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Ligand Angiotensin I

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (17 results)

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Show Natural Substrate (17 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.4.11.21

angiotensin + H2O = Asp + des-Asp-angiotensin

137169, 137168, 137167

-

3.4.15.1

angiotensin I + H2O = angiotensin II + His-Leu

709124, 707026, 708183, 708199, 708687, 708800, 708830, 710060, 707126, 708537, 709653, 755273, 652617, 650873, 707811, 707023, 708590, 697774, 709149

-

3.4.15.1

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

679708, 695587, 697020, 697516, 697714, 699475, 700299, 701190, 701430, 695446, 695492, 697774, 697821, 697822, 698423, 699285, 699747, 699781, 695571, 695798, 697524, 698406, 698416, 698425, 698426, 698430, 700690, 697146, 699887, 695904, 696268, 753311, 753643, 755108, 752610, 753955, 698092, 755554, 753829

-

3.4.15.1

2 entries

3.4.17.1

angiotensin I + H2O = ?

706874

-

3.4.17.23

angiotensin I + H2O = angiotensin-(1-9) + Leu

658884, 660025, 657531, 657967, 658455, 658963, 659147, 659172, 659198, 660035, 762787, 667166

-

3.4.17.23

angiotensin I + H2O = DRVYIHPFH + L-Leu

753311

-

3.4.17.23

2 entries

3.4.21.20

angiotensin I + H2O = angiotensin II + ?

683724

-

3.4.21.26

angiotensin I + H2O = ?

683926, 709476

-

3.4.21.39

angiotensin I + H2O = angiotensin II + ?

709684

-

3.4.21.39

angiotensin I + H2O = angiotensin II + His-Leu

695966, 701374, 752910, 697785, 700577, 732860, 731891, 732148, 732379, 732525, 732730, 732957, 732378, 732427, 654835

-

3.4.24.15

angiotensin I + H2O = ?

735106

-

3.4.24.15

angiotensin I + H2O = angiotensin-(1-7) + ?

733958

-

3.4.24.15

angiotensin-I + H2O = ?

683813

-

3.4.21.39

2 entries

3.4.24.15

3 entries

3.4.24.16

angiotensin I + H2O = ?

734522

-

3.4.24.18

angiotensin I + H2O = ?

733064

-

3.4.24.71

angiotensin I + H2O = ?

734021

-

3.4.24.71

angiotensin-I + H2O = ?

683696

-

3.4.24.71

2 entries

In Vivo Product in Enzyme-catalyzed Reactions (2 results)

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Show Natural Product (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.4.21.20

angiotensinogen + H2O = angiotensin I + ?

0

-

3.4.23.15

angiotensinogen + H2O = angiotensin I + angiotensinogen propeptide

0

-

Substrate in Enzyme-catalyzed Reactions (58 results)

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Show Substrate (58 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.1.3.48

angiotensin I + H2O = ? + phosphate

94969

-

3.4.11.21

angiotensin + H2O = Asp + des-Asp-angiotensin

137169, 137168, 137167

-

3.4.11.21

angiotensin I + H2O = ?

664909

-

3.4.11.21

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

664909

-

3.4.11.21

angiotensin I + H2O = Asp + des-Asp-angiotensin I

681000, 681632

-

3.4.11.21

angiotensin I + H2O = L-Asp + des-Asp-angiotensin I

707859

-

3.4.11.21

5 entries

3.4.11.22

DRVYIHPFHL + H2O = L-Asp + L-Arg + VYIHPFHL

680333

-

3.4.11.7

angiotensin I + H2O = ?

663609

-

3.4.11.7

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

36026

-

3.4.11.7

2 entries

3.4.14.9

DRVYIHPFHL + H2O = DRV + YIHPFHL

647183

-

3.4.15.1

angiotensin I + H2O = ?

668893, 731940

-

3.4.15.1

angiotensin I + H2O = angiotensin II + His-Leu

81270, 81209, 81273, 81274, 81241, 668570, 81275, 709124, 81212, 81213, 81215, 81233, 81235, 81236, 81237, 81238, 81239, 81245, 81246, 81247, 81248, 81250, 669424, 707026, 708183, 708199, 708687, 708800, 708830, 710060, 653416, 81261, 81263, 81266, 652617, 680278, 707126, 81269, 81214, 81227, 81257, 81258, 81259, 81287, 708537, 81286, 81285, 650873, 679999, 709653, 755273, 679858, 707811, 707023, 708590, 697774, 709149

-

3.4.15.1

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

679708, 695587, 697020, 697516, 697714, 699475, 700299, 701190, 701430, 695446, 695492, 697774, 697821, 697822, 698423, 699285, 699747, 699781, 695571, 695798, 697524, 698406, 698416, 698425, 698426, 698430, 700690, 697146, 699887, 695904, 696268, 753311, 753643, 755108, 752610, 753955, 698092, 755554, 753829

-

3.4.15.1

3 entries

3.4.15.5

angiotensin I + H2O = DRVYIHPF + His-Leu

707614

-

3.4.16.6

angiotensin 1 + H2O = ?

731176

-

3.4.17.1

angiotensin I + H2O = ?

706874, 704669

-

3.4.17.1

angiotensin I + H2O = angiotensin II + His-Leu

683036

-

3.4.17.1

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

36323

-

3.4.17.1

angiotensin I + H2O = des-Leu10 angiotensin I + Leu

683036

-

3.4.17.23

angiotensin I + H2O = angiotensin-(1-9) + Leu

679072, 679135, 679706, 667485, 668219, 668220, 679876, 658884, 679300, 660025, 657531, 657967, 658455, 658459, 658963, 659147, 659172, 659198, 660035, 678973, 692319, 694351, 762787, 681022, 667166, 678102, 693733

-

3.4.17.23

angiotensin I + H2O = DRVYIHPFH + L-Leu

753311

-

3.4.17.1

4 entries

3.4.17.23

2 entries

3.4.21.20

angiotensin I + H2O = angiotensin II + ?

683724

-

3.4.21.25

angiotensin I + H2O = ?

95358

-

3.4.21.26

angiotensin I + H2O = ?

81354, 683926, 709476, 81342, 653873

-

3.4.21.26

angiotensin I + H2O = DRVYIHP + FHL

755073

-

3.4.21.26

2 entries

3.4.21.35

angiotensin I + H2O = ?

647530

-

3.4.21.39

angiotensin I + H2O = angiotensin II + ?

709272, 678669, 679069, 680901, 681586, 682260, 681726, 708640, 709290, 709684

-

3.4.21.39

angiotensin I + H2O = angiotensin II + His-Leu

695966, 701374, 752910, 81372, 81374, 81375, 81379, 682307, 697785, 700577, 732860, 731891, 699923, 732148, 732379, 732525, 732730, 732957, 732378, 732427, 654835, 695395

-

3.4.21.39

2 entries

3.4.21.B21

angiotensin + H2O = ?

673907

-

3.4.22.53

angiotensin + H2O = ?

644032

-

3.4.23.18

angiotensin + H2O = ?

30559

-

3.4.23.29

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

30728

-

3.4.23.30

angiotensin + H2O = ?

30752, 668792

-

3.4.23.32

angiotensin I + H2O = ?

30762, 668804

-

3.4.24.1

angiotensin I + H2O = ?

36970

-

3.4.24.11

angiotensin + H2O = ?

735116

-

3.4.24.11

angiotensin I + H2O = ?

81609, 81644, 667485, 31020, 81637, 709308

-

3.4.24.11

2 entries

3.4.24.12

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

36991

-

3.4.24.15

angiotensin I + H2O = ?

735106, 652505

-

3.4.24.15

angiotensin I + H2O = angiotensin-(1-7) + ?

733958

-

3.4.24.15

angiotensin-I + H2O = ?

683813

-

3.4.24.16

angiotensin I + H2O = ?

734522, 652505, 754221

-

3.4.24.16

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

37075, 37078, 37070, 37061, 37084

-

3.4.24.18

angiotensin I + H2O = ?

733064, 652104

-

3.4.24.18

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

31021, 31031, 31020

-

3.4.24.30

angiotensin I + H2O = ?

668832

-

3.4.24.30

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

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 I + H2O = DRVY + IHPFLHL + DRVYI + HPFHL

650288

-

3.4.24.42

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

36970

-

3.4.24.48

angiotensin + H2O = ?

668851

-

3.4.24.48

angiotensin I + H2O = ?

36970

-

3.4.24.48

2 entries

3.4.24.50

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

668843, 31291

-

3.4.24.56

angiotensin + H2O = ?

755263

-

3.4.24.71

angiotensin I + H2O = ?

734021

-

3.4.24.71

angiotensin-I + H2O = ?

683696

-

3.4.24.B14

angiotensin + H2O = ?

669280

-

3.4.24.B14

angiotensin I + H2O = ?

651958, 692350

-

3.4.24.B14

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

690798

-

3.4.24.71

2 entries

3.4.24.B14

3 entries

Product in Enzyme-catalyzed Reactions (16 results)

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Show Product (16 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.1.3.1

phospho-Tyr angiotensin + H2O = angiotensin + phosphate

0

-

3.1.3.16

phosphoangiotensin + H2O = angiotensin + phosphate

0

-

3.1.3.16

DRVY(P)IHPFHL + H2O = DRVYIHPFHL + phosphate

0

-

3.1.3.16

2 entries

3.1.3.48

DRVpYIHPFHL + H2O = DRVYIHPFHL + phosphate

0

-

3.4.17.15

angiotensin-(1-12) + H2O = angiotensin I + ?

0

-

3.4.21.20

angiotensinogen + H2O = angiotensin I + ?

0

-

3.4.21.35

angiotensinogen + H2O = angiotensin

0

-

3.4.21.54

Synthetic tetradecapeptide renin substrate + H2O = Angiotensin I

29366, 0

-

3.4.23.15

angiotensinogen + H2O = angiotensin I + ?

650745, 95772, 0, 95799, 95774, 95790, 95797

-

3.4.23.15

angiotensinogen + H2O = angiotensin I + angiotensinogen propeptide

0

-

3.4.23.15

human angiotensinogen + H2O = angiotensin I + VIHN

0

-

3.4.23.15

porcine angiotensinogen + H2O = angiotensin I + angiotensinogen propeptide

0

-

3.4.23.15

recombinant ovine angiotensinogen from CHO cells + H2O = angiotensin I + angiotensinogen propeptide

0

-

3.4.23.15

recombinant ovine angiotensinogen from Escherichia coli + H2O = angiotensin I + angiotensinogen propeptide

0

-

3.4.23.15

H-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-Thr-Glu + H2O = H-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu + Val-Ile-His-Thr-Glu

95776

-

3.4.23.15

7 entries

3.4.23.34

Human renin substrate + H2O = Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu + Val-Ile-His

30798

-

Activator in Enzyme-catalyzed Reactions (2 results)

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Show Activating Compound (2 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.1.1.189

at 0.1 mM concentration

389477

-

2.7.11.12

causes an increase in expression of isozyme cGKIbeta, and a decrease in expression of isozyme cGKIalpha

661497

-

Inhibitor in Enzyme-catalyzed Reactions (14 results)

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Show Inhibitors (14 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

1.6.3.1

angiotensin-(1-7) decreases the elevated levels of renal NADPH oxidase activity and attenuates the activation of subunit NOX-4 gene expression in the diabetic hypertensive kidney. Angiotensin-(1-7) treatment increases sodium excretion but does not affect mean arterial pressure in diabetic hypertensive rats. The significant increase in urinary protein in the diabetic compared to control hypertensive rat is reduced by angiotensin-(1-7). Angiotensin-(1-7) treatment also attenuates the diabetes-induced increase in renal vascular responsiveness to endothelin-1, norepinephrine, and angiotensin II in hypertensive rats, but significantly increases the vasodilation of the renal artery of hypertensive and diabetic hypertensive rats to the vasodilator agonists

684312

-

2.7.11.12

causes a decrease in expression of isozyme cGKIalpha, and an increase in expression of isozyme cGKIbeta

661497

-

3.4.11.3

-

35916

-

3.4.15.1

-

679672, 81253

-

3.4.16.2

inhibits the mutant DELTA317-496 in a dose-dependent manner

696003

-

3.4.17.23

-

658963, 668219

-

3.4.23.31

-

30559

-

3.4.24.11

-

670479

-

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

-

37068

-

3.4.24.16

inhibits 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.B14

-

669280

-

3.4.24.B14

-

690798

-

3.4.24.16

3 entries

3.4.24.B14

2 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (33 results)

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Show Turnover Number (33 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

3.4.15.1

0.03

0.55

35°C, pH 7.0, 0 mM NaCl

668570

3.4.15.1

0.057

0.65

35°C, pH 8.0, 0 mM NaCl

668570

3.4.15.1

0.057

0.65

35°C, pH 8.0, 100 mM NaCl

668570

3.4.15.1

0.58

-

37°C

668893

3.4.15.1

1.4

-

pH 7.5, 37°C, enzyme from brain, 200 mM NaCl

653416

3.4.15.1

2.95

-

detergent-solubilized enzyme

81270

3.4.15.1

6.58

-

trypsin-extracted enzyme

81270

3.4.15.1

6.83

-

35°C, pH 7.0, 100 mM NaCl

668570

3.4.15.1

6.84

-

35°C, pH 7.0, 0 mM NaCl

668570

3.4.15.1

7.88

-

-

679858

3.4.15.1

8.33

-

-

81237

3.4.15.1

8.7

-

37°C

668893

3.4.15.1

10.78

-

35°C, pH 8.0, 100 mM NaCl

668570

3.4.15.1

11.06

-

35°C, pH 8.0, 0 mM NaCl

668570

3.4.15.1

12

-

enzyme from testis

81227

3.4.15.1

13.2

-

-

81209

3.4.15.1

13.2

-

enzyme from testis

81257

3.4.15.1

13.5

-

enzyme from lung

81227, 81257

3.4.15.1

52

-

37°C, pH 7.5, wild-type enzyme

669424

3.4.15.1

60

-

37°C, pH 7.5, mutant enzyme R1098Q

669424

3.4.15.1

20 entries

3.4.17.1

8.23

-

in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C

704669

3.4.17.23

2

-

pH 6.5, room temperature

658963, 659172

3.4.17.23

2.9

-

37°C, pH 7.4

667485

3.4.17.23

2 entries

3.4.21.26

0.85

-

-

81342

3.4.21.39

65

-

-

81375

3.4.21.39

140

-

glycosylated enzyme

81374

3.4.21.39

143

-

deglycosylated enzyme

81374

3.4.21.39

149

-

-

81383

3.4.24.11

0.0551

-

37°C, pH 7.4

667485

3.4.24.11

8.2

-

wild-type enzyme, pH and temperature not specified in the publication

735116

3.4.24.40

1.52

-

pH 8.6, 30°C

650288

3.4.24.40

2.94

-

pH 8.6, 30°C

650288

3.4.21.39

4 entries

3.4.24.11

2 entries

3.4.24.40

2 entries

3.4.24.B14

3

-

37°C

690798

K_M Value (40 results)

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Show KM Value (40 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

3.4.11.21

0.064

-

-

664909

3.4.15.1

0.009

-

enzyme from lung and testis

81257

3.4.15.1

0.01

-

-

81235

3.4.15.1

0.016

-

recombinant enzyme

81212

3.4.15.1

0.028

-

37°C

668893

3.4.15.1

0.0308

-

-

679858

3.4.15.1

0.04

-

pH 7.5, 37°C, enzyme from brain, 200 mM NaCl

653416

3.4.15.1

0.052

-

37°C, pH 7.5, wild-type enzyme

669424

3.4.15.1

0.062

-

lung enzyme

81236

3.4.15.1

0.065

-

detergent-solubilized enzyme

81270

3.4.15.1

0.067

-

37°C

668893

3.4.15.1

0.07

-

-

81209

3.4.15.1

0.071

-

-

81245

3.4.15.1

0.076

-

kidney enzyme

81236

3.4.15.1

0.076

-

serum enzyme

81274

3.4.15.1

0.078

-

lung enzyme

81274

3.4.15.1

0.078

-

trypsin-extracted enzyme

81270

3.4.15.1

0.09

-

enzyme from testis and lung

81227

3.4.15.1

0.1

-

37°C, pH 7.5, mutant enzyme R1098Q

669424

3.4.15.1

0.119

-

-

81287

3.4.15.1

0.21

-

pH 7.5, 0.2 mM NaCl

81233

3.4.15.1

0.42

-

pH 9.0, 0.5 mM NaCl

81233

3.4.15.1

0.54

-

pH 6.0, without NaCl

81233

3.4.15.1

0.82

-

35°C, pH 7.0, 100 mM NaCl

668570

3.4.15.1

1.04

-

35°C, pH 8.0, 100 mM NaCl

668570

3.4.15.1

1.23

-

35°C, pH 8.0, 0 mM NaCl

668570

3.4.15.1

2.7

-

35°C, pH 7.0, 0 mM NaCl

668570

3.4.17.1

0.227

-

in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C

704669

3.4.17.1

0.78

-

-

36323

3.4.17.23

0.0069

-

-

658963

3.4.17.23

0.0868

-

37°C, pH 7.4

667485

3.4.15.1

26 entries

3.4.17.1

2 entries

3.4.17.23

2 entries

3.4.21.26

0.016

-

-

81354

3.4.21.39

0.0223

-

deglycosylated enzyme

81374

3.4.21.39

0.0255

-

glycosylated enzyme

81374

3.4.21.39

0.067

-

-

81375

3.4.21.39

0.398

-

-

81379

3.4.24.11

0.0004

-

-

81637

3.4.24.11

0.0086

-

wild-type enzyme, pH and temperature not specified in the publication

735116

3.4.24.11

0.036

-

-

81644

3.4.24.11

34.1

-

37°C, pH 7.4

667485

3.4.21.39

4 entries

3.4.24.11

4 entries

K_i Value (7 results)

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Show KI Value (7 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

3.4.15.1

0.000002747

-

-

679672

3.4.17.23

0.0022

-

-

668219, 658963

3.4.24.11

0.036

-

hydrolysis of Leu5-enkephalin

670479

3.4.24.15

0.00429

-

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

652505

3.4.24.16

0.00535

-

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

652505

3.4.24.B14

0.006

-

37°C

690798

3.4.24.B14

0.008

-

37°C, pH 7.2, wild-type enzyme

669280

3.4.24.B14

2 entries

IC₅₀ Value (1 result)

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Show IC50 Value (1 entry)

EC NUMBER

IC50 VALUE

IC50 VALUE MAXIMUM

COMMENTARY

LITERATURE

3.4.16.2

1

-

-

696003

References & Links

Literature References (247)

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Show Reference (247 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

29366

6337154

Purification and properties of renin and gamma-renin from the mouse submaxillary gland

1983

Poe, M.; Wu, J.K.; Florance, J.R.; Rodkey, J.A.; Bennett, C.D.; Hoogsteen, K.

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258

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30559

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Comparative study on the specificities of several fungal aspartic and acidic proteinases towards the tetradecapeptide of a renin substrate

1988

Majima, E.; Oda, K.; Murao, S.; Ichishima, E.

Agric. Biol. Chem.

52

787-793

30728

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Substrate specificity of a carboxyl proteinase from Irpex lacteus

1983

Kobayashi, H.; Kusakabe, I.; Murakami, K.

Agric. Biol. Chem.

47

1921-1923

30752

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Carboxyl proteinase from the wood deteriorating basidiomycete Pycnoporus coccineus: substrate specificity with oxidized insulin peptide B1 .apprx. B16 and B15 .apprx. B24, angiotensin and proangiotensin

1981

Kumagai, H.; Matsue, M.; Majima, E.; Tomoda, K.; Ichishima, E.

Agric. Biol. Chem.

45

981-985

30762

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Studies on new acid proteases from Scytalidium lignicolum ATCC 24568. Part IX. Additional evidence for the identity of Scytalidium lignicolum acid proteinases with the carboxyl proteinase group: the interaction between angiotensin I and S-PI-insensitive acid proteinases by means of a zinc(II)-dye complex as a probe

1986

Oda, K.; Murao, S.

Agric. Biol. Chem.

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1995-2001

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Procathepsin E and cathepsin E

1995

Kageyama, T.

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31020

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The metabolism of neuropeptides. Hydrolysis of peptides by the phosphoramidon-insensitive rat kidney enzyme endopeptidase-2 and by rat microvillar membranes

1988

Stephenson, S.L.; Kenny, A.J.

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31021

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N-Benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase: a metalloendopeptidase of the human intestinal microvillus membrane which degrades biologically active peptides

1988

Sterchi, E.E.; Naim, H.Y.; Lentze, M.J.; Hauri, H.P.; Fransen, J.A.M.

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Purification and substrate specificity of a strongly hydrophobic extracellular metalloendopeptidase (gelatinase) from Streptococcus faecalis (strain 0G1-10)

1989

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Purification and some characteristics of a zinc metalloprotease from the venom of Bothrops jararaca (jararaca)

1989

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Toxicon

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35916

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Properties of aminopeptidase activity involved in the conversion of vasopressin by rat brain membranes [published erratum appears in Peptides 1994;15(5):933

1993

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A soluble aspartate aminopeptidase from dog kidney

1971

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1987

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1987

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1991

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Biochemistry

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1998

Rioli, V.; Kato, A.; Portaro, F.C.V.; Cury, G.K.; te Kaat, K.; Vincent, B.; Checler, F.; Camargo, A.C.M.; Glucksman, M.J.; Roberts, J.L.; Hirose, S.; Ferro, E.S.

Biochem. Biophys. Res. Commun.

250

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37068

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1986

Checler, F.; Vincent, J.P.; Kitabgi, P.

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261

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1988

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37075

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1996

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270

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37083

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1997

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37084

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1991

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81209

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1976

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81212

1848554

Expression and characterization of recombinant human angiotensin I-converting enzyme. Evidence for a C-terminal transmembrane anchor and for a proteolytic processing of the secreted recombinant and plasma enzymes

1991

Wei, L.; Alhenc-Gelas, F.; Soubrier, F.; Michaud, A.; Corvol, P.; Clauser, E.

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266

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81213

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Human peptidyl dipeptidase (converting enzyme, kininase II)

1981

Stewart, T.A.; Weare, J.A.; Erdös, E.G.

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80

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81214

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1973

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293

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81215

228989

Development of specific inhibitors of angiotensin I converting enzyme (kininase II)

1979

Cushman, D.W.; Cheung, H.S.; Sabo, E.F.; Rubin, B.; Ondetti, M.A.

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38

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81227

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Angiotensin-converting enzyme: immunologic, structural, and developmental aspects

1983

Soffer, R.L.; El-Dorry, H.A.

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81233

2846041

Catalysis of angiotensin I hydrolysis by human angiotensin-converting enzyme: effect of chloride and pH

1988

Ehlers, M.R.W.; Kirsch, R.E.

Biochemistry

27

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81235

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Affinity chromatography and some properties of the angiotensin-converting enzyme from human heart

1987

Sakharov, I.Y.; Danilov, S.M.; Dukhanina, E.A.

Biochim. Biophys. Acta

923

143-149

81236

3017438

Rapid affinity chromatographic purification of human lung and kidney angiotensin-converting enzyme with the novel N-carboxyalkyl dipeptide inhibitor N-[1(S)-carboxy-5-aminopentyl]glycylglycine

1986

Ehlers, M.R.W.; Maeder, D.L.; Kirsch, R.E.

Biochim. Biophys. Acta

883

361-372

81237

2987059

Structure and functions of human angiotensin I converting enzyme (kininase II)

1985

Erdös, E.G.; Skidgel, R.A.

Biochem. Soc. Trans.

13

42-44

81238

2999099

Angiotensin-converting enzyme from human tissues. Physicochemical, catalytic, and immunological properties

1985

Lanzillo, J.J.; Stevens, J.; Dasarathy, Y.; Yotsumoto, H.; Fanburg, B.L.

J. Biol. Chem.

260

14938-14944

81239

2989307

Rapid purification of human placental angiotensin I converting enzyme by captopril affinity chromatography

1985

Taira, H.; Mizutani, S.; Kurauchi, O.; Narita, O.; Tomoda, Y.

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339

399-403

81241

7674927

Peptidyl dipeptidase A: angiotensin I-converting enzyme

1995

Corvol, P.; Williams, T.A.; Soubrier, F.

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248

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81245

6264817

Purification of human serum angiotensin I-converting enzyme by affinity chromatography

1981

Harris, R.B.; Ohlsson, J.T.; Wilson, I.B.

Anal. Biochem.

111

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81246

202323

Properties of three different forms of angiotensin I-converting enzyme from human lung

1978

Nishimura, K.; Yoshida, N.; Hiwada, K.; Ueda, E.; Kokubu, T.

Biochim. Biophys. Acta

522

229-237

81247

200263

Angiotensin I converting enzyme from human plasma

1977

Lanzillo, J.J.; Fanburg, B.L.

Biochemistry

16

5491-5495

81248

19071

Purification of angiotensin I-converting enzyme from human lung

1977

Nishimura, K.; Yoshida, N.; Hiwada, K.; Ueda, E.; Kokubu, T.

Biochim. Biophys. Acta

483

398-408

81250

207335

Dipeptidyl carboxypeptidase from human seminal plasma

1978

Depierre, D.; Bargetzi, J.P.; Roth, M.

Biochim. Biophys. Acta

523

469-476

81253

6284250

Angiotensin I converting enzyme of rat intestinal and vascular surface membrane

1982

Ward, P.E.; Sheridan, M.A.

Biochim. Biophys. Acta

716

208-216

81257

6754723

Molecular and catalytic properties of rabbit testicular dipeptidyl carboxypeptidase

1982

El-Dorry, H.A.; Bull, H.G.; Iwata, K.; Thornberry, N.A.; Cordes, E.H.; Soffer, R.L.

J. Biol. Chem.

257

14128-14133

81258

186121

Solubilization of angiotensin I-coverting enzyme from rabbit lung using trypsin treatment

1976

Nishimura, K.; Hiwada, K.; Ueda, E.; Kokubu, T.

Biochim. Biophys. Acta

452

144-150

81259

169257

Pulmonary angiotensin-converting enzyme. Structural and catalytic properties

1975

Das, M.; Soffer, R.L.

J. Biol. Chem.

250

6762-6768

81261

4366382

Angiotensin I-converting enzyme of the kidney cortex

1974

Oshima, G.; Gecse, A.; Erdös, E.G.

Biochim. Biophys. Acta

350

26-37

81263

4340117

Angiotensin-converting enzyme and a second dipeptidyl carboxypeptidase from hog plasma

1972

Angus, C.W.; Lee, H.J.; Wilson, I.B.

Biochim. Biophys. Acta

276

228-233

81266

2439065

Isolation of two differentially glycosylated forms of peptidyl-dipeptidase A (angiotensin converting enzyme) from pig brain: a re-evaluation of their role in neuropeptide metabolism

1987

Hooper, N.M.; Turner, A.J.

Biochem. J.

241

625-633

81269

2851588

Molecular and catalytic properties of angiotensin converting enzyme-I from bovine seminal plasma

1988

Sharma, M.; Singh, U.S.

J. Biochem.

104

57-61

81270

1311747

Characterization of chicken lung angiotensin I-converting enzyme

1992

Polanco, M.J.; Miguel, J.L.; Agapito, M.T.; Recio, J.M.

J. Endocrinol.

132

261-268

81273

2990346

Enkephalin-degrading dipeptidyl carboxypeptidase in guinea pig serum: its properties and action on bioactive peptides

1985

Kase, R.; Hazato, T.; Shimamura, M.; Kiuchi, Y.; Katayama, T.

Arch. Biochem. Biophys.

240

330-336

81274

182273

Angiotensin I-converting enzyme from guinea pig lung and serum. A comparison of some kinetic and inhibition properties

1976

Lanzillo, J.J.; Fanburg, B.L.

Biochim. Biophys. Acta

445

161-168

81275

2841312

The isolation of angiotensin-converting enzyme cDNA

1988

Bernstein, K.E.; Martin, B.M.; Bernstein, E.A.; Linton, J.; Striker, L.; Striker, G.

J. Biol. Chem.

263

11021-11024

81285

1368555

Purification and some properties of dipeptidyl carboxypeptidase from Bacillus pumilus

1990

Nagamori, Y.; Fujishima, N.; Okada, S.

Agric. Biol. Chem.

54

999-1005

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

81287

1368711

Enzymatic properties of dipeptidyl carboxypeptidase from Bacillus pumilus

1991

Nagamori, Y.; Kusaka, K.; Fujishima, N.; Okada, S.

Agric. Biol. Chem.

55

1695-1699

81342

3071531

Thiazolidine derivatives as potent inhibitors specific for prolyl endopeptidase

1988

Tsuru, D.; Yoshimoto, T.; Koriyama, N.; Furukawa, S.

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580-586

81354

1644866

Prolyl endopeptidase purified from granulomatous inflammation in mice

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Nozaki, Y.; Sato, N.; Iida, T.; Hara, K.; Fukuyama, K.; Epstein, W.L.

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81372

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The 2.2 A crystal structure of human chymase in complex with succinyl-Ala-Ala-Pro-Phe-chloromethylketone: structural explanation for its dipeptidyl carboxypeptidase specificity

1999

Pereira, P.J.B.; Wang, Z.M.; Rubin, H.; Huber, R.; Bode, W.; Schechter, N.M.; Strobl, S.

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163-173

81374

10082988

Lack of effect of carbohydrate depletion on some properties of human mast cell chymase

1999

Takao, K.; Takai, S.; Shiota, N.; Song, K.; Nishimura, K.; Ishihara, T.; Miyazaki, M.

Biochim. Biophys. Acta

1427

74-81

81375

9352125

Characterization of chymase from human vascular tissues

1997

Takai, S.; Shiota, N.; Sakaguchi, M.; Muraguchi, H.; Matsumura, E.; Miyazaki, M.

Clin. Chim. Acta

265

13-20

81379

8226889

Reaction of human chymase with reactive site variants of alpha 1-antichymotrypsin. Modulation of inhibitor versus substrate properties

1993

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23626-23633

81383

8632712

Purification and characterization of angiotensin II-generating chymase from hamster cheek pouch

1996

Takai, S.; Shiota, N.; Yamamoto, D.; Okunishi, H.; Miyazaki, M.

Life Sci.

58

591-597

81609

2521610

Neutral endopeptidase 24.11 (enkephalinase) and related regulators of peptide hormones

1989

Erdös, E.G.; Skidgel, R.A.

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81637

8806762

Heterologous expression and characterization of recombinant Lactococcus lactis neutral endopeptidase (neprilysin)

1996

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333

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81644

8387132

A comparison of the properties and enzymatic activities of three angiotensin processing enzymes: angiotensin converting enzyme, prolyl endopeptidase and neutral endopeptidase 24.11

1993

Welches, W.R.; Broshihan, K.B.; Ferrario, C.M.

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1461-1480

94969

2844226

Purification and physicochemical characterization of a human placental acid phosphatase possessing phosphotyrosyl protein phosphatase activity

1988

Waheed, A.; Laidler, P.M.; Wo, Y.Y.P.; Van Etten, R.L.

Biochemistry

27

4265-4273

95358

8586630

Cleavage specificity of cucumisin, a plant serine protease

1995

Uchikoba, T.; Yonezawa, H.; Kaneda, M.

J. Biochem.

117

1126-1130

95772

1732722

Stable expression, secretion, and characterization of active human renin in mammalian cells

1991

Norman, J.A.; Hadjilambris, O.; Baska, R.; Sharp, D.Y.; Kumar, R.

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95774

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Role of the tissue renin-angiotensin system in the action of angiotensin-converting enzyme inhibitors

1995

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Proc. Soc. Exp. Biol. Med.

208

391-396

95776

7043197

Renin

1981

Slater, E.E.

Methods Enzymol.

80

427-442

95790

1600638

Expression of rat renin in mammalian cells and its purification

1992

Yamauchi, T.; Suzuki, F.; Takahashi, A.; Tsutsumi, I.; Hori, H.; Watanabe, T.; Ishizuka, Y.; Nakamura, Y.; Muakami, K.

Clin. Exp. Hypertens. A

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95797

1848255

Purification and amino-terminal sequence of rat kidney renin: Evidence for a two-chain structure

1991

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29-33

95799

2184838

Substrate specificity and inhibitor structure-activity relationships of recombinant human renin: Implications in the in vivo evaluation of renin inhibitors

1990

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Biotechnol. Appl. Biochem.

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161-175

137167

10871154

Comparative distribution of glutamyl and aspartyl aminopeptidase activities in mouse organs

2000

Ramirez-Exposito, M.J.; Martinez, J.M.; Prieto, I.; Alba, F.; Ramirez, M.

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161-163

137168

9632644

Purification, characterization and cloning of a cytosolic aspartyl aminopeptidase

1998

Wilk, S.; Wilk, E.; Magnusson, R.P.

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273

15961-15970

137169

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Decrease in cytosolic aspartyl-aminopeptidase but not in alanyl-aminopeptidase activity in the frontal cortex of the aged rat

1995

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389477

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Purification and regulatory properties of chicken heart prostaglandin E 9-ketoreductase

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644032

6094523

Purification and characterization of a calcium-activated neutral protease from monkey brain and its action on neuropeptides

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647183

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Rat tripeptidyl peptidase I: molecular cloning, functional expression, tissue localization and enzymatic characterization

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382

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647530

1320938

Biochemical characterization and substrate specificity of rat prostate kallikrein (S3): comparison with tissue kallikrein, tonin and T-kininogenase

1992

Wang, C.; Tang, C.Q.; Zhou, G.X.; Chao, L.; Chao, J.

Biochim. Biophys. Acta

1121

309-316

650288

9748654

Specificity of Pseudomonas aeruginosa serralysin revisited, using biologically active peptides as substrates

1998

Louis, D.; Bernillon, J.; Wallach, J.M.

Biochim. Biophys. Acta

1387

378-386

650745

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Characterization of renin mRNA expression and enzyme activity in rat and mouse mesangial cells

2002

Andrade, A.Q.; Casarini, D.E.; Schor, N.; Boim, M.A.

Braz. J. Med. Biol. Res.

35

17-24

650873

10825662

Purification and characterization of a dipeptidyl carboxypeptidase from the polychaete Neanthes virens resembling angiotensin I converting enzyme

2000

Kawamura, T.; Oda, T.; Muramatsu, T.

Comp. Biochem. Physiol. B

126

29-37

651958

10542292

Molecular identification and characterization of novel membrane-bound metalloprotease, the soluble secreted form of which hydrolyzes a variety of vasoactive peptides

1999

Ikeda, K.; Emoto, N.; Raharjo, S.B.; Nurhantari, Y.; Saiki, K.; Yokoyama, M.; Matsuo, M.

J. Biol. Chem.

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652104

11278902

Marked differences between metalloproteases meprin A and B in substrate and peptide bond specificity

2001

Bertenshaw, G.P.; Turk, B.E.; Hubbard, S.J.; Matters, G.L.; Bylander, J.E.; Crisman, J.M.; Cantley, L.C.; Bond, J.S.

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276

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652505

12500972

Novel natural peptide substrates for endopeptidase 24.15, neurolysin, and angiotensin-converting enzyme

2003

Rioli, V.; Gozzo, F.C.; Heimann, A.S.; Linardi, A.; Krieger, J.E.; Shida, C.S.; Almeida, P.C.; Hyslop, S.; Eberlin, M.N.; Ferro, E.S.

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278

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652617

12450545

Purification of angiotensin I converting enzyme from pig lung using concanavalin-A Sepharose chromatography

2003

Andujar-Sanchez, M.; Camara-Artigas, A.; Jara-Perez, V.

J. Chromatogr. B

783

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653416

14499287

Kinetic-controlled hydrolysis of Leu-Val-Val-hemorphin-7 catalyzed by angiotensin-converting enzyme from rat brain

2003

Hayakari, M.; Satoh, K.; Izumi, H.; Kudoh, T.; Asano, J.; Yamazaki, T.; Tsuchida, S.

Peptides

24

1075-1082

653873

-

Proline-specific endopeptidases

2003

Besedin, D.V.; Rudenskaya, G.N.

Russ. J. Bioorg. Chem.

29

1-17

654835

12007614

Lys40 but not Arg143 influences selectivity of angiotensin conversion by human alpha-chymase

2002

Muilenburg, D.J.; Raymond, W.W.; Wolters, P.J.; Caughey, G.H.

Biochim. Biophys. Acta

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346-356

657531

12531198

Development of intramolecularly quenched fluorescent peptides as substrates of angiotensin-converting enzyme 2

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Yan, Z.H.; Ren, K.J.; Wang, Y.; Chen, S.; Brock, T.A.; Rege, A.A.

Anal. Biochem.

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657967

14609329

Angiotensin-converting enzyme-2 (ACE2): comparative modeling of the active site, specificity requirements, and chloride dependence

2003

Guy, J.L.; Jackson, R.M.; Acharya, K.R.; Sturrock, E.D.; Hooper, N.M.; Turner, A.J.

Biochemistry

42

13185-13192

658455

10969042

A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9

2000

Donoghue, M.; Hsieh, F.; Baronas, E.; Godbout, K.; Gosselin, M.; Stagliano, N.; Donovan, M.; Woolf, B.; Robison, K.; Jeyaseelan, R.; Breitbart, R.E.; Acton, S.

Circ. Res.

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Effects of chymase inhibitor on angiotensin II-induced abdominal aortic aneurysm development in apolipoprotein E-deficient mice

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Probing the basis of domain-dependent inhibition using novel ketone inhibitors of angiotensin-converting enzyme

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Characterization of angiotensin-converting enzyme expression during epidermis morphogenesis in humans: a potential marker for epidermal stem cells

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Matrix metalloproteinase-9/tissue inhibitors of metalloproteinase-1 expression and atrial structural remodeling in a dog model of atrial fibrillation: inhibition with angiotensin-converting enzyme

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Pharmacogenetics of ACE inhibition in stable coronary artery disease: steps towards tailored drug therapy

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Hydrolyzates of silkworm pupae (Bombyx mori) protein is a new source of angiotensin I-converting enzyme inhibitory peptides (ACEIP)

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Injections of angiotensin-converting enzyme 2 inhibitor MLN4760 into nucleus tractus solitarii reduce baroreceptor reflex sensitivity for heart rate control in rats

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Characterization of the bovine angiotensin converting enzyme promoter: essential roles of Egr-1, ATF-2 and Ets-1 in the regulation by phorbol ester

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Investigations into inhibitor type and mode, simulated gastrointestinal digestion, and cell transport of the angiotensin I-converting enzyme-inhibitory peptides in Pacific hake (Merluccius productus) fillet hydrolysate

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Angiotensin receptor blockers are superior to angiotensin-converting enzyme inhibitors in the suppression of hepatic fibrosis in a bile duct-ligated rat model

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