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• • Molecular Structure
  • Sum Formula
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• Roles as Enzyme Ligand
• • In Vivo Substrate
  • In Vivo Product
  • Substrate
  • Product
  • Cofactor
  • Activator
  • Inhibitor
  • Metals and Ions
  • 3D Structure (PDB)
• Enzyme Kinetic Parameters
• • k_cat Value (Turnover Number)
  • K_M Value
  • K_i Value
  • IC₅₀ Value
• References & Links
• • References
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Ligand CuCl2

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (4 results)

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Show Substrate (4 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.5.99.12

N6-(2-isopentenyl)adenine + CuCl2 = ?

689597, 685469

-

1.5.99.12

N6-isopentenyladenine + CuCl2 = adenine + 3-methyl-2-butenal + reduced electron acceptor

685468

-

1.5.99.12

N6-(2-isopentenyl)adenine + CuCl2 + H2O = adenine + 3-methylbut-2-enal + ?

712868

-

1.5.99.12

N6-(DELTA2-isopentenyl)adenine + CuCl2 + H2O = adenine + 3-methyl-2-butenal + CuCl + Cl-

742212

-

1.5.99.12

4 entries

Activator in Enzyme-catalyzed Reactions (5 results)

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Show Activating Compound (5 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.3.4

stimulation of activity, 123% relative activity to no addition

389785

-

1.10.3.3

1 mM, 2fold activation

439932

-

1.16.3.1

increase in enzyme mRNA due to transcriptional activation of enzyme gene’s promoter

672774

-

3.2.1.11

1 mM, 107% activity compared to control without any metal ion

671015

-

4.1.1.59

-

727635

-

Inhibitor in Enzyme-catalyzed Reactions (181 results)

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Show Inhibitors (181 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.1

1 mM, 68% inhibition

668532

-

1.1.1.1

1 mM, 24% inhibition

684583

-

1.1.1.1

1 mM, complete inhibition

669540, 687850

-

1.1.1.1

3 entries

1.1.1.103

1 mM, 100% inhibition

655857

-

1.1.1.159

-

286073

-

1.1.1.159

nearly complete inhibition

286085

-

1.1.1.159

2 entries

1.1.1.165

complete inhibition at 2 mM

286099

-

1.1.1.184

only enzyme forms CR2, CR3

347762

-

1.1.1.192

-

288324

-

1.1.1.200

-

655664

-

1.1.1.21

addition of dithiothreitol or 2-mercaptoethanol recovers activity

656089

-

1.1.1.21

0.007 mM, 20% residual activity, addition of dithiothreitol recovers activity

656089

-

1.1.1.21

2 entries

1.1.1.216

-

347993

-

1.1.1.239

1 mM, complete inhibition

287218

-

1.1.1.26

1 mM, 66% inhibition

727414

-

1.1.1.299

1 mM, 10% residual activity

668012

-

1.1.1.37

1 mM, 89.8% inhibition

668012

-

1.1.1.40

about 40% loss of activity within 60 min

723390

-

1.1.1.6

strong

654038

-

1.1.1.64

10 mM, 40% inhibition

287234

-

1.1.1.9

strong inhibition

742112

-

1.1.3.4

6.5% activity remains at 10 mM

389830

-

1.1.3.6

1 mM, 30 min at 4°C, 29% inhibition

656321

-

1.1.5.4

completely inhibits the enzyme at 0.01 mM

722575

-

1.1.99.6

1 mM, complete loss of activity

693285

-

1.12.1.2

0.2 mM, complete inhibition

439709

-

1.13.11.1

0.1 mM, 41% inhibition

671650

-

1.13.11.3

-

439500

-

1.13.11.55

1 mM, 70°C, 0.7% activity

663712

-

1.13.12.21

31% loss of activity

721576

-

1.13.12.3

-

439341

-

1.13.12.5

1 microM, inhibition of 95%

695982

-

1.14.11.2

0.4 mM, 67% inhibition

657621

-

1.14.13.114

1 mM, complete inhibition

697700

-

1.14.13.22

-

438970

-

1.14.14.21

complete inhibition at 1 mM

735526

-

1.14.99.29

above 0.01 mM

438285

-

1.17.1.5

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

644529

-

1.2.1.12

1 mM

673587

-

1.21.99.5

1 mM cuprous chloride: slight inhibition

349703

-

1.3.1.116

-

744377

-

1.3.1.116

1.0 mM, 99% inhibition

745196

-

1.3.1.116

2 entries

1.3.1.57

tested at 0.1 mM, 100% inhibition

288477

-

1.3.4.1

5 mM, about 80% loss of activity

723990

-

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

-

349537

-

1.4.1.1

1 mM, 52% inhibition

349595

-

1.4.1.1

2 entries

1.4.3.14

-

391751

-

1.4.3.21

strong inhibition at 1 mM

742933

-

1.4.3.22

1 mM, strongly inhibited,more than 90%

720756

-

1.5.1.30

with 1 mM 11.2% activity

699057

-

1.5.1.36

-

744377

-

1.5.1.36

1.0 mM, 99% inhibition

745196

-

1.5.1.36

2 entries

1.5.1.48

1 mM, 41% inhibition

724593

-

1.6.3.3

1 mM, 58% inhibition

721365

-

1.6.3.3

3 mM, 60% inhibition

722518

-

1.6.3.3

2 entries

1.7.2.2

0.01 mM,70% inhibition; 0.1 mM, 69% inhibition

288626

-

2.3.1.171

0.1 mM, complete inhibition

656963

-

2.3.1.22

10 mM

486609

-

2.3.2.5

0.1 mM

487989

-

2.4.1.11

-

488407

-

2.4.1.150

-

638566

-

2.4.1.195

-

644892

-

2.4.1.234

1 mM, 100% inhibition

489559

-

2.4.1.74

5-10 mM, more than 90% inhibition

659073

-

2.5.1.65

25°C, 10 min, 79% inhibition of the O-phospho-L-serine sulfhydrylation reaction, 98.7% inhibition of the O-acetyl-L-serine sulfhydrylation reaction

655576

-

2.6.1.42

-

640032

-

2.6.1.71

complete inhibition at 1 mM or higher

640193

-

2.7.1.165

-

641338

-

2.7.1.165

1 mM, 61% inhibition; 61% inhibition at 1 mM

673501

-

2.7.1.165

2 entries

2.7.7.19

remaining activity 0.1%

662628

-

2.8.2.9

-

644823

-

2.8.2.B1

0.1 mM, 50% inhibition

289091

-

3.1.1.1

1 mM, 59% residual activity

661545

-

3.1.1.73

-

729036

-

3.1.1.93

the recombinant enzyme shows about 20% residual activity at 1 mM

720062

-

3.1.13.3

slight

134081

-

3.1.3.1

10 mM, 24% inhibition

679942

-

3.1.3.2

-

134696, 702777

-

3.1.4.1

-

134081

-

3.1.4.11

0.1 mM, 53% inhibition

135131

-

3.1.4.37

-

135380

-

3.1.6.1

-

135518, 135535

-

3.2.1.1

10 mM, 95% inhibition

654300

-

3.2.1.1

5 mM, 88% inhibition; 5 mM, 89% inhibition; 5 mM, 94% inhibition

656951

-

3.2.1.1

5 mM, pH 4.0, 55°C, 26% relative activity

693602

-

3.2.1.1

1 mM, complete inhibition

722877

-

3.2.1.1

4 entries

3.2.1.132

10 mM, 69% inhibition

665286

-

3.2.1.133

-

646794

-

3.2.1.139

-

26103

-

3.2.1.159

2 mM, 7% residual activity

665765

-

3.2.1.2

1 mM, 93% inhibition

654141

-

3.2.1.20

1 mM, 65% loss of activity

748424

-

3.2.1.22

1.0 mM, 30.8% inhibition

655765

-

3.2.1.22

1 mM, 50% inhibition

656702

-

3.2.1.22

2 entries

3.2.1.28

20 mM, 20% residual activity

716128

-

3.2.1.37

1 mM, 83% inhibition

655001

-

3.2.1.4

82% inhibition

677759

-

3.2.1.40

1 mM, 4% residual activity; 1 mM, 70% residual activity

654359

-

3.2.1.40

1 mM, 11% residual activity

654992

-

3.2.1.40

2 entries

3.2.1.41

5 mM, no residual activity

655828

-

3.2.1.52

5 mM, 37% inhibition

656623

-

3.2.1.58

-

136658, 136681

-

3.2.1.68

1 mM, 30% inhibition

136806

-

3.2.1.68

0.1 mM reduce activity to 3%

136815

-

3.2.1.68

5 mM, 30% residual activity

654414

-

3.2.1.68

3 entries

3.2.1.74

-

136842

-

3.2.1.76

-

171561

-

3.2.1.76

strong noncompetitive inhibitor for enzyme from healthy individuals and mucopolysaccharidosis type I patients

655246

-

3.2.1.81

2 mM, 76% inhibition

656317

-

3.2.1.81

complete inhibition

677750

-

3.2.1.81

1mM, complete inhibition

678815

-

3.2.1.81

completely inhibits the activity

695736

-

3.2.1.76

2 entries

3.2.1.81

4 entries

3.2.2.3

-

326393, 326394, 326395

-

3.2.2.8

at 1 mM: inhibition less than 10%

137117

-

3.4.11.24

1 mM, 96% inhibition in presence of 1 mM CoCl2

667014

-

3.4.11.3

0.1 mM, 91% inhibition. 0.01 mM, 87% inhibition

651074

-

3.4.11.5

1 mM, 9% residual activity

683034

-

3.4.15.1

73% inhibition at 0.1 mM, 99% inhibition at 1.0 mM

650873

-

3.4.15.1

-

81286

-

3.4.15.1

2 entries

3.4.16.5

1 mM, 39% inhibition

665930

-

3.4.17.1

complete inhibition at 1 mM

668430

-

3.4.17.10

-

81296, 81298, 81304

-

3.4.21.65

-

29526

-

3.4.21.B6

-

671687

-

3.4.22.15

-

647927, 647935

-

3.4.22.16

94% inhibition at 1 mM

638839

-

3.4.23.12

-

36772

-

3.4.23.49

significant inhibition at 1 mM

708495

-

3.4.24.19

-

31033, 31041

-

3.4.24.19

inhibits at 0.01-0.1 mM

668838

-

3.4.24.19

2 entries

3.5.1.100

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

664820

-

3.5.1.104

-

687500

-

3.5.1.12

-

171922, 171924, 171933

-

3.5.1.19

-

682380

-

3.5.1.2

20% inhibition at 1 mM, 17% at 0.1 mM

669739

-

3.5.1.23

ceramide synthesis activity, 1 mM, total inhibition

655998

-

3.5.1.24

98.1% inhibition at 5 mM

733164

-

3.5.1.24

complete inhibition at 2 mM

734498

-

3.5.1.24

97.2% inhibition of recombinant enzyme at 5 mM

734840

-

3.5.1.24

-

734840

-

3.5.1.24

4 entries

3.5.1.62

1 mM: 74.4% inhibition

172070

-

3.5.1.81

93% inibition at 1 mM

734334

-

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

3.5.4.23

-

209567, 209568

-

3.7.1.4

85% inhibition at 1 mM

654284

-

3.7.1.9

-

247052

-

4.1.1.15

1 mM, 43% inhibition

655656

-

4.1.1.15

-

727202

-

4.1.1.15

2 entries

4.1.1.59

-

4733

-

4.1.1.61

2.5 mM, 91% loss of activity

677849

-

4.1.1.91

1 mM, 70% loss of carboxylation activity, 14% loss of decarboxylation activity

707400

-

4.1.1.92

1 mM, complete inhibition

711507

-

4.1.1.93

1 mM, 97% inhibition

711887

-

4.1.2.13

1 mM, complete inhibition

727401

-

4.1.2.42

0.1 mM, complete inhibition

748886

-

4.1.3.1

-

33121

-

4.2.1.2

inhibits 37% at 5 mM

716122

-

4.2.1.32

-

5653

-

4.2.1.84

1 mM, relative activity: 4.8%

672727

-

4.2.1.84

1 mM, strong inhibition of EDTA-dialysed enzyme, 19% remaining activity

676087

-

4.2.2.11

1 mM, 58% remaining activity

648527

-

4.2.2.11

97% inhibition at 1 mM

729470

-

4.2.1.84

2 entries

4.2.2.11

2 entries

4.2.2.12

0.1 mM, 70% loss of activity

648538

-

4.2.2.3

97% inhibition at 1 mM

729470

-

4.3.1.16

1 mM causes inhibition enzyme activity (92% relative activity)

692924

-

4.3.1.17

0.7 mM, 50% inhibition

210775

-

5.3.2.2

-

2874

-

5.3.3.1

strong

2900

-

5.3.3.5

IC50: 0.01 mM, ifenprodil-labeled enzyme

653279

-

5.3.3.5

IC50: 0.0023 mM, ifenprodil-labeled enzyme

653279

-

5.3.3.5

IC50: 0.0011 mM, ifenprodil-labled enzyme

653279

-

5.3.3.5

IC50: 0.57 mM, ifenprodil-labeled enzyme

653279

-

5.3.3.5

4 entries

5.5.1.2

-

3661

-

6.2.1.25

CuCl2

711

-

6.2.1.25

-

713

-

6.2.1.25

2 entries

6.4.1.3

-

649502

-

Metals and Ions (24 results)

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Show Metals Ions (24 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.3.4

activates

743775

-

1.10.3.2

1 mM, increases activity by 28.5%

741648

-

1.11.1.7

5 mM, activation to 166% of control

674130

-

1.14.99.39

stimulates enzyme activity in vitro

727350

-

1.2.3.1

1 mM, 123% of initial activity

699045

-

1.6.3.3

10 mM, 3-4fold stimulation

722505

-

2.3.1.22

2.5 mM, stimulation

486609

-

2.4.1.230

1 mM, elevates hydrolysis activity by 40%

725294

-

2.5.1.18

0.05 mM and 0.5 mM increases activity of GPOX

396634

-

2.7.1.23

5 mM, substrate polyP27, 100% activity, substrate ATP, 62% activity

660762

-

2.8.2.14

activity 136%

645714

-

3.1.1.93

inhibition

731709

-

3.1.22.1

high concentrations cause cyclic changes in the enzyme activity, the changes of enzyme activity are likely to be caused by adaption and compensation processes in the organisms of the molluscs exposed to toxicants in vivo

649345

-

3.2.1.11

1 mM, 107% activity compared to control without any metal ion

671015

-

3.2.1.132

1 mM, 19% enhancement of activity

665286

-

3.2.1.3

1 mM

709374

-

3.2.1.37

5 mM, 87.8% activity compared to activity without addition of MgCl2, 1.25 mM 4-nitrophenyl beta-D-xylopyranoside as substrate, pH 4.6, 40°C; 5 mM, 96.4% activity compared to activity without addition of MgCl2, 1.25 mM 4-nitrophenyl beta-D-xylopyranoside as substrate, pH 4.6, 42°C

717112

-

3.2.1.4

1 mM, 236% of initial activity

729140

-

3.2.1.74

5 mM, 79.5% activity compared to activity without addition of MgCl2, 1.25 mM 4-nitrophenyl beta-D-glucopyranoside as substrate, pH 4.6, 40°C; 5 mM, 83.6% activity compared to activity without addition of MgCl2, 1.25 mM 4-nitrophenyl beta-D-glucopyranoside as substrate, pH 4.6, 42°C

717112

-

3.4.16.5

1 mM, 36% inhibition, isoenzyme MpiCP-1; 1 mM, 73% inhibition, isoenzyme MpiCP-2

665932

-

3.4.23.31

activates

30754

-

3.4.23.32

10 mM, activates

30754

-

3.5.1.14

relative activity of ACY is 22.9% when dipicolinic acid is removed; relative activity of ACY is 26.4% when EDTA is removed

680973

-

4.2.1.48

no significant activity with 5-oxo-D-proline, stimulates activity with D-glutamate

746927

-

Enzyme Kinetic Parameters

K_i Value (2 results)

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Show KI Value (2 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

3.4.21.B6

0.0021

-

with acetyl-PRLR-7-amido-4-carbamoylmethylcoumarin

671687

4.3.1.17

0.7

-

-

210775

IC₅₀ Value (4 results)

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Show IC50 Value (4 entries)

EC NUMBER

IC50 VALUE

IC50 VALUE MAXIMUM

COMMENTARY

LITERATURE

5.3.3.5

0.0011

-

IC50: 0.0011 mM, ifenprodil-labled enzyme

653279

5.3.3.5

0.0023

-

IC50: 0.0023 mM, ifenprodil-labeled enzyme

653279

5.3.3.5

0.01

-

IC50: 0.01 mM, ifenprodil-labeled enzyme

653279

5.3.3.5

0.57

-

IC50: 0.57 mM, ifenprodil-labeled enzyme

653279

5.3.3.5

4 entries

References & Links

Literature References (211)

top print hide

Show Reference (211 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

711

1369492

Purification and chracterization of benzoyl-CoA ligase from a syntrophic, benzoate-degrading, anaerobic mixed culture

1992

Auburger, G.; Winter, J.

Appl. Microbiol. Biotechnol.

37

789-795

713

1885526

Purification and characterization of benzoate-coenzyme A ligase and 2-aminobenzoate-coenzyme A ligase from a denitrifying Pseudomonas sp.

1991

Altenschmidt, U.; Oswald, B.; Fuchs, G.

J. Bacteriol.

173

5494-5501

2874

5781999

Oxalacetate keto-enol tautomerase. Purification and characterization

1969

Annett, R.G.; Kosicki, G.W.

J. Biol. Chem.

244

2059-2067

2900

2770297

Human placental 3beta-hydroxy-5-ene-steroid dehydrogenase and steroid 5-->4-ene-isomerase: purification from mitochondria and kinetic profiles, biophysical characterization of the purified mitochondrial and microsomal enzymes

1989

Thomas, J.L.; Myers, R.P.; Strickler, R.C.

J. Steroid Biochem.

33

209-217

3661

5916392

The conversion of catechol and protocatechuate to beta-ketoadipate by Pseudomonas putida

1966

Ornston, L.N.

J. Biol. Chem.

241

3787-3794

4733

9835557

Purification and characterization of gallic acid decarboxylase from Pantoea agglomerans T71

1998

Zeida, M.; Wieser, M.; Yoshida, T.; Sugio, T.; Nagasawa, T.

Appl. Environ. Microbiol.

64

4743-4747

5653

14342293

Tartaric acid metabolism

1965

Hurlbert, R.E.; Jakoby, W.B.

J. Biol. Chem.

240

2772-2777

26103

7496513

alpha-D-Glucuronidases from the xylanolytic thermophiles Clostridium stercorarium and Thermoanaerobacterium saccharolyticum

1995

Bronnenmeier, K.; Meissner, H.; Stocker, S.; Staudenbauer, W.L.

Microbiology

141

2033-2040

29526

1012007

Thermomycolin

1976

Gaucher, G.M.; Stevenson, K.J.

Methods Enzymol.

45

415-433

30754

-

New acid proteases from Scytalidium lignicolum M-133. II. Purification and some enzymatic properties of acid protease A and B of Scytalidium lignicolum ATCC 24568.

1974

Oda, K.; Murao, S.

Agric. Biol. Chem.

38

2435-2444

31033

3905801

Type I procollagen carboxyl-terminal proteinase from chick embryo tendons. Purification and characterization

1985

Hojima, Y.; van der Rest, M.; Prockop, P.J.

J. Biol. Chem.

260

15996-16003

31041

8061925

Cadmium ions inhibit procollagen C-proteinase and cupric ions inhibit procollagen N-proteinase

1994

Hojima, Y.; Behta, B.; Romanic, A.M.; Prockop, D.J.

Matrix Biol.

14

113-120

33121

100334120

Purification and some properties of isocitrate lyase from the pollen of Pinus densiflora Sieb. et Zucc.

1986

Tsukamoto, C.; Ejiri, S.I.; Katsumata, T.

Agric. Biol. Chem.

50

409-416

36772

24549466

Reinigung der Proteinase aus Nepenthes-Kannensaft

1967

Steckelberg, R.; Luettge, U.; Weigl, J.

Planta

76

238-241

81286

9178563

Purification and characterization of a dipeptidyl carboxypeptidase from Pseudomonas sp. WO24

1997

Ogasawara, W.; Abe, N.; Hagio, T.; Okada, H.; Morikawa, Y.

Biosci. Biotechnol. Biochem.

61

858-863

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Cytokinin dehydrogenase activity in primary roots and characterization of primary metabolites from leaves and rootlets of Ricinus communis

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Braz. Arch. Biol. Technol.

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Characterization of two amine oxidases from Aspergillus carbonarius AIU 205

2015

Sugawara, A.; Matsui, D.; Yamada, M.; Asano, Y.; Isobe, K.

J. Biosci. Bioeng.

119

629-635

743775

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Research journal of pharmaceutical, biological and chemical sciences purification, characterization, thermostability and shelf life studies of glucose oxidase from Aspergillus niger PIL7

2015

Jithendar, T.; Sairam, K.; Verma, V.

Res. J. Pharm. Biol. Chem. Sci.

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Expression of the bile acid-inducible NADHflavin oxidoreductase gene of Eubacterium sp. VPI 12708 in Escherichia coli

1995

Baron, S.; Hylemon, P.

Biochim. Biophys. Acta

1249

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745196

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Characterization of the baiH gene encoding a bile acid-inducible NADHflavin oxidoreductase from Eubacterium sp. strain VPI 12708

1993

Franklund, C.; Baron, S.; Hylemon, P.

J. Bacteriol.

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746927

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Structural and enzymatic properties of mammalian D-glutamate cyclase

2018

Katane, M.; Ariyoshi, M.; Tateishi, S.; Koiwai, S.; Takaku, K.; Nagai, K.; Nakayama, K.; Saitoh, Y.; Miyamoto, T.; Sekine, M.; Mita, M.; Hamase, K.; Matoba, S.; Homma, H.

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Characterization of the catalytic and kinetic properties of a thermostable Thermoplasma acidophilum alpha-glucosidase and its transglucosylation reaction with arbutin

2011

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Cloning and characterization of D-threonine aldolase from the green alga Chlamydomonas reinhardtii

2017

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Phytochemistry

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