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Literature summary for 3.4.24.16 extracted from

  • Lim, E.J.; Sampath, S.; Coll-Rodriguez, J.; Schmidt, J.; Ray, K.; Rodgers, D.W.
    Swapping the substrate specificities of the neuropeptidases neurolysin and thimet oligopeptidase (2007), J. Biol. Chem., 282, 9722-9732.
    View publication on PubMed
Search for more literature for 3.4.24.16

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Rattus norvegicus

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Protein Variants

Protein Variants Comment Organism
R470E/T499R site-directed mutagenesis of the substrate recognition residues leads to a swap of substrate specificity from thimet oligopeptidase to neurolysin, EC 3.4.24.16, the mutant cleaves neurolysin sites, overview Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.002
-
 neurotensin recombinant wild-type enzyme, pH 7.5, 37°C Rattus norvegicus
0.00295
-
 neurotensin recombinant mutant R470E/T499R, pH 7.5, 37°C Rattus norvegicus

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ a zinc-dependent metallopeptidase Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Rattus norvegicus the enzyme cleaves several bioactive peptides at sites similar or different from thimet oligopeptidase, EC 3.4.24.15 ?
-
 ?
neurotensin + H2O Rattus norvegicus
-
 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3) Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme cleaves several bioactive peptides at sites similar or different from thimet oligopeptidase, EC 3.4.24.15 Rattus norvegicus ?
-
 ?
additional information residues R470, R491, N496, and T499 determine the substrate specificity of thimet oligopeptidase different from closely related thimet oligopeptidase, EC 3.4.24.15 Rattus norvegicus ?
-
 ?
neurotensin + H2O
-
 Rattus norvegicus ?
-
 ?
neurotensin + H2O determination of specific cleavage sites, overview Rattus norvegicus ?
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Rattus norvegicus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.8
-
 neurotensin recombinant mutant R470E/T499R, pH 7.5, 37°C Rattus norvegicus
5
-
 neurotensin recombinant wild-type enzyme, pH 7.5, 37°C Rattus norvegicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Rattus norvegicus