3.4.24.15: thimet oligopeptidase

This is an abbreviated version!
For detailed information about thimet oligopeptidase, go to the full flat file.

Reaction

Preferential cleavage of bonds with hydrophobic residues at P1, P2 and P3' and a small residue at P1' in substrates of 5-15 residues =

Synonyms

BIE, bradykinin-inactivating endopeptidase, EC 3.4.22.19, EC 3.4.99.31, endo-oligopeptidase A, endooligopeptidase A, endopeptidase 24-15, endopeptidase 24.15, endopeptidase EC 3.4.24.15, EOPA, EP 24.15, EP24.15, MdpA, metallo-dipeptidase aeruginosa, metalloendopeptidase 24.15, metalloendopeptidase EC 3.4.24.15, metallopeptidase, More, MP78, neutral endopeptidase 24.15, PA4498, peptidase, thimet oligo-, Pz peptidase A, Pz peptidase B, Pz-peptidase, Pz-peptidase A, soluble metallo-endopeptidase, soluble metallopeptidase, thimet oligopeptidase, thimet peptidase, thimet-oligopeptidase, thiol-dependent metalloendopeptidase, THOP1, TOP, Top1, Top2

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.24 Metalloendopeptidases

                3.4.24.15 thimet oligopeptidase

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Results	in table
16	Activating Compound
165	AA Sequence
1	Application
1	CAS Registry Number
26	Cloned(Commentary)
6	Crystallization (Commentary)
948	Disease/ Diagnostics
6	Expression
46	General Information
2	General Stability
20	IC50 Value
171	Inhibitors
20	kcat/KM [mM/s]
31	Ki Value [mM]
242	KM Value [mM]
60	Localization
39	Metals/Ions
17	Molecular Weight [Da]
66	Natural Substrates/ Products (Substrates)
296	Organism
2	Oxidation Stability
2	PDB ID
15	pH Optimum
5	pH Range
2	pH Stability
5	Posttranslational Modification
30	Protein Variants
20	Purification (Commentary)
1	Reaction
2	Reaction Type
89	Reference
1	Renatured (Commentary)
119	Source Tissue
12	Specific Activity [micromol/min/mg]
1	Storage Stability
417	Substrates and Products (Substrate)
21	Subunits
91	Synonyms
9	Temperature Optimum [°C]
1	Temperature Range [°C]
2	Temperature Stability [°C]
252	Turnover Number [1/s]

IC50 Value

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IC50 Value on EC 3.4.24.15 - thimet oligopeptidase

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IC50 VALUE [mM]

INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.007

Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg

Rattus norvegicus

-

IC50: 0.007 mM, degradation by EC 3.4.24.15

651221

0.0063

N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-((3S)-pyrrolidine-3-carboxyl)-Phe-(3-aminopropanoic acid)

Rattus norvegicus

-

IC50: 0.0063 mM, no cleavage by nephrilysin

650099

0.0069

N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-((3S)-pyrrolidine-3-carboxyl)-Tyr-(3-aminopropanoic acid)

Rattus norvegicus

-

IC50: 0.0069 mM, no cleavage by nephrilysin

650099

0.0794

N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-(3-amino-2-methylpropanoyl)-((3R)-3-amino-4-phenylbutanoyl)-(3-aminopropanoic acid)

Rattus norvegicus

-

IC50: 0.0794 mM, no cleavage by nephrilysin

650099

0.0631

N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-(3-amino-2-methylpropanoyl)-((3S)-3-amino-4-phenylbutanoyl)-(3-aminopropanoic acid)

Rattus norvegicus

-

IC50: 0.0631 mM, no cleavage by nephrilysin

650099

0.158

N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-(3-amino-2-methylpropanoyl)-(2-aminomethyl-3-phenylpropionyl)-(3-aminopropanoic acid)

Rattus norvegicus

-

IC50: 0.158 mM, no cleavage by nephrilysin

650099

0.0028

N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-(3-amino-2-methylpropanoyl)-Phe-(3-aminopropanoic acid)

Rattus norvegicus

-

IC50: 0.0028 mM, no cleavage by nephrilysin

650099

0.0063

N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-(3-amino-2-methylpropanoyl)-Tyr-3-aminopropanoic acid

Rattus norvegicus

-

IC50: 0.0063 mM, no cleavage by nephrilysin

650099

0.0056

N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-(3-aminopropanoyl)-Tyr-(3-aminopropanoic acid)

Rattus norvegicus

-

IC50: 0.0056 mM, no cleavage by nephrilysin

650099

0.01

N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-(piperidine-3-carboxyl)-Phe-(3-aminopropanoic acid)

Rattus norvegicus

-

IC50: 0.01 mM, no cleavage by nephrilysin

650099

0.0056

N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-(piperidine-3-carboxyl)-Tyr-(3-aminopropanoic acid)

Rattus norvegicus

-

IC50: 0.0056 mM, no cleavage by nephrilysin

650099

0.0251

N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-Ala-((3S)-3-amino-4-(4-hydroxyphenyl)butanoyl)-(3-aminopropanoic acid)

Rattus norvegicus

-

IC50: 0.0251 mM, no cleavage by nephrilysin

650099

0.04

N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-Ala-beta-2-Phe-(3-aminopropanoylic acid)

Rattus norvegicus

-

IC50: 0.04 mM, no cleavage by nephrilysin

650099

0.0036

N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-Ala-Phe-(3-aminopropanoic acid)

Rattus norvegicus

-

IC50: 0.0036 mM, no cleavage by nephrilysin

650099

0.00012

N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-Ala-Tyr-(3-aminopropanoic acid)

Rattus norvegicus

-

IC50: 0.00012 mM, complete degradation by nephrilysin

650099

0.00006

N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-Ala-Tyr-p-aminobenzoate

Rattus norvegicus

-

IC50: 0.00006 mM, potent and specific inhibitor, unstable in vivo due to cleavage between the alanine and tyrosine residues by the enzyme nephrilysin. This cleavage generates a potent inhibitor of angiotensin converting enzyme, thereby limiting the use of

650099

0.00079

N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-Pro-Phe-(3-aminopropanoic acid)

Rattus norvegicus

-

IC50: 0.00079 mM, no cleavage by nephrilysin

650099

0.00066

N-[1-(R,S)-carboxy-3-phenylpropyl]-Ala-Pro-Tyr-(3-aminopropanoic acid)

Rattus norvegicus

-

IC50: 0.00066 mM, no cleavage by nephrilysin

650099

0.012

RPPG-((3R)-3-amino-4-phenylbutanoic acid)-SPFR

Rattus norvegicus

-

IC50: 0.012 mM

651221

0.02

RPPG-((3S)-3-amino-4-phenylbutanoic acid)-SPFR

Rattus norvegicus

-

IC50: 0.02 mM

651221