3.4.24.16: neurolysin

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

Reaction

Preferential cleavage in neurotensin: Pro10-/-Tyr =

Synonyms

endopeptidase 24.16, endopeptidase 24.16B, endopeptidase 3.4.24.16, EP 24.16, ep24.16, EP24.16c, EP24.16m, MEP, Microsomal endopeptidase, mitochondrial peptidase, MOP, More, NEL, neurolisin, neurolysin, neurotensin endopeptidase, neurotensin-cleaving enzyme, Nln, oligopeptidase M, peptidase, neurotensin endo, peptidase, neurotensin endo-, SABP, soluble angiotensin II-binding protein, Soluble angiotensin-binding protein, thimet oligopeptidase II, thimet peptidase II

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.24 Metalloendopeptidases

                3.4.24.16 neurolysin

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Results	in table
3	Activating Compound
26	AA Sequence
5	Application
2	CAS Registry Number
21	Cloned(Commentary)
6	Crystallization (Commentary)
77	Disease/ Diagnostics
4	Expression
17	General Information
3	General Stability
2	IC50 Value
196	Inhibitors
11	Ki Value [mM]
167	KM Value [mM]
46	Localization
24	Metals/Ions
12	Molecular Weight [Da]
60	Natural Substrates/ Products (Substrates)
202	Organism
8	PDB ID
8	pH Optimum
1	pH Range
3	Posttranslational Modification
17	Protein Variants
15	Purification (Commentary)
1	Reaction
2	Reaction Type
63	Reference
130	Source Tissue
13	Specific Activity [micromol/min/mg]
1	Storage Stability
343	Substrates and Products (Substrate)
13	Subunits
56	Synonyms
7	Temperature Optimum [°C]
207	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.4.24.16 - neurolysin

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

purified recombinant enzyme mutant NLNE475Q in complex with the products of neurotensin cleavage, X-ray diffraction structure determination and analysis at 2.7 A resolution

Homo sapiens

Q9BYT8

754429

-

Rattus norvegicus

-

668828

crystal structure analysis and comparisons, overview

Rattus norvegicus

-

707285

purified enzyme with bound inhibitor R2, hanging drop vapor diffusion, mixing 2 ml of 48 mM protein in the presence of 5fold stoichiometric excess of inhibitor R2 with 1 ml of well solution containing 0.1 M HEPES, pH 7.0, 0.1 M LiSO4,2 mM 2-mercaptoethanol, and 12-15% PEG 4000, 4°C, X-ray diffraction structure determination and analysis at 2.8 A resolution

Rattus norvegicus

P42676

734291

purified recombinant mutant R470E/T499R, hanging drop vapour diffusion method, 4°C, 0.001 ml of 10 mg/ml protein is mixed with 0.001 ml of well solution containing 100 mM sodium cacodylate, pH 6.5, 100 mM magnesium acetate, 2 mM 2-mercaptoethanol, and 12-14% w/v polyethylene glycol 6000, cryoprotection by 25% glycerol, X-ray diffraction structure determination and analysis at 2.2 A resolution

Rattus norvegicus

-

683672

recombinant enzyme from Escherichia coli, hanging-drop vapor-diffusion method

Rattus norvegicus

-

649118