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Ligand AgNO3

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

Activator in Enzyme-catalyzed Reactions (2 results)

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Show Activating Compound (2 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

2.3.1.167

-

688912

-

4.2.2.3

activates 31% at 1 mM

730133

-

Inhibitor in Enzyme-catalyzed Reactions (193 results)

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Show Inhibitors (193 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.1

0.1 mM, 66% inhibition

667255

-

1.1.1.1

1 mM, 37% inhibition

688442

-

1.1.1.1

2 entries

1.1.1.14

-

285874, 285881

-

1.1.1.145

-

389394

-

1.1.1.184

-

347769

-

1.1.1.184

enzyme form CR1 inhibited, CR2 not

347758

-

1.1.1.184

2 entries

1.1.1.188

at 0.05 mM 87-100% inhibition, depending on the substrate

389454

-

1.1.1.200

complete inhibition at 0.1 mM

347839

-

1.1.1.284

NADH protects more effectively than NAD+

287888

-

1.1.1.29

-

286506

-

1.1.1.31

-

286551

-

1.1.1.37

-

286631

-

1.1.1.38

inhibition with 20 mM, complete inhibition with 300 mM

286679

-

1.1.1.71

1 mM, 100% inhibition

287280

-

1.1.1.9

-

246421

-

1.1.1.9

complete inhibition

742112

-

1.1.1.90

-

389592

-

1.1.1.90

10 mM, 58% inhibition

692723

-

1.1.1.9

2 entries

1.1.1.90

2 entries

1.1.1.91

1 mM

389592

-

1.1.1.B3

2 mM, complete inhibition

689823

-

1.1.1.B3

2 mM, no% residual activity

685643

-

1.1.1.B3

2 entries

1.1.3.13

1 mM, complete loss of activity

685404

-

1.1.3.17

-

389719

-

1.1.3.4

24% activity remains at 10 mM

389830

-

1.1.3.6

-

287648, 763657

-

1.1.3.6

1 mM, 100% inhibition, 0.1 mM, 62% inhibition

287646

-

1.1.3.6

cholesterol oxidase II

655611

-

1.1.3.6

markedly inhibited by AgNO3

710959

-

1.1.3.6

4 entries

1.1.3.9

complete inhibition at 0.1 mM

389873

-

1.1.99.1

1 mM causes 100% inhibition

389887

-

1.11.1.13

5 mM, about 60% inhibition

725141

-

1.11.1.14

-

764314

-

1.11.1.7

0.25 mM, 31% loss of activity

674130

-

1.13.11.1

0.001 mM, 93% loss of activity

671650

-

1.13.11.1

0.1 mM, 10 min, complete inhibition

697245

-

1.13.11.1

0.1 mM, enzyme from aniline-grown cells loses 88% of its activity, enzyme from L-malate-grown cells loses 67% of its activity

659536

-

1.13.11.1

3 entries

1.13.11.37

-

439430

-

1.13.11.74

6% residual activity at 0.5 mM

722603

-

1.14.13.20

-

439011, 439012

-

1.14.13.27

93% inactivation at 0.1 mM

438909

-

1.14.13.40

at least 90% inhibition at 0.01 mM

438851

-

1.14.13.44

0.01 mM, complete inhibition

438850

-

1.14.13.7

0.01 mM

438777

-

1.17.1.10

complete inhibition at 1 mM

711869

-

1.17.1.5

1 mM, 10 min at 35°C, complete loss of activity

644529

-

1.17.1.9

0.01 mM

288104

-

1.17.1.9

1 mM; 80% inhibition

288115

-

1.17.1.9

2 entries

1.18.1.1

-

437855, 437858, 437860

-

1.2.1.10

1 mM 20% inhibition

390167

-

1.2.1.8

3 mM, 90-100% inhibition

390342

-

1.2.4.1

18 mol per mol enzyme, complete inhibition

348974

-

1.3.1.32

-

390699

-

1.3.3.6

-

391050, 391060

-

1.3.8.1

0.1 mM, complete inhibition

391270

-

1.3.8.7

-

391270

-

1.3.8.8

strong inhibition of apo and holo forms at 0.1 mM

391270

-

1.3.99.4

-

391392

-

1.4.1.1

0.1 mM, 57% inhibition

349555

-

1.4.1.13

at 0.001 mM completely inhibits

391447

-

1.4.1.20

1 mM, complete inhibition

349634

-

1.4.1.4

1 mM, 30°C, complete loss of aminating activity

656309

-

1.4.1.9

1 mM, complete

656565

-

1.4.3.3

0.1 mM, 66% inhibition

655274

-

1.5.1.30

with 1 mM 1.05% activity

699057

-

1.5.1.48

1 mM, 97% inhibition

724593

-

1.5.3.1

2 mM, 0% relative activity

392382

-

1.5.3.15

0.1-1 mM

694075

-

1.6.3.3

1 mM, 63% inhibition

721365

-

1.8.1.7

-

394748, 394751

-

1.8.1.8

0.009 mM, 66% inhibition

437710

-

2.1.1.11

-

485101

-

2.3.1.1

0.1 mM, 70-90% inhibition

486062

-

2.3.1.331

22.4% residual activity after 1 h at 1 mM

735497

-

2.3.1.5

-

487116

-

2.4.1.10

1 mM, 86% inhibition

672335

-

2.4.2.1

-

489671, 489673

-

2.5.1.47

1 mM, 22% inhibition

637382

-

2.5.1.47

1 mM, complete loss of activity

676961

-

2.5.1.47

2 entries

2.5.1.56

1 mM, 61% inhibition

637321

-

2.6.1.14

-

637254

-

2.6.1.45

strong inhibition

636693

-

2.6.1.5

10 mM, complete inhibition

657704

-

2.7.1.165

-

641338

-

2.7.1.2

-

641060

-

2.7.1.72

strong inhibition

641921

-

2.7.1.78

-

642022

-

2.7.1.78

complete inhibition at 0.3 mM

642023

-

2.7.1.78

2 entries

2.7.2.2

-

642220

-

2.7.4.10

weak

642538

-

3.1.1.11

-

694840

-

3.1.1.11

complete inhibition

750823

-

3.1.1.11

2 entries

3.1.1.20

98.77% residual activity at 1 mM

715957

-

3.1.1.74

90% inhibition at 1 mM; 93% inhibition at 1 mM

729000

-

3.1.1.8

-

94440

-

3.1.1.93

the recombinant enzyme is completely inhibited at 0.1 mM

720062

-

3.1.3.1

1 mM, 61.8% of initial activity

772615

-

3.1.3.25

-

114224

-

3.1.6.1

0.2 mM, 20-30% inhibition

135528

-

3.1.6.2

5 mM, 65% inhibition

656643

-

3.1.6.2

slight

135613

-

3.1.6.2

2 entries

3.1.6.8

50% decreased activity in milt plasma with 60 nM AgNO3 and 50% decreased activity in spermatozoon with 4 nM AgNO3

668313

-

3.2.1.1

1 mM, 40°C, 30 min, 12% loss of activity, alpha-amylase I

678804

-

3.2.1.1

2 mM, complete inhibition

656916

-

3.2.1.1

2 entries

3.2.1.11

1 mM, 71% activity compared to control without any metal ion

671015

-

3.2.1.131

1 mM, 94% loss of activity

750430

-

3.2.1.159

2 mM, 9% residual activity

665765

-

3.2.1.17

-

171040

-

3.2.1.2

1 mM, 94% inhibition

654141

-

3.2.1.21

0.5 mM, 81% inhibition, reversible by the addition of 50 mM beta-mercaptoethanol

654861

-

3.2.1.21

1 mM, 88% inhibition

655773

-

3.2.1.21

10 mM, 84% inhibition

655757

-

3.2.1.21

100 mM, 69% inhibition; 100 mM, 90% inhibition

655652

-

3.2.1.21

4 entries

3.2.1.211

0.001 M, 58% loss of activity

749735

-

3.2.1.212

0.001 M, 58% loss of activity

749735

-

3.2.1.22

1.0 mM, complete inhibition, alpha-galactosidase 1; 1.0 mM, complete inhibition, alpha-galactosidase 2; 1.0 mM, complete inhibition, alpha-galactosidase 3

666568

-

3.2.1.23

10 mM, 87% inhibition

655099

-

3.2.1.23

competitive inhibitor

697390

-

3.2.1.23

2 entries

3.2.1.26

0.1 mM, 37% inhibition; 1 mM, 88% inhibition

700860

-

3.2.1.37

1 mM, 64% inhibition

655001

-

3.2.1.39

complete inhibition at 1 mM

136372

-

3.2.1.39

inhibition at 1 mM

136378

-

3.2.1.39

inhibition on both laminarin hydrolysis and disruption of living yeast cells

136374

-

3.2.1.39

3 entries

3.2.1.4

10 mM, 90.8% loss of activity

771344

-

3.2.1.52

0.1 mM, complete inhibition

655935

-

3.2.1.52

1 mM final concentration

664296

-

3.2.1.52

5 mM, 93% inhibition

656623

-

3.2.1.52

3 entries

3.2.1.53

-

136607

-

3.2.1.54

10 mM, complete inhibition

664779, 665437

-

3.2.1.58

-

136645

-

3.2.1.81

1mM, complete inhibition

678815

-

3.2.1.83

1 mM, complete inhibition

208832

-

3.2.1.93

1 mM, complete inhibition, rTRE_P3; 1 mM, inhibition to 0.32% of control, rTRE_P2

771475

-

3.2.1.95

2 mM, 97% inhibition

208775

-

3.2.1.98

-

171734

-

3.2.1.98

extracellular enzyme, strong inhibition

171738

-

3.2.1.98

G-6

171741

-

3.2.1.98

native and immobilized enzyme, immobilized enzyme less than native enzyme

171735

-

3.2.1.98

4 entries

3.2.1.99

IFO 3134

171761

-

3.2.1.B47

2 mM, 2-10% inhibition

750087

-

3.4.13.20

30°C, 10 min, 1 mM, 95% loss of activity

708466

-

3.4.22.15

-

647927

-

3.5.1.100

1 mM, incubation at 30°C for 10 min, complete inhibition

664820

-

3.5.1.13

-

696876

-

3.5.1.14

-

288858

-

3.5.1.21

1 mM, 94% inhibition

171973

-

3.5.1.24

77.3% residual activity

697838

-

3.5.1.30

0.00125 mM, 100% inhibition

172031

-

3.5.1.43

-

288897

-

3.5.1.44

-

288897

-

3.5.1.5

-

773420

-

3.5.1.91

0.25 mM, complete inhibition

660362

-

3.5.1.91

complete inhibition at 1 mM

733172

-

3.5.1.91

2 entries

3.5.2.9

-

209394

-

3.5.3.3

-

663469

-

3.5.5.5

1 mM, inhibition to 2.0% of control

776477

-

3.7.1.9

-

247052

-

4.1.1.14

-

3969

-

4.1.1.15

-

727202

-

4.1.1.15

1 mM, 68% residual activity

679946

-

4.1.1.15

44.4% inhibition at 2 mM

748385

-

4.1.1.15

79% inhibition at 2 mM

748381

-

4.1.1.15

complete inhibition at 5 mM; complete inhibition at 5mM

699147

-

4.1.1.15

5 entries

4.1.1.46

-

4578

-

4.1.1.57

-

4720

-

4.1.1.91

1 mM, complete loss of decarboxylation activity, 60% loss of carboxylation activity

707400

-

4.1.1.92

1 mM, 50% inhibition

711507

-

4.1.1.93

1 mM, complete inhibition

711887

-

4.1.2.10

0.2 mM, 85% inhibition

37319

-

4.1.2.10

1 mM, 100% inhibition

691375

-

4.1.2.10

2 entries

4.1.2.11

-

4897

-

4.1.2.35

5% inhibition at 0.32 mM, complete inhibition at 3.2 mM

648385

-

4.1.2.47

strong inhibition

775558

-

4.2.1.103

1 mM, 99% inhibition

393828

-

4.2.1.65

-

5826

-

4.2.1.84

1 mM, complete inhibition of the enzyme

672727

-

4.2.1.84

complete inhibition at 1 mM

703995

-

4.2.1.84

82% reduced activity at 1 mM

699597

-

4.2.1.84

3 entries

4.2.2.16

10 mM, 62% inhibition

652596

-

4.2.2.2

-

37393

-

4.2.2.3

relative activity: 28%

695268

-

4.3.1.15

-

6046

-

4.4.1.1

alpha,beta-elimination L-homoserine

586904

-

4.4.1.15

-

648731

-

4.5.1.2

-

34751, 34753

-

4.6.1.19

-

24191

-

4.8.1.2

very sensitive to, concentration-dependent, 1 mM, 85.8% inhibition

648793

-

5.1.1.8

-

2156

-

5.3.99.7

0.1 mM, 29% inhibition

648825

-

5.4.2.6

-

3338

-

5.4.4.3

at 1 mM

648845

-

5.4.99.14

-

3482

-

6.2.1.2

-

669

-

6.3.3.2

-

1324

-

Metals and Ions (6 results)

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Show Metals Ions (6 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.10.3.2

1 mM, 3% residual activity

655602

-

3.1.1.20

activates

749445

-

3.1.1.93

inhibition

731709

-

3.2.1.11

1 mM, 71% activity compared to control without any metal ion

671015

-

3.2.1.58

activity enhanced by 15%

136672

-

3.5.5.7

1 mM, 1.97fold activation

756271

-

Enzyme Kinetic Parameters

K_i Value (3 results)

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Show KI Value (3 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.1.188

0.005

-

prostaglandin D2 11-ketoreductase activity

389454

3.2.1.23

0.00012

-

-

697390

3.5.1.13

0.2

-

-

696876

IC₅₀ Value (1 result)

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Show IC50 Value (1 entry)

EC NUMBER

IC50 VALUE

IC50 VALUE MAXIMUM

COMMENTARY

LITERATURE

3.5.1.5

0.0000085

-

pH 7.5, temperature not specified in the publication

773420

References & Links

Literature References (211)

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Show Reference (211 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

669

6800377

Butyryl-CoA synthetase of Pseudomonas aeruginosa. Purification and characterization

1981

Shimizu, S.; Inoue, K.; Tani, Y.; Yamada, H.

Biochem. Biophys. Res. Commun.

103

1231-1237

1324

-

Further studies on N5-formyltetrahydrofolic acid cyclodehydrase

1965

Greenberg, D.M.; Wynston, L.K.; Nagabhushanam, A.

Biochemistry

4

1872-1878

2156

14189888

Purification and properties of inducible hydroxyproline 2-epimerase from Pseudomonas

1964

Adams, E.; Norton, I.L.

J. Biol. Chem.

239

1525-1535

3338

-

Purification and some properties of beta-phosphoglucomutase from Lactobacillus lactis subsp. cremonis IFP 3427

1998

Nakamura, K.; Shirokane, Y.; Suzuki, M.

J. Ferment. Bioeng.

85

350-353

3482

2818569

Purification and characterization of 4-methylmuconolactone methyl-isomerase, a novel enzyme of the modified 3-oxoadipate pathway in nocardioform actinomycetes

1989

Bruce, N.C.; Cain, R.B.; Pieper, D.H.; Engesser, K.H.

Biochem. J.

262

303-312

3969

5110120

_ber eine Valin-carboxylase aus Bacillus sphaericus

1971

Bast, E.; Hartmann, T.; Steiner, M.

Arch. Mikrobiol.

79

12-24

4578

6066253

o-Pyrocatechuic acid carboxy-lyase from Aspergillus niger

1967

Subba Rao, P.V.; Moore, K.; Towers, G.H.N.

Arch. Biochem. Biophys.

122

466-473

4720

-

Amino acid metabolism in microorganisms. Part IV. L-Methionine decarboxylase produced by a Streptomyces strain

1968

Hagino, H.; Nakayama, K.

Agric. Biol. Chem.

32

727-733

4897

2780553

Mandelonitrile lyase from Ximenia americana L.: stereospecificity and lack of flavin prosthetic group

1989

Kuroki, G.W.; Conn, E.E.

Proc. Natl. Acad. Sci. USA

86

6978-6981

5826

4627358

Cyanide metabolism in higher plants. V. The formation of asparagine from beta-cyanoalanine

1972

Castric, P.A.; Farnden, J.F.; Conn, E.E.

Arch. Biochem. Biophys.

152

62-69

6046

3275662

Diaminopropionate ammonia-lyase from Salmonella typhimurium. Purification and characterization of the crystalline enzyme and sequence determination of the pyridoxal 5'-phosphate binding peptide

1988

Nagasawa, T.; Tanizawa, K.; Satoda, T.; Yamada, H.

J. Biol. Chem.

263

958-964

24191

-

Microbial ribonucleases with special reference to RNases T1, T2, N1, and U2

1971

Uchida, T.; Egami, F.

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

4

205-250

34751

6815180

3-Chloro-D-alanine chloride-lyase (deaminating) of Pseudomonas putida CR 1.1. Purification and characterization of a novel enzyme occurring in 3-chloro-D-alanine-resistant pseudomonads

1982

Nagasawa, T.; Ohkishi, H.; Kavakami, B.; Yamano, H.; Hosono, H.; Tani, Y.; Yamada, H.

J. Biol. Chem.

257

13749-13756

34753

6427787

3-Chloro-D-alanine chloride-lyase (deaminating) of Pseudomonas putida CR 1-1

1984

Nagasawa, T.; Ohkishi, H.; Yamada, H.

Prog. Clin. Biol. Res.

144A

365-375

37319

12228664

Purification and characterization of a novel (R)-mandelonitrile lyase from the fern Phlebodium aureum

1995

Wajant, H.; Foerster, S.; Selmar, D.; Effenberger, F.; Pfizenmaier, K.

Plant Physiol.

109

1231-1238

37393

7764545

Purification, characterization, and production of two pectic transeliminases with protopectinase activity from Bacillus subtilis

1994

Sakamoto, T.; Hours, R.A.; Sakai, T.

Biosci. Biotechnol. Biochem.

58

353-358

94440

5141

Purification and characterization of butyrylcholine-hydrolyzing enzyme from Pseudomonas polycolor

1976

Nagasawa, T.; Sugisaki, H.; Tani, Y.; Ogata, K.

Biochim. Biophys. Acta

429

817-827

114224

-

Inositol 1-phosphate synthetase and inositol 1-phosphatase from yeast

1966

Charalampous, F.; Chen, I.W.

Methods Enzymol.

9

698-704

135528

6884544

Further studies on arylsulphatase activity from fowl seminal plasma

1983

Droba, M.; Droba, B.

Folia Biol. (Krakow)

31

107-117

135613

7200

Solubilization and partial purification of steroid sulfatase from rat liver: characterization of estrone sulfatase

1976

Iwamori, M.; Moser, H.W.; Kishimoto, Y.

Arch. Biochem. Biophys.

174

199-208

136372

-

Purification, crystallization, and properties of an endo beta-1,3-glucanase from Rhizopus chinensis R-69

1975

Yamamoto, S.; Nagasaki, S.

Agric. Biol. Chem.

39

2163-2169

136374

-

Enzymatic and structural properties of crystalline yeast cell lytic enzyme from a species of fungi imperfecti

1974

Nagasaki, S.; Fukuyama, J.; Yamamoto, S.; Kobayashi, R.

Agric. Biol. Chem.

38

349-357

136378

-

Purification and some properties of beta-1,3-glucanase of suspension-cultured tobacco cells

1973

Kato, K.; Yamada, A.; Noguchi, M.

Agric. Biol. Chem.

37

1269-1275

136607

6055190

Isolation of beta-N-acetylhexosaminidase, beta-N-acetylglucosaminidase, and beta-N-acetylgalactosaminidase from calf brain

1967

Frohwein, Y.Z.; Gatt, S.

Biochemistry

6

2775-2782

136645

236727

Comparative studies on beta-glucan hydrolases. Isolation and characterization of an exo(1 yields 3)-beta-glucanase from the snail, Helix pomatia

1975

Marshall, J.J.; Grand, R.J.A.

Arch. Biochem. Biophys.

167

165-175

136672

-

Purification and characterization of an exo beta-1,3-glucanase from a Fungi imperfecti

1977

Nagasaki, S.; Saito, K.; Yamamoto, S.

Agric. Biol. Chem.

41

493-502

171040

-

Purification and characterization of a lysozyme from wheat germ

1988

Audy, P.; Trudel, J.; Asselin, A.

Plant Sci.

58

43-50

171734

1094

Purification and some properties of a novel maltohexaose-producing exo-amylase from Aerobacter aerogenes

1975

Kainuma, K.; Wako, K.; Kobayashi, S.; Nogami, A.; Suzuki, S.

Biochim. Biophys. Acta

410

333-346

171735

18548722

Immobilization of the exo-maltohexaohydrolase by the irradiation method

1983

Nakakuki, T.; Hayashi, T.; Monma, M.; Kawashima, K.; Kainuma, K.

Biotechnol. Bioeng.

25

1095-1107

171738

-

Purification and some properties of an extracellular exo-maltohexaohydrolase from an Aerobacter aerogenes mutant

1982

Nakakuki, T.; Azuma, K.; Monma, M.; Kainuma, K.

J. Jpn. Soc. Starch Sci.

29

188-197

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Links to other databases for AgNO3

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