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Literature summary extracted from

  • Chesneau, V.; Pierotti, A.R.; Barre, N.; Creminon, C.; Tougard, C.; Cohen, P.
    Isolation and characterization of a dibasic selective metalloendopeptidase from rat testes that cleaves at the amino terminus of arginine residues (1994), J. Biol. Chem., 269, 2056-2061.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.61 1,10-phenanthroline dynorphin A or [Ala17,Tyr20]-somatostatin-28-(10-20)-NH2 as substrate Rattus norvegicus
3.4.24.61 amastatin 0.02 mM; dynorphin A or [Ala17,Tyr20]-somatostatin-28-NH2 as substrate; strong Rattus norvegicus
3.4.24.61 bestatin dynorphin A or [Ala17,Tyr20]-somatostatin-28-NH2 as substrate; less efficient than amastatin Rattus norvegicus
3.4.24.61 Ca2+ not Rattus norvegicus
3.4.24.61 Co2+ 0.1 mM Rattus norvegicus
3.4.24.61 Cu2+
-
 Rattus norvegicus
3.4.24.61 DTT dynorphin A or [Ala17,Tyr20]-somatostatin-28-NH2 as substrate; weak Rattus norvegicus
3.4.24.61 EDTA dynorphin A or [Ala17,Tyr20]-somatostatin-28-(10-20)-NH2 as substrate; reversible by low concentrations of Zn2+ or Mn2+; to a lesser extent by Co2+, Ca2+; to a lesser extent by Mg2+ (not) Rattus norvegicus
3.4.24.61 EGTA dynorphin A or [Ala17,Tyr20]-somatostatin-28-(10-20)-NH2 as substrate Rattus norvegicus
3.4.24.61 Mn2+
-
 Rattus norvegicus
3.4.24.61 additional information no inhibition by IAA, phosphoramidon, captopril, phenylmethylsulfonyl fluoride, leupeptin, guanidylethylmercaptosuccinic acid (i.e. GEMSA) Rattus norvegicus
3.4.24.61 N-ethylmaleimide strong, dynorphin A or [Ala17,Tyr20]-somatostatin-28-NH2 as substrate Rattus norvegicus
3.4.24.61 N-tosyl-L-Phe chloromethyl ketone i.e. TPCK, 0.25 mM Rattus norvegicus
3.4.24.61 Zn2+ strong Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.24.61 0.00625
-
 ANF-(1-28)
-
 Rattus norvegicus
3.4.24.61 0.00645
-
 dynorphin A
-
 Rattus norvegicus
3.4.24.61 0.0173
-
 Preproneurotensin-(154-170)
-
 Rattus norvegicus
3.4.24.61 0.024
-
 dynorphin A-(1-13)
-
 Rattus norvegicus
3.4.24.61 0.043
-
 Somatostatin-28
-
 Rattus norvegicus
3.4.24.61 0.103
-
 Bovine adrenal medulla dodecapeptide
-
 Rattus norvegicus
3.4.24.61 0.127
-
 dynorphin A-(1-10)
-
 Rattus norvegicus
3.4.24.61 0.162
-
 dynorphin A-(1-9)
-
 Rattus norvegicus
3.4.24.61 0.209
-
 dynorphin B
-
 Rattus norvegicus
3.4.24.61 0.227
-
 [Arg0,Ala17]-somatostatin-28-(1-19)-NH2
-
 Rattus norvegicus
3.4.24.61 0.428
-
 [Ala17,Tyr20]-Somatostatin-28-(10-20)-NH2
-
 Rattus norvegicus
3.4.24.61 0.974
-
 alpha-neoendorphin
-
 Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.24.61 cytoplasm testis Rattus norvegicus 5737
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.24.61 additional information metalloendopeptidase Rattus norvegicus
3.4.24.61 additional information cation-dependent enzyme, structural rather than catalytical role of metal ions cannot be excluded Rattus norvegicus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.24.61 110000
-
 PAGE, 2 catalytically active forms: MW 110000 and MW 140000 Rattus norvegicus
3.4.24.61 140000
-
 PAGE, 2 catalytically active forms: MW 110000 and MW 140000 Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.61 Rattus norvegicus
-
 male Wistar
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.24.61 2 catalytically active forms Rattus norvegicus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.24.61 adrenal gland
-
 Rattus norvegicus
-
3.4.24.61 brain cerebral cortex, enzyme is catalytically and immunologically related to testis enzyme Rattus norvegicus
-
3.4.24.61 heart
-
 Rattus norvegicus
-
3.4.24.61 additional information tissue distribution Rattus norvegicus
-
3.4.24.61 additional information not in intestinal muscle Rattus norvegicus
-
3.4.24.61 testis immature and mature spermatids Rattus norvegicus
-
3.4.24.61 testis enzyme is catalytically and immunologically related to brain enzyme Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.61 alpha-Neoendorphin + H2O i.e. Tyr-Gly-Gly-Phe-Leu-Arg-Lys-Tyr-Pro-Leu, cleavage at Arg-Lys processing site Rattus norvegicus Tyr-Gly-Gly-Phe-Leu-Arg + Lys-Tyr-Pro-Leu
-
 ?
3.4.24.61 ANF-(1-28) + H2O i.e. atrial natriuretic factor, cleavage site: Arg+Arg Rattus norvegicus ?
-
 ?
3.4.24.61 Bovine adrenal medulla dodecapeptide + H2O
-
 Rattus norvegicus Tyr-Gly-Gly-Phe-Met-Arg + Arg-Val-Gly-Arg-Pro-Glu
-
 ?
3.4.24.61 dynorphin A + H2O i.e. Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-Trp-Asp-Asn-Gln-NH2 Rattus norvegicus Tyr-Gly-Gly-Phe-Leu-Arg + Arg-Ile-Arg-Pro-Lys-Leu-Lys-Trp-Asp-Asn-Gln-NH2
-
 ?
3.4.24.61 dynorphin A-(1-10) + H2O i.e. Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro, cleavage site: Arg-Arg Rattus norvegicus Tyr-Gly-Gly-Phe-Leu-Arg + Arg-Ile-Arg-Pro
-
 ?
3.4.24.61 dynorphin A-(1-13) + H2O i.e. Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys, cleavage site: Arg-Arg Rattus norvegicus Tyr-Gly-Gly-Phe-Leu-Arg + Arg-Ile-Arg-Pro-Lys-Leu-Lys
-
 ?
3.4.24.61 dynorphin A-(1-9) + H2O i.e. Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg, cleavage site: Arg-Arg Rattus norvegicus Tyr-Gly-Gly-Phe-Leu-Arg + Arg-Ile-Arg
-
 ?
3.4.24.61 dynorphin B + H2O i.e. Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Gln-Phe-Lys-Val-Val-Thr Rattus norvegicus Tyr-Gly-Gly-Phe-Leu-Arg + Arg-Gln-Phe-Lys-Val-Val-Thr
-
 ?
3.4.24.61 additional information [Tyr20]-somatostatin-28-(13-20)-NH2, dynorphin A-(1-7), [Ala17]-somatostatin-(6-19)-NH2, prosomatostatin-(56-68)-NH2, the Lys-Arg-doublet in preproenkephalin-(128-140) or pro-oxytocin/neurophysin-(1-20) Rattus norvegicus ?
-
 ?
3.4.24.61 additional information cleavage occurs selectively at amino-terminal side of an Arg-residue in dibasic stretches Rattus norvegicus ?
-
 ?
3.4.24.61 additional information no aminopeptidase or carboxypeptidase activity Rattus norvegicus ?
-
 ?
3.4.24.61 additional information cleavage efficiency is higher for the larger substrates Rattus norvegicus ?
-
 ?
3.4.24.61 additional information independent of the nature of the basic doublet of the peptide Rattus norvegicus ?
-
 ?
3.4.24.61 additional information no cleavage of single Arg-Xaa site Rattus norvegicus ?
-
 ?
3.4.24.61 Preproneurotensin-(154-170) + H2O cleavage site: prohormonal maturation site, Lys-Arg Rattus norvegicus ?
-
 ?
3.4.24.61 Preproneurotensin-(154-170) + H2O not monobasic site Rattus norvegicus ?
-
 ?
3.4.24.61 Somatostatin-28 + H2O cleavage site: Xaa-+-Arg-Lys, the term -+- depicts the point of cleavage Rattus norvegicus Somatostatin-28-(13-28) + somatostatin-28-(1-12)
-
 ?
3.4.24.61 [Ala17,Tyr20]-Somatostatin-28-(10-20)-NH2 + H2O derived from somatostatin-28, mimicking the peptide sequence around the dibasic (i.e. maturation) site Rattus norvegicus Pro-Arg-Glu + Arg-Lys-Ala-Gly-Ala-Lys-Asn-Tyr-NH2
-
 ?
3.4.24.61 [Ala17,Tyr20]-Somatostatin-28-(10-20)-NH2 + H2O i.e. Pro-Arg-Glu-Arg-Lys-Ala-Gly-Ala-Lys-Asn-Tyr-NH2 Rattus norvegicus Pro-Arg-Glu + Arg-Lys-Ala-Gly-Ala-Lys-Asn-Tyr-NH2
-
 ?
3.4.24.61 [Arg0,Ala17]-somatostatin-28-(1-19)-NH2 + H2O
-
 Rattus norvegicus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.24.61 monomer 1 * 110000, testis, SDS-PAGE, 1 * 140000, brain, SDS-PAGE Rattus norvegicus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.24.61 37
-
 assay at Rattus norvegicus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.24.61 8.9
-
 [Ala17,Tyr20]-somatostatin-28-(10-20)-NH2 as substrate Rattus norvegicus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.4.24.61 8.2 9.3 [Ala17,Tyr20]-somatostatin-28-(10-20)-NH2 as substrate, about half-maximal activity at pH 8.2 and 9.3 Rattus norvegicus