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Basic Ligand Information
Roles as Enzyme Ligand
Enzyme Kinetic Parameters
References & Links
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Ligand Met-4-methylcoumaryl-7-amide

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Basic Ligand Information

Molecular Structure

Picture of Met-4-methylcoumaryl-7-amide (click for magnification)

Molecular Formula

BRENDA Name

InChIKey

C₁₅H₁₈N₂O₃S

Met-4-methylcoumaryl-7-amide

FHLNBHBQGFIHKH-LBPRGKRZSA-N

Synonyms:

L-Met 7-amido-4-methylcoumarin, L-methionine-4-methyl-coumaryl-7-amide, L-methionine-4-methylcoumarin-7-amide, L-methionine-4-methylcoumaryl-7-amide, L-methionine-7-amido-4-methylcoumarin, L-methionine 4-methylcoumaryl-7-amide, L-methionyl-4-methylcoumarin-7-amide, L-methionyl-7-amido-4-methylcoumarin, L-methionyl 4-methylcoumarin-7-amide

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Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (15 results)

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EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

3.3.2.6

L-methionine-7-amido-4-methylcoumarin + H2O = L-methionine + 7-amino-4-methylcoumarin

731116

3.4.11.1

L-Met 7-amido-4-methylcoumarin + H2O = L-Met + 7-amino-4-methylcoumarin

754671

3.4.11.1

L-methionine-4-methylcoumaryl-7-amide + H2O = L-methionine + 7-amino-4-methylcoumarin

680250, 718187

3.4.11.1

L-methionyl-7-amido-4-methylcoumarin + H2O = L-methionine + 7-amino-4-methylcoumarin

755091

3.4.11.1

Met-4-methylcoumaryl-7-amide + H2O = Met + 7-amino-4-methyl-coumarin

L-methionine-4-methylcoumaryl-7-amide + H2O = L-methionine + 7-amino-4-methylcoumarin

717515

3.4.11.18

L-methionine 4-methylcoumaryl-7-amide + H2O = L-methionine + 7-amino-4-methylcoumarin

732863, 755640, 755484

3.4.11.18

L-methionine-4-methylcoumarin-7-amide + H2O = L-methionine + 7-amino-4-methylcoumarin

753843, 707703

3.4.11.18

L-methionine-7-amido-4-methylcoumarin + H2O = L-methionine + 7-amino-4-methylcoumarin

717497, 681310, 681317

3.4.11.18

L-methionyl 4-methylcoumarin-7-amide + H2O = L-methionine + 7-amino-4-methylcoumarin

707698, 709466

3.4.11.18

L-methionyl-7-amido-4-methylcoumarin + H2O = L-methionine + 7-amino-4-methylcoumarin

717497

3.4.11.18

Met-4-methylcoumaryl-7-amide + H2O = Met + 7-amino-4-methylcoumarin

L-methionine 4-methylcoumaryl-7-amide + H2O = L-methionine + 7-amino-4-methylcoumarin

752601

3.4.11.20

L-methionyl-7-amido-4-methylcoumarin + H2O = L-methionine + 7-amino-4-methylcoumarin

731736

3.4.11.3

Met-4-methylcoumaryl-7-amide + H2O = Met + 7-amino-4-methylcoumarin

651074

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (16 results)

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EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

3.4.11.1

0.085

pH 8.5, 37Â°C

718187

3.4.11.1

0.33

pH 8.0, 37Â°C, recombinant enzyme

25.6

pH 7.0, 37Â°C

717515

3.4.11.18

0.0000508

after removal of divalent metal ions activated with 0.020 mM Mn2+, pH not specified in the publication, temperature not specified in the publication

717345

3.4.11.18

0.000055

after removal of divalent metal ions activated with 0.020 mM Mn2+, pH not specified in the publication, temperature not specified in the publication

717345

3.4.11.18

0.000137

after removal of divalent metal ions activated with 0.020 mM Co2+, pH not specified in the publication, temperature not specified in the publication

717345

3.4.11.18

0.000159

after removal of divalent metal ions activated with 0.020 mM Co2+, pH not specified in the publication, temperature not specified in the publication

717345

3.4.11.18

0.000263

after removal of divalent metal ions activated with 0.0025 mM Fe2+, pH not specified in the publication, temperature not specified in the publication

717345

3.4.11.18

0.000305

after removal of divalent metal ions activated with 0.005 mM Ni2+, pH not specified in the publication, temperature not specified in the publication

717345

3.4.11.18

0.000312

after removal of divalent metal ions activated with 0.020 mM Ni2+, pH not specified in the publication, temperature not specified in the publication

717345

3.4.11.18

0.000449

after removal of divalent metal ions activated with 0.0025 mM Fe2+, pH not specified in the publication, temperature not specified in the publication

717345

3.4.11.18

0.014

recombinant isozyme MetAP1a in presence of Fe2+

707703

3.4.11.18

0.045

recombinant isozyme MetAP1a in presence of Ni2+

707703

3.4.11.18

0.07

recombinant isozyme MetAP1a in presence of Mn2+

707703

3.4.11.18

0.36

recombinant isozyme MetAP1a in presence of Co2+

0.704

pH 7.4, 37Â°C

731736

K_M Value (18 results)

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EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

3.4.11.1

0.0038

pH 8.0, 37Â°C, recombinant enzyme

755091

3.4.11.1

0.1092

pH 8.5, 37Â°C

0.12

0.01

pH 7.0, 37Â°C

717515

3.4.11.18

0.011

recombinant isozyme MetAP1a in presence of Ni2+

707703

3.4.11.18

0.0143

pH 7.5, temperature not specified in the publication

755640

3.4.11.18

0.082

recombinant isozyme MetAP1a in presence of Co2+

707703

3.4.11.18

0.111

after removal of divalent metal ions activated with 0.005 mM Ni2+, pH not specified in the publication, temperature not specified in the publication

717345

3.4.11.18

0.115

after removal of divalent metal ions activated with 0.020 mM Mn2+, pH not specified in the publication, temperature not specified in the publication

717345

3.4.11.18

0.13

after removal of divalent metal ions activated with 0.020 mM Co2+, pH not specified in the publication, temperature not specified in the publication

717345

3.4.11.18

0.144

after removal of divalent metal ions activated with 0.020 mM Ni2+, pH not specified in the publication, temperature not specified in the publication

717345

3.4.11.18

0.154

after removal of divalent metal ions activated with 0.020 mM Mn2+, pH not specified in the publication, temperature not specified in the publication

717345

3.4.11.18

0.155

after removal of divalent metal ions activated with 0.0025 mM Fe2+, pH not specified in the publication, temperature not specified in the publication

717345

3.4.11.18

0.161

recombinant isozyme MetAP1a in presence of Fe2+

707703

3.4.11.18

0.161

after removal of divalent metal ions activated with 0.0025 mM Fe2+, pH not specified in the publication, temperature not specified in the publication

717345

3.4.11.18

0.168

after removal of divalent metal ions activated with 0.020 mM Co2+, pH not specified in the publication, temperature not specified in the publication

717345

3.4.11.18

0.17

recombinant isozyme MetAP1a in presence of Mn2+

0.0314

pH 7.4, 37Â°C

731736

References & Links

Literature References (21)

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BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

651074

10601849

Characterization of a recombinant soluble form of human placental leucine aminopeptidase/oxytocinase expressed in Chinese hamster ovary cells

2000

Matsumoto, H.; Rogi, T.; Yamashiro, K.; Kodama, S.; Tsuruoka, N.; Hattori, A.; Takio, K.; Mizutani, S.; Tsujimoto, M.

Eur. J. Biochem.

267

46-52

680250

16814790

Identification and characterisation of a leucine aminopeptidase from the hard tick Haemaphysalis longicornis

2006

Hatta, T.; Kazama, K.; Miyoshi, T.; Umemiya, R.; Liao, M.; Inoue, N.; Xuan, X.; Tsuji, N.; Fujisaki, K.

Int. J. Parasitol.

1123-1132

681310

17636946

Highly potent inhibitors of methionine aminopeptidase-2 based on a 1,2,4-triazole pharmacophore

2007

Marino, J.P.; Fisher, P.W.; Hofmann, G.A.; Kirkpatrick, R.B.; Janson, C.A.; Johnson, R.K.; Ma, C.; Mattern, M.; Meek, T.D.; Ryan, M.D.; Schulz, C.; Smith, W.W.; Tew, D.G.; Tomazek, T.A.; Veber, D.F.; Xiong, W.C.; Yamamoto, Y.; Yamashita, K.; Yang, G.; Thompson, S.K.

J. Med. Chem.

3777-3785

681317

17948983

Inhibition of monometalated methionine aminopeptidase: inhibitor discovery and crystallographic analysis

2007

Huang, M.; Xie, S.X.; Ma, Z.Q.; Huang, Q.Q.; Nan, F.J.; Ye, Q.Z.

J. Med. Chem.

5735-5742

707698

20207144

A cell-based assay that targets methionine aminopeptidase in a physiologically relevant environment

2010

Chai, S.C.; Ye, Q.Z.

Bioorg. Med. Chem. Lett.

2129-2132

707703

20363127

Expression and characterization of Mycobacterium tuberculosis methionine aminopeptidase type 1a

2010

Lu, J.P.; Ye, Q.Z.

Bioorg. Med. Chem. Lett.

2776-2779

709466

20038112

Catalysis and inhibition of Mycobacterium tuberculosis methionine aminopeptidase

2010

Lu, J.P.; Chai, S.C.; Ye, Q.Z.

J. Med. Chem.

1329-1337

717345

21524572

Two methionine aminopeptidases from Acinetobacter baumannii are functional enzymes

2011

Yuan, H.; Chai, S.C.; Lam, C.K.; Howard Xu, H.; Ye, Q.Z.

Bioorg. Med. Chem. Lett.

3395-3398

717497

21465667

Inhibition of Mycobacterium tuberculosis methionine aminopeptidases by bengamide derivatives

2011

Lu, J.P.; Yuan, X.H.; Yuan, H.; Wang, W.L.; Wan, B.; Franzblau, S.G.; Ye, Q.Z.

ChemMedChem

1041-1048

717515

21276865

Identification of a puromycin-sensitive aminopeptidase from zebrafish (Danio rerio)

2011

Chen, S.H.; Cao, M.J.; Huang, J.Z.; Wu, G.P.

Comp. Biochem. Physiol. B

159

10-17

718172

21569035

The Arabidopsis aminopeptidase LAP2 regulates plant growth, leaf longevity and stress response

2011

Waditee-Sirisattha, R.; Shibato, J.; Rakwal, R.; Sirisattha, S.; Hattori, A.; Nakano, T.; Takabe, T.; Tsujimoto, M.

New Phytol.

191

958-969

718187

21414242

Molecular cloning and characterization of a M17 leucine aminopeptidase of Cryptosporidium parvum

2011

Kang, J.; Ju, H.; Sohn, W.; Na, B.

Parasitology

138

682-690

731116

24573245

A remarkable activity of human leukotriene A4 hydrolase (LTA4H) toward unnatural amino acids

2014

Byzia, A.; Haeggstroem, J.Z.; Salvesen, G.S.; Drag, M.

Amino Acids

1313-1320

731736

24839124

Aminopeptidase N1 (EtAPN1), an M1 metalloprotease of the apicomplexan parasite Eimeria tenella, participates in parasite development

2014

Gras, S.; Byzia, A.; Gilbert, F.B.; McGowan, S.; Drag, M.; Silvestre, A.; Niepceron, A.; Lecaille, F.; Lalmanach, G.; Brossier, F.

Eukaryot. Cell

884-895

732863

25595410

Expression and biochemical characterization of a type I methionine aminopeptidase of Plasmodium vivax

2015

Kang, J.; Ju, J.; Kim, J.; Ju, H.; Lee, J.; Lee, K.; Lee, W.; Sohn, W.; Kim, T.; Na, B.

Protein Expr. Purif.

108

48-53

752601

A specific tripeptidyl substrate for tripeptidyl peptidase activity is effectively hydrolyzed by alanyl aminopeptidase/aminopeptidase N/CD13 in the rat kidney

2016

Shibata, M.; Koike, M.; Kusumi, S.; Sato, N.; Uchiyama, Y.

Arch. Histol. Cytol.

1-8

753843

29680505

Structural and functional highlights of methionine aminopeptidase 2 from Leishmania donovani

2018

Bhat, S.Y.; Dey, A.; Qureshi, I.A.

Int. J. Biol. Macromol.

115

940-954