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• • In Vivo Substrate
  • In Vivo Product
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  • Inhibitor
  • Metals and Ions
  • 3D Structure (PDB)
• Enzyme Kinetic Parameters
• • k_cat Value (Turnover Number)
  • K_M Value
  • K_i Value
  • IC₅₀ Value
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Ligand angiotensin II

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (16 results)

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Show Natural Substrate (16 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.4.11.1

angiotensin II + H2O = Asp + angiotensin III

664275

-

3.4.11.1

angiotensin II + H2O = angiotensin IV + ?

651776

-

3.4.11.1

2 entries

3.4.11.21

angiotensin II + H2O = Asp + angiotensin III

663814

-

3.4.11.7

angiotensin II + H2O = ?

36029, 36034

-

3.4.11.7

angiotensin II + H2O = Asp + angiotensin III

664275, 665723, 665903, 663814, 665570

-

3.4.11.7

angiotensin II + H2O = aspartic acid + angiotensin III

684050, 683663, 681000, 681632, 683521, 683799

-

3.4.11.7

angiotensin II + H2O = angiotensin III + L-Asp

752443, 755153, 753433, 753895

-

3.4.17.23

angiotensin II + H2O = angiotensin-(1-7) + Phe

668896, 670526, 690356, 693733

-

3.4.17.23

angiotensin II + H2O = angiotensin-(1-7) + L-Phe

695418

-

3.4.17.23

angiotensin II + H2O = angiotensin(1-7) + L-Phe

708141, 708685, 708195, 708649, 708684, 710532, 710214, 708683, 707314, 709990, 710616

-

3.4.17.23

angiotensin II + H2O = DRVYIHP + L-Phe

753311

-

3.4.11.7

4 entries

3.4.17.23

4 entries

3.4.21.26

angiotensin II + H2O = ?

683926

-

3.4.24.15

angiotensin-II + H2O = ?

683813

-

3.4.24.16

angiotensin II + H2O = ?

734522, 754607

-

3.4.24.18

angiotensin II + H2O = ?

754593, 733064

-

3.4.24.63

angiotensin II + H2O = ?

754592

-

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

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Show Natural Product (7 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.4.15.1

angiotensin I + H2O = angiotensin II + His-Leu

652617, 650873

-

3.4.15.1

angiotensin I + H2O = angiotensin II + L-His-L-Leu

-

-

3.4.21.20

angiotensin I + H2O = angiotensin II + ?

-

-

3.4.21.20

angiotensinogen + H2O = angiotensin II + ?

-

-

3.4.21.39

angiotensin I + H2O = angiotensin II + His-Leu

-

-

3.4.21.39

angiotensin I + H2O = angiotensin II + ?

-

-

3.4.21.39

angiotensin I + H2O = angiotensin II

-

-

3.4.15.1

2 entries

3.4.21.20

2 entries

3.4.21.39

3 entries

Substrate in Enzyme-catalyzed Reactions (49 results)

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Show Substrate (49 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.4.11.1

angiotensin II + H2O = Asp + angiotensin III

664275

-

3.4.11.1

angiotensin II + H2O = angiotensin IV + ?

651776

-

3.4.11.21

angiotensin II + H2O = ?

664909

-

3.4.11.21

angiotensin II + H2O = Asp + angiotensin III

678807, 137168, 663814, 665077, 664909

-

3.4.11.1

2 entries

3.4.11.21

2 entries

3.4.11.4

angiotensin II + H2O = ?

35936

-

3.4.11.7

angiotensin II + H2O = ?

36029, 36034, 654587

-

3.4.11.7

angiotensin II = Asp + Arg-Val-Tyr-Ile-His-Pro-Phe

36029, 36034

-

3.4.11.7

angiotensin II + H2O = Asp + angiotensin III

664275, 665723, 665903, 663814, 665570

-

3.4.11.7

angiotensin II + H2O = angiotensin III + Arg

663609

-

3.4.11.7

angiotensin II + H2O = aspartic acid + angiotensin III

696103, 698166, 698879, 683509, 684050, 683663, 681000, 681632, 683520, 683521, 683799

-

3.4.11.7

angiotensin II + H2O = L-Asp + angiotensin III

697164

-

3.4.11.7

angiotensin II + H2O = L-aspartic acid + angiotensin III

699650

-

3.4.11.7

angiotensin II + H2O = angiotensin III + L-Asp

752443, 755153, 753433, 753895

-

3.4.11.7

8 entries

3.4.14.1

Ile5-angiotensin II + H2O = ?

36137

-

3.4.14.4

angiotensin II + H2O = Asp-Arg + Val-Tyr + Ile-His + Pro-Phe

36196, 36178, 35011, 36179

-

3.4.14.4

Asp-Arg-Val-Tyr-Ile-His-Pro-Phe + H2O = ?

683338

-

3.4.14.4

DRVYIHPF + H2O = IHPF + ?

755158

-

3.4.14.9

DRVYIHPF + H2O = DRV + YIHPF

647186, 647183

-

3.4.14.9

angiotensin II + H2O = ? + Asp-Arg-Val

679200

-

3.4.14.4

3 entries

3.4.14.9

2 entries

3.4.15.1

angiotensin II + H2O = ?

731901

-

3.4.16.2

angiotensin II + H2O = ?

36267, 36272, 36274, 36268, 36270

-

3.4.17.15

angiotensin II + H2O = angiotensin-(1-7) + L-Phe

732609

-

3.4.17.23

angiotensin II + H2O = angiotensin-(1-7) + Phe

668895, 677486, 679072, 679135, 679703, 679706, 679707, 680388, 667485, 668219, 668220, 677603, 678710, 679705, 679708, 679876, 681041, 681323, 668418, 677475, 677488, 679300, 680099, 680103, 681178, 681678, 678973, 692319, 694351, 657967, 693733, 690356, 658459, 678102, 659172, 659147, 668896, 670526, 681022

-

3.4.17.23

angiotensin II + H2O = angiotensin-(1-7) + L-Phe

695418

-

3.4.17.23

angiotensin II + H2O = angiotensin(1-7) + L-Phe

708141, 708683, 707314, 708685, 708195, 708649, 708684, 710532, 710616, 710214, 709990

-

3.4.17.23

angiotensin II + H2O = DRVYIHP + L-Phe

753311

-

3.4.17.23

angiotensin II + H2O = angiotensin-(1-7) + L-phenylalanine

752436

-

3.4.21.26

angiotensin II + H2O = ?

81354, 683926, 81324

-

3.4.21.26

DRVYIHPF + H2O = DRVYIHP + L-Phe

81352

-

3.4.21.26

angiotensin II + H2O = DRVYIHP + L-Phe

755073

-

3.4.17.23

5 entries

3.4.21.26

3 entries

3.4.21.39

angiotensin II + H2O = ?

81383

-

3.4.21.9

angiotensin II + H2O = ?

667758

-

3.4.21.B3

angiotensin II + H2O = fragments of angiotensin II

658590

-

3.4.22.33

angiotensin II + H2O = hydrolyzed angiotensin II

30274, 30299

-

3.4.23.18

angiotensin II + H2O = ?

30571

-

3.4.23.19

angiotensin II + H2O = DRVYIH + Pro-Phe

669433, 670655

-

3.4.24.11

angiotensin II + H2O = ?

81609, 667485, 31020

-

3.4.24.15

angiotensin II + H2O = ?

652505

-

3.4.24.15

Asp-Arg-Val-Tyr-Ile-His-Pro-Phe + H2O = Asp-Arg-Val-Tyr + Ile-His-Pro-Phe

37066, 37053

-

3.4.24.15

angiotensin-II + H2O = ?

683813

-

3.4.24.16

angiotensin II + H2O = ?

734522, 652505, 754607

-

3.4.24.16

Asp-Arg-Val-Tyr-Ile-His-Pro-Phe + H2O = Asp-Arg-Val-Tyr + Ile-His-Pro-Phe

37053, 37084

-

3.4.24.18

angiotensin II + H2O = ?

754593, 733064

-

3.4.24.18

angiotensin II + H2O = Asp-Arg-Val-Tyr + Ile-His-Pro-Phe

31019, 31020, 31031, 31021

-

3.4.24.30

angiotensin II + H2O = ?

668832

-

3.4.24.30

angiotensin II + H2O = Asp-Arg-Val-Tyr + Ile-His-Pro-Phe

31192

-

3.4.24.15

3 entries

3.4.24.16

2 entries

3.4.24.18

2 entries

3.4.24.30

2 entries

3.4.24.40

angiotensin II + H2O = ?

650288

-

3.4.24.60

angiotensin II + H2O = ?

31362, 31363, 31364, 668827

-

3.4.24.63

angiotensin II + H2O = ?

754592

-

Product in Enzyme-catalyzed Reactions (10 results)

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Show Product (10 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.4.15.1

angiotensin I + H2O = angiotensin II + His-Leu

81275, 81239, 81248, 653416, 81261, 81263, 81266, 652617, 81286, 81285, 81287, 650873

-

3.4.15.1

angiotensin I + H2O = angiotensin II + L-His-L-Leu

-

-

3.4.15.1

2 entries

3.4.15.5

angiotensin I + H2O = DRVYIHPF + His-Leu

-

-

3.4.17.1

angiotensin I + H2O = angiotensin II + His-Leu

-

-

3.4.21.20

angiotensin I + H2O = angiotensin II + ?

-

-

3.4.21.20

angiotensinogen + H2O = angiotensin II + ?

-

-

3.4.21.39

angiotensin I + H2O = angiotensin II + His-Leu

81372, 81375

-

3.4.21.39

angiotensin I + H2O = angiotensin II + ?

-

-

3.4.21.39

angiotensin I + H2O = angiotensin II

-

-

3.4.21.39

proangiotensin-12 + H2O = angiotensin II

-

-

3.4.21.20

2 entries

3.4.21.39

4 entries

Activator in Enzyme-catalyzed Reactions (20 results)

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Show Activating Compound (20 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.17.3.2

Ang II substantially increases endothelial enzyme protein levels and enzyme-dependent superoxide production in cultured endothelial cells

684783

-

1.6.3.1

potent stimulator of NAD(P)H oxidase O2- production in the vasculature

711688

-

1.6.3.1

stimulates Nox1

724778

-

2.7.10.1

induces transactivation of epidermal growth factor receptor, mechanism

660727

-

2.7.10.1

-

661483

-

1.6.3.1

2 entries

2.7.10.1

2 entries

2.7.11.24

-

703567

-

3.2.1.166

-

732437

-

3.3.2.10

induces sEH activity

700587

-

3.4.22.52

1.2-fold increased activity of calpain-1, influence in expression of calpain-1

700880

-

3.4.22.B30

activates the enzyme in vivo, reduced by pan-calpain inhibitors

731722

-

3.4.24.80

-

754128

-

3.4.24.86

treatment with angiotensin II results in angiotensin II type 1 receptor AT1R-mediated increase in myocardial TACE expression and activity, and membrane translocation of TACE

734505

-

3.4.24.B4

-

711052

-

3.5.1.2

activates

670129

-

3.6.5.2

stimulates Rac1 as cardiovascular stimulus

734348

-

5.3.99.3

angiotension II infusion induces mRNA expression of mPGES-1, mPGES-2 and cytosolic PGE synthase

692588

-

7.2.2.3

stimulates the renal Na+-ATPase, reversed by Ang-(1-7) via MAS and the A779-sensitive MAS receptor in a Gs/PKA pathway, molecular mechanism, overview

711011

-

7.2.2.3

stimulates the proximal tubule Na+-ATPase through the AT1 receptor/phosphoinositide phospholipase Cbeta/protein kinase C pathway, molecular mechanisms, overview. Ang II induces fast and correlated activation of Na+-ATPase and PKC activities with the maximal effect of 115% activation observed at 1 min and sustained for 30 min. Involvement of phospholipase A2, PLA2, on the modulation of Na+-ATPase activity by Ang II, and modulation of the effect of Ang II on Na+-ATPase activity by PLA2 inhibitors, e.g. quinacrine, PACOCF3 and a specific inhibitor, BEL, overview

711296

-

7.2.2.3

angiotensin II has an activating and regulatory role for Na+-ATPase activity in healthy rats, and angiotensin II links the enzyme activity to hypertension in spontaneously hypertensive rats, where it has an inhibitory effect on Na+-ATPase activity. Ang II interacts with different receptors in spontaneously hypertensive rats and WKY wild-type rats

711297

-

7.2.2.3

physiological activation at femtomolar concentration. The activation by angiotensin II is completely abolished in the adult progeny of rats that are undernourished during lactation

720830

-

7.2.2.3

4 entries

Inhibitor in Enzyme-catalyzed Reactions (18 results)

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Show Inhibitors (18 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

3.4.11.2

-

683431

-

3.4.11.3

-

667548, 683431

-

3.4.11.7

competitive against Glu-4-methylcoumaryl-7-amide, IC50 is 0.065 mM in presence of Ca2+

665723

-

3.4.14.4

-

650445

-

3.4.14.9

0.3 mM, 22% inhibition

647182

-

3.4.15.1

angiotensin II shows selective competitive inhibition of the carboxy-terminal domain of human somatic ACE

732909

-

3.4.15.1

hydrolysis of hippuryl-His-Leu

81209

-

3.4.15.1

inhibits hydrolysis of angiotensin I and Gly-Ala-Ala

81263

-

3.4.15.1

-

81209, 81246, 81247, 81269, 81270, 81273, 81274

-

3.4.16.2

IC50: 3 mM, inhibits hydrolysis of Gly-Pro-4-nitroanilide

650716

-

3.4.16.2

IC50: 0.1 mM

651307

-

3.4.16.2

IC50: 0.002 mM

652251

-

3.4.16.2

-

664442

-

3.4.15.1

4 entries

3.4.16.2

4 entries

3.4.24.15

inhibits hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)

652505

-

3.4.24.16

degradation of 3-carboxy-7-methoxycoumaryl-Pro-Leu-Gly-Pro-D-Lys-dinitrophenyl

37083

-

3.4.24.16

inhibits hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)

652505

-

3.4.24.16

2 entries

3.5.3.18

1 microM, about 55% relative activity; 1 microM, about 55% relative activity

697831

-

7.2.2.3

angiotensin II has an activating and regulatory role for Na+-ATPase activity in healthy rats, and angiotensin II links the enzyme activity to hypertension in spontaneously hypertensive rats, where it has an inhibitory effect on Na+-ATPase activity. The Ang II inhibitory effect is completely reversed by a specific antagonist of AT2 receptor, PD123319. Ang II interacts with different receptors in spontaneously hypertensive rats and WKY wild-type rats

711297

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (16 results)

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Show Turnover Number (16 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

3.4.11.7

2.4

-

pH 7.4, 37°C, mutant enzyme wild-type enzyme N353Q

654587

3.4.11.7

2.76

-

wild-type, in the absence of CaCl2

683663

3.4.11.7

3

6

wild-type, in the absence of CaCl2

683663

3.4.11.7

3.01

-

wild-type, in the presence of 1.0 mM CaCl2

683663

3.4.11.7

3.22

-

mutant D221N, in the presence of 1.0 mM CaCl2

683663

3.4.11.7

3.88

-

mutant D221N, in the absence of CaCl2

683663

3.4.11.7

4.8

-

pH 7.4, 37°C, mutant enzyme wild-type enzyme N353A

654587

3.4.11.7

20

-

pH 7.4, 37°C, wild-type enzyme

654587

3.4.11.7

8 entries

3.4.14.1

87

-

removal of the first dipeptide

36137

3.4.17.23

12.8

-

37°C, pH 7.4

667485

3.4.17.23

1110

-

pH 7.4, 37°C

657967

3.4.17.23

2 entries

3.4.21.39

1.19

-

-

81383

3.4.21.9

0.4

-

in 0.1 M Tris-HCl buffer pH 8.0 at 37°C

667758

3.4.24.11

40

-

37°C, pH 7.4

667485

3.4.24.40

0.53

-

pH 8.6, 30°C

650288

3.4.24.40

6.08

-

pH 8.6, 30°C

650288

3.4.24.40

2 entries

K_M Value (23 results)

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Show KM Value (23 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

3.4.11.21

0.25

-

-

137168

3.4.11.7

0.062

-

pH 7.4, 37°C, mutant enzyme wild-type enzyme N353A

654587

3.4.11.7

0.073

-

pH 7.4, 37°C, wild-type enzyme

654587

3.4.11.7

0.161

-

pH 7.4, 37°C, mutant enzyme wild-type enzyme N353Q

654587

3.4.11.7

0.84

-

wild-type, in the presence of 1.0 mM CaCl2

683663

3.4.11.7

1.18

-

mutant D221N, in the absence of CaCl2

683663

3.4.11.7

1.22

-

mutant D221N, in the presence of 1.0 mM CaCl2

683663

3.4.11.7

2.85

-

wild-type, in the absence of CaCl2

683663

3.4.11.7

7 entries

3.4.14.1

0.34

-

-

36137

3.4.16.2

0.34

-

-

36274

3.4.16.2

1

-

-

36268

3.4.16.2

1

-

-

36270

3.4.16.2

3 entries

3.4.17.15

0.191

-

pH 8.1, 37°C

732609

3.4.17.23

0.005

-

pH 7.4, 37°C

657967

3.4.17.23

0.0057

-

37°C, pH 7.4

667485

3.4.17.23

0.053

-

pH 7.4, 37°C, mutant enzyme R514Q

692319

3.4.17.23

0.0586

-

pH 7.4, 37°C, wild-type enzyme

692319

3.4.17.23

4 entries

3.4.21.26

0.036

-

-

81354

3.4.21.39

0.85

-

-

81383

3.4.21.9

3.3

-

in 0.1 M Tris-HCl buffer pH 8.0 at 37°C

667758

3.4.24.11

0.179

-

37°C, pH 7.4

667485

3.4.24.60

0.063

-

-

31363

3.4.24.60

0.063

-

-

668827

3.4.24.60

2 entries

K_i Value (6 results)

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Show KI Value (6 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

TABLE ID

3.4.14.4

0.00066

-

37°C, pH 7.4

650445

22467

3.4.14.4

0.00083

-

37°C, pH 7.4

650445

22469

3.4.15.1

0.004

-

C-terminal domain of sACE, pH 7.5, temperature not specified in the publication

732909

23052

3.4.15.1

0.076

-

N-terminal domain of sACE, pH 7.5, temperature not specified in the publication

732909

23102

3.4.14.4

2 entries

3.4.15.1

2 entries

3.4.24.15

0.00812

-

inhibition of hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)

652505

31798

3.4.24.16

0.00795

-

inhibition of hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)

652505

31811

IC₅₀ Value (4 results)

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Show IC50 Value (4 entries)

EC NUMBER

IC50 VALUE

IC50 VALUE MAXIMUM

COMMENTARY

LITERATURE

3.4.11.7

0.065

-

competitive against Glu-4-methylcoumaryl-7-amide, IC50 is 0.065 mM in presence of Ca2+

665723

3.4.16.2

0.002

-

IC50: 0.002 mM

652251

3.4.16.2

0.1

-

IC50: 0.1 mM

651307

3.4.16.2

3

-

IC50: 3 mM, inhibits hydrolysis of Gly-Pro-4-nitroanilide

650716

3.4.16.2

3 entries

References & Links

Literature References (189)

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Show Reference (189 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

30274

1012011

Bromelain enzymes

1976

Murachi, T.

Methods Enzymol.

45

475-485

30299

956152

Purification and characterization of a proteinase from pineapple fruit, fruit bromelain FA2

1976

Yamada, F.; Takahashi, N.; Murachi, T.

J. Biochem.

79

1223-1234

30571

21699

Purification of an acid proteinase from Aspergillus saitoi and determination of peptide bond specificity

1977

Tanaka, N.; Takeuchi, M.; Ichishima, E.

Biochim. Biophys. Acta

485

406-416

31019

3105525

Characterization of meprin, a membrane-bound metalloendopeptidase from mouse kidney

1987

Butler, P.E.; McKay, M.J.; Bond, J.S.

Biochem. J.

241

229-235

31020

2461706

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Fajtova, P.; Stefanic, S.; Hradilek, M.; Dvorak, J.; Vondrasek, J.; Jilkova, A.; Ulrychova, L.; McKerrow, J.H.; Caffrey, C.R.; Mares, M.; Horn, M.

PLoS Negl. Trop. Dis.

9

e0003827

755153

28877217

Involvement of arginine 878 together with Ca2+ in mouse aminopeptidase A substrate specificity for N-terminal acidic amino-acid residues

2017

Couvineau, P.; de Almeida, H.; Maigret, B.; Llorens-Cortes, C.; Iturrioz, X.

PLoS ONE

12

e0184237

755158

29190734

A novel Porphyromonas gingivalis enzyme An atypical dipeptidyl peptidase III with an ARM repeat domain

2017

Hromic-Jahjefendic, A.; Jajcanin Jozic, N.; Kazazic, S.; Grabar Branilovic, M.; Karacic, Z.; Schrittwieser, J.H.; Das, K.M.P.; Tomin, M.; Oberer, M.; Gruber, K.; Abramic, M.; Tomic, S.

PLoS ONE

12

e0188915

Links to other databases for angiotensin II

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ChEBI

PubChem