosoma brucei brucei and mammalian cells

1988

Ghoda, L.Y.; Savarese, T.M.; Northup, C.H.; Parks, R.E.; Garofalo, J.; Katz, L.; Ellenbogen, B.B.; Bacchi, C.J.

Mol. Biochem. Parasitol.

27

109-118

637534

-

5'-Methyladenosine (MTA) phosphorylase from promastigotes of Leishmania donovani

1986

Koszalka, G.W.; Krenitsky, T.A.

Adv. Exp. Med. Biol.

195B

559-563

637545

7732755

Substrate specificity of methylthioadenosine phosphorylase from human liver

1994

Fabianowska-Majewska, K.; Duley, J.; Fairbanks, L.; Simmonds, A.; Wasiak, T.

Acta Biochim. Pol.

41

391-395

638040

13563482

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