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Ligand MET-enkephalin

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

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

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Show Natural Substrate (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.4.11.2

Met-enkephalin + H2O = Met + enkephalin

666240

-

3.5.1.12

Met-enkephalin + H2O = ?

171928, 171935

-

In Vivo Product in Enzyme-catalyzed Reactions (4 results)

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Show Natural Product (4 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.8.4.11

Tyr-Gly-Gly-Phe-L-methionine-(S)-S-oxide + thioredoxin = Tyr-Gly-Gly-Phe-L-methionine + thioredoxin disulfide + H2O

-

-

3.4.22.15

BAM-22P + H2O = (Met)enkephalin + ?

-

-

3.4.22.38

beta-endorphin + H2O = Met-enkephalin + ?

-

-

3.4.22.43

proenkephalin + H2O = (Met)enkephalin + ?

-

-

Substrate in Enzyme-catalyzed Reactions (23 results)

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Show Substrate (23 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.1.1.7

[met5] enkephalins + H2O = Tyr + Met

114159

-

3.4.11.14

Met-enkephalin + H2O = ?

682118

-

3.4.11.2

Met-enkephalin + H2O = Met + enkephalin

666240

-

3.4.11.2

Met5-enkephalin + H2O = tyrosin + (2-5)Met5-enkephalin

35867, 35871

-

3.4.11.2

2 entries

3.4.11.24

Met-enkephalin + H2O = ?

665642

-

3.4.11.6

Met-enkephalin + H2O = ?

731349

-

3.4.14.1

Met-enkephalin + H2O = Tyr-Gly + Gly-Phe-Met

36118

-

3.4.14.4

Met-enkephalin + H2O = ?

36179

-

3.4.14.4

Tyr-Gly-Gly-Phe-Met + H2O = ?

668562

-

3.4.15.1

Met5-enkephalin + H2O = Tyr-Gly-Gly + Phe-Met

81273, 81241, 81237, 81238

-

3.4.15.1

Tyr-Gly-Gly-Phe-Met + H2O = Tyr-Gly-Gly + Phe-Met

650873

-

3.4.15.1

[Met5]enkephalin + H2O = ?

668570

-

3.4.14.4

2 entries

3.4.15.1

3 entries

3.4.17.1

Met-enkephalin + H2O = ?

704669

-

3.4.22.15

Tyr-Gly-Gly-Phe-Met + H2O = Tyr-Gly + Gly-Phe-Met

647910

-

3.4.22.53

Met-enkephalin + H2O = ?

644032

-

3.4.24.11

Met-enkephalin + H2O = ?

81637

-

3.4.24.11

Tyr-Gly-Gly-Phe-Met + H2O = Tyr-Gly-Gly + Phe-Met

81644, 81639, 81628, 81630

-

3.4.24.11

2 entries

3.4.24.42

Met-enkephalin + H2O = Tyr-Gly-Gly + Phe-Met

36970

-

3.4.24.48

(Met)enkephalin + H2O = ?

668851

-

3.4.24.48

Met-enkephalin + H2O = Tyr-Gly-Gly + Phe-Met

36970

-

3.4.24.48

2 entries

3.4.24.77

Tyr-Gly-Gly-Phe-Met + H2O = Tyr-Gly-Gly + Phe-Met

667346

-

3.4.24.B14

Tyr-Gly-Gly-Phe-Met + H2O = Tyr-Gly-Gly + Phe-Met

690798

-

3.5.1.12

Met-enkephalin + H2O = ?

171928, 171935

-

Product in Enzyme-catalyzed Reactions (19 results)

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Show Product (19 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.8.4.11

L-methionine sulfoxide enkephalin + thioredoxin = L-methionine enkephalin

-

-

1.8.4.11

Tyr-Gly-Gly-Phe-L-methionine-(S)-S-oxide + DTT = Tyr-Gly-Gly-Phe-L-methionine + DTT disulfide + H2O

-

-

1.8.4.11

Tyr-Gly-Gly-Phe-L-methionine-(S)-S-oxide + thioredoxin = Tyr-Gly-Gly-Phe-L-methionine + thioredoxin disulfide + H2O

-

-

1.8.4.11

3 entries

1.8.4.12

L-methionine sulfoxide enkephalin + thioredoxin = L-methionine enkephalin

-

-

1.8.4.13

L-methionine sulfoxide enkephalin + NADPH = L-methionine enkephalin + NADP+ + H2O

-

-

3.4.11.6

L-Arg-(Met)enkephalin + H2O = L-Arg + (Met)enkephalin

-

-

3.4.11.6

L-Lys-(Met)enkephalin + H2O = L-Lys + (Met)enkephalin

-

-

3.4.11.6

Arg-Met-enkephalin + H2O = Arg + Met-enkephalin

-

-

3.4.11.6

[Arg0]-Met-enkephalin + H2O = Met-enkephalin + de-[Tyr]-Met-enkephalin

-

-

3.4.17.10

(Met)enkephalin-Arg + H2O = Tyr-Gly-Gly-Phe-Met + Arg

-

-

3.4.17.10

(Met)enkephalin-Lys + H2O = Tyr-Gly-Gly-Phe-Met + Lys

-

-

3.4.17.20

Arg6-Met5-enkephalin + H2O = Tyr-Gly-Gly-Phe-Met + Arg

-

-

3.4.17.20

Lys6-Met5-enkephalin + H2O = Tyr-Gly-Gly-Phe-Met + Lys

-

-

3.4.11.6

4 entries

3.4.17.10

2 entries

3.4.17.20

2 entries

3.4.22.15

BAM-22P + H2O = (Met)enkephalin + ?

-

-

3.4.22.16

Lys-Arg-(Met)enkephalin + H2O = Lys-Arg + (Met)enkephalin

-

-

3.4.22.16

Lys-Lys-(Met)enkephalin + H2O = Lys-Lys + (Met)enkephalin

-

-

3.4.22.16

2 entries

3.4.22.38

beta-endorphin + H2O = Met-enkephalin + ?

-

-

3.4.22.43

proenkephalin + H2O = (Met)enkephalin + ?

-

-

3.4.24.16

Tyr-Gly-Gly-Phe-Met-Arg-Arg-Val-(NH2) + H2O = Tyr-Gly-Gly-Phe-Met + Arg-Arg-Val-(NH2)

37061

-

Inhibitor in Enzyme-catalyzed Reactions (9 results)

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Show Inhibitors (9 entries)

EC NUMBER

COMMENTARY

LITERATURE

ENZYME 3D STRUCTURE

3.4.11.4

-

35923

-

3.4.11.7

-

665723

-

3.4.14.4

i.e. L-Tyr-Gly-Gly-L-Phe-L-Met, 61% inhibition at 0.5 mM, competitive inhibitor

699225

-

3.4.14.4

Met-enkephalin

650445

-

3.4.14.4

2 entries

3.4.17.10

-

81295, 81310

-

3.4.24.11

-

670479, 81646

-

3.4.24.11

hydrolysis of succinyl-Ala-Ala-Phe-4-methylcoumarin 7-amide

81646

-

3.4.24.11

2 entries

3.4.24.60

inhibitor of dactylysin towards substance P

668827

-

3.4.24.B14

-

690798

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (7 results)

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Show Turnover Number (7 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

3.4.11.6

0.47

-

pH 7.4, 37°C, wild-type

731349

3.4.11.6

0.48

-

pH 7.4, 37°C, mutant Q169N

731349

3.4.11.6

2 entries

3.4.15.1

58.3

-

-

81237

3.4.17.1

3.43

-

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

704669

3.4.24.11

7.8

-

-

81637

3.4.24.11

21.1

-

-

81639

3.4.24.11

2 entries

3.4.24.B14

9

-

37°C

690798

K_M Value (16 results)

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Show KM Value (16 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

3.4.11.14

0.00095

-

-

682118

3.4.11.2

0.045

-

from brain

35871

3.4.11.2

0.06

-

from kidney

35871

3.4.11.6

0.0251

-

pH 7.4, 37°C, wild-type

731349

3.4.11.6

0.36

-

pH 7.4, 37°C, mutant Q169N

731349

3.4.14.4

0.0419

-

-

668562

3.4.14.4

0.053

-

-

36179

3.4.15.1

0.3

-

-

81273

3.4.15.1

1

-

-

81237

3.4.11.2

2 entries

3.4.11.6

2 entries

3.4.14.4

2 entries

3.4.15.1

2 entries

3.4.17.1

0.55

-

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

704669

3.4.24.11

0.008

-

-

81639, 81644

3.4.24.11

0.022

-

-

81644

3.4.24.11

0.04

-

-

81644

3.4.24.11

0.062

-

-

81628, 81630, 81644

3.4.24.11

0.1

-

-

81637

3.4.24.11

5 entries

3.5.1.12

0.303

-

-

171928

K_i Value (5 results)

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Show KI Value (5 entries)

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

3.4.14.4

0.027

-

37°C, pH 7.4

650445

3.4.14.4

0.0343

-

37°C, pH 7.4

650445

3.4.14.4

0.13

-

in 50 mM Tris-HCl, pH 8.5, with 100 mM NaCl and 1 mM beta-mercaptoethanol, at 37°C

699225

3.4.14.4

3 entries

3.4.24.11

0.022

-

hydrolysis of Leu5-enkephalin

670479

3.4.24.B14

0.01

-

37°C

690798

References & Links

Literature References (40)

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Show Reference (40 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

35867

8963385

Purification and characterization of aminopeptidase M from muscle and mucosa of the pig intestine

1995

Terashima, H.; Bunnett, N.W.

J. Gastroenterol.

30

696-704

35871

2859885

Identification of aminopeptidase M as an enkephalin-inactivating enzyme in rat cerebral membranes

1985

Gros, C.; Giros, B.; Schwartz, J.C.

Biochemistry

24

2179-2185

35923

7126601

A highly specific aminotripeptidase of rat brain cytosol. Substrate specificity and effects of inhibitors

1982

Sachs, L.; Marks, N.

Biochim. Biophys. Acta

706

229-238

36118

3663681

The preparation and properties of immobilised dipeptidyl-aminopeptidase I (cathepsin C)

1987

Hutchinson, D.W.; Tunnicliffe, A.

Biochim. Biophys. Acta

916

1-4

36179

3297170

Purification and characterization of enkephalinase B from rat brain membrane

1987

Inaoka, Y.; Tamaoki, H.

Biochim. Biophys. Acta

925

27-35

36970

2949699

Biochemical characterization of hemorrhagic toxins with fibrinogenase activity isolated from Crotalus ruber ruber venom

1987

Mori, N.; Nikali, T.; Sugihara, H.; Tu, A.T.

Arch. Biochem. Biophys.

253

108-121

37061

9735321

Neuropeptide specificity and inhibition of recombinant isoforms of the endopeptidase 3.4.24.16 family: comparison with the related recombinant endopeptidase 3.4.24.15

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

5-11

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

81241

7674927

Peptidyl dipeptidase A: angiotensin I-converting enzyme

1995

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

Methods Enzymol.

248

283-305

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

81295

2887569

Product inhibition of carboxypeptidase H

1987

Hook, V.Y.H.; LaGamma, E.F.

J. Biol. Chem.

262

12583-12588

81310

2122147

Arginine and lysine product inhibition of bovine adrenomedullary carboxypeptidase H, a prohormone processing enzyme

1990

Hook, V.Y.H.

Life Sci.

47

1135-1139

81628

3894108

Endopeptidase-24.11: a cell-surface enzyme for metabolizing regulatory peptides

1985

Kenny, A.J.; Bowes, M.A.; Gee, N.S.; Matsas, R.

Biochem. Soc. Trans.

13

293-295

81630

3888721

Endopeptidase-24.11 and neuropeptide metabolism

1985

Turner, A.J.; Matsas, R.; Kenny, A.J.

Biochem. Soc. Trans.

13

39-42

81637

8806762

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

1996

Lian, W.; Wu, D.; Konings, W.N.; Mierau, I.; Hersh, L.B.

Arch. Biochem. Biophys.

333

121-126

81639

7049171

Properties of enkephalinase from rat kidney: comparison of dipeptidyl-carboxypeptidase and endopeptidase activities

1982

Malfroy, B.; Schwartz, J.C.

Biochem. Biophys. Res. Commun.

106

276-285

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.

Life Sci.

52

1461-1480

81646

2322317

Characterization of endopeptidase 3.4.24.11 ( enkephalinase ) activity in human plasma and cerebrospinal fluid

1990

Spillantini, M.G.; Sicuteri, F.; Salmon, S.; Malfroy, B.

Biochem. Pharmacol.

39

1353-1356

114159

-

Multiple molecular forms of acetylcholinesterase and their possible role in the degradation of neurohormones

1985

Brodbeck, U.

Colloq. Ges. Biol. Chem. Mosbach

36

22-32

171928

1679665

Enkephalin hydrolysis by human serum biotinidase

1991

Oizumi, J.; Hayakawa, K.

Biochim. Biophys. Acta

1074

433-438

171935

9211294

Biotinidase in serum and tissues

1997

Hymes, J.; Fleischhauer, K.; Wolf, B.

Methods Enzymol.

279

422-435

644032

6094523

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

1984

Hirao, T.; Takahashi, K.

J. Biochem.

96

775-784

647910

3688881

Rat brain cathepsin L: characterization and differentiation from cathepsin B utilizing opioid peptides

1987

Marks, N.; Berg, M.J.

Arch. Biochem. Biophys.

259

131-143

650445

11209758

Human and rat dipeptidyl peptidase III: biochemical and mass spectrometric arguments for similarities and differences

2000

Abramic, M.; Schleuder, D.; Dolovcak, L.; Schroder, W.; Strupat, K.; Sagi, D.; Peter-Katalini, J.; Vitale, L.

Biol. Chem.

381

1233-1243

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

665642

15932875

Staphylococcus aureus aminopeptidase S is a founding member of a new peptidase clan

2005

Odintsov, S.G.; Sabala, I.; Bourenkov, G.; Rybin, V.; Bochtler, M.

J. Biol. Chem.

280

27792-27799

665723

16790432

Enzymatic properties of aminopeptidase A: regulation of its enzymatic activity by calcium and angiotensin IV

2006

Goto, Y.; Hattori, A.; Ishii, Y.; Mizutani, S.; Tsujimoto, M.

J. Biol. Chem.

281

23503-23513

666240

16216010

Aminopeptidase-N/CD13 (EC 3.4.11.2) inhibitors: chemistry, biological evaluations, and therapeutic prospects

2006

Bauvois, B.; Dauzonne, D.

Med. Res. Rev.

26

88-130

667346

16521041

Extracellular metalloendopeptidase of Streptomyces rimosus

2006

Vitale, L.; Vukelic, B.; Krizaj, I.

Arch. Microbiol.

185

183-191

668562

16478478

Identification and characterization of two dipeptidyl-peptidase III isoforms in Drosophila melanogaster

2006

Mazzocco, C.; Gillibert-Duplantier, J.; Neaud, V.; Fukasawa, K.M.; Claverol, S.; Bonneu, M.; Puiroux, J.

FEBS J.

273

1056-1064

668570

16403023

Structural diversity of angiotensin-converting enzyme

2006

Bingham, R.J.; Dive, V.; Phillips, S.E.; Shirras, A.D.; Isaac, R.E.

FEBS J.

273

362-373

668827

-

Dactylysin

2004

Clamagirand, C.; Joudiou, C.; Cohen, P.

Handbook Of Proteolytic Enzymes(Barrett,A. J. ,Rawlings,N. D. ,Woessner,J. F. ,Eds. )Academic Press

1

1042-1044

668851

-

Ruberlysin

2004

Tu, A.T.

Handbook Of Proteolytic Enzymes(Barrett,A. J. ,Rawlings,N. D. ,Woessner,J. F. ,Eds. )Academic Press

1

682-683

670479

15134871

Angiotensin converting enzyme (ACE) and neprilysin hydrolyze neuropeptides: a brief history, the beginning and follow-ups to early studies

2004

Skidgel, R.A.; Erdoes, E.G.

Peptides

25

521-525

682118

17476590

Brain-specific aminopeptidase: from enkephalinase to protector against neurodegeneration

2007

Hui, K.S.

Neurochem. Res.

32

2062-2071

690798

11964170

Cell-specific activity of neprilysin 2 isoforms and enzymic specificity compared with neprilysin

2002

Rose, C.; Voisin, S.; Gros, C.; Schwartz, J.C.; Ouimet, T.

Biochem. J.

363

697-705

699225

18343901

Functional characterization and specific effects of various peptides on enzymatic activity of a DPP-III homologue from goat brain

2008

Dhanda, S.; Singh, H.; Singh, J.; Singh, T.P.

J. Enzyme Inhib. Med. Chem.

23

174-181

704669

20385563

Characterization of the substrate specificity of human carboxypeptidase A4 and implications for a role in extracellular peptide processing

2010

Tanco, S.; Zhang, X.; Morano, C.; Aviles, F.X.; Lorenzo, J.; Fricker, L.D.

J. Biol. Chem.

285

18385-18396

731349

24412328

Role of glutamine-169 in the substrate recognition of human aminopeptidase B

2014

Ogawa, Y.; Ohnishi, A.; Goto, Y.; Sakuma, Y.; Watanabe, J.; Hattori, A.; Tsujimoto, M.

Biochim. Biophys. Acta

1840

1872-1881

Links to other databases for MET-enkephalin

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