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Ligand Leu-Met-NH2

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

Product in Enzyme-catalyzed Reactions (12 results)

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Show Product (12 entries)

EC NUMBER

LITERATURE

REACTION DIAGRAM

REACTION

ENZYME 3D STRUCTURE

3.4.15.1

, 81252

Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 + H2O = Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly + Leu-Met-NH2

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3.4.15.1

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His-Lys-Thr-Asp-Ser-Phe-Val-Gly-Leu-Met-NH2 + H2O = His-Lys-Thr-Asp-Ser-Phe-Val-Gly + Leu-Met-NH2

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3.4.15.1

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physalaemin + H2O = pGlu-Ala-Asp-Pro-Asn-Lys-Phe-Tyr-Gly + Leu-Met-NH2

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3.4.15.1

3 entries

3.4.24.11

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His-Lys-Thr-Asp-Ser-Phe-Val-Gly-Leu-Met-NH2 + H2O = His-Lys-Thr-Asp-Ser + Phe-Val-Gly + Leu-Met-NH2

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3.4.24.30

31192

Substance P + H2O = Arg-Pro-Lys-Pro-Gln-Gln + Phe + Phe-Gly + Leu-Met-NH2

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3.4.24.32

651751

KFIGLM-NH2 + H2O = KFIG + Leu-Met-NH2

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3.4.24.40

650288

substance P + H2O = RPKPQQFFG + LM-NH2 + RPKPQQFF + GLM-NH2 + RPKQQF + FGLM-NH2

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3.4.24.60

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neurokinin A + H2O = HKTDSFVG + Leu-Met-NH2

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3.4.24.60

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substance P + H2O = RPKQQF + Phe-Gly + Leu-Met-NH2

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3.4.24.B14

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Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 + H2O = Arg-Pro-Lys-Pro-Gln-Gln + Phe-Phe-Gly + Leu-Met-NH2

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3.4.24.B14

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Phe-Gly-Leu-Met-NH2 + H2O = Phe-Gly + Leu-Met-NH2

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3.4.24.B14

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Phe-Phe-Gly-Leu-Met-NH2 + H2O = Phe-Phe-Gly + Leu-Met-NH2

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3.4.24.60

2 entries

3.4.24.B14

3 entries

Inhibitor in Enzyme-catalyzed Reactions (2 results)

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Show Inhibitors (2 entries)

COMMENTARY

EC NUMBER

LITERATURE

ENZYME 3D STRUCTURE

-

3.4.24.B14

669280

-

-

7.4.2.1

700356

-

-

2 entries

Enzyme Kinetic Parameters

K_i Value (1 result)

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Show KI Value (1 entry)

COMMENTARY

EC NUMBER

KI VALUE [MM]

KI VALUE MAXIMUM [MM]

LITERATURE

37°C, pH 7.2, wild-type enzyme

3.4.24.B14

0.175

-

669280

References & Links

Literature References (6)

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Show Reference (6 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

31192

2536744

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

1989

Mäkinen, P.L.; Clewell, D.B.; An, F.; Mäkinen, K.K.

J. Biol. Chem.

264

3325-3334

81252

2991265

A rat brain isozyme of angiotensin-converting enzyme. Unique specificity for amidated peptide substrates

1985

Strittmatter, S.M.; Thiele, E.A.; Kapiloff, M.S.; Snyder, S.H.

J. Biol. Chem.

260

9825-9832

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

651751

9685723

Bacteriolytic activity and specificity of Achromobacter beta-lytic protease

1998

Li, S.; Norioka, S.; Sakiyama, F.

J. Biochem.

124

332-339

669280

15294904

A three-dimensional model of the neprilysin 2 active site based on the X-ray structure of neprilysin. Identification of residues involved in substrate hydrolysis and inhibitor binding of neprilysin 2

2004

Voisin, S.; Rognan, D.; Gros, C.; Ouimet, T.

J. Biol. Chem.

279

46172-46181

700356

19060912

Transport and signaling via the amino acid binding site of the yeast Gap1 amino acid transceptor

2009

Van Zeebroeck, G.; Bonini, B.M.; Versele, M.; Thevelein, J.M.

Nat. Chem. Biol.

5

45-52

Links to other databases for Leu-Met-NH2

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Show Links (1 entry)

ChEBI

PubChem

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