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Literature summary extracted from

  • Li, X.; Lou, Z.; Li, X.; Zhou, W.; Ma, M.; Cao, Y.; Geng, Y.; Bartlam, M.; Zhang, X.C.; Rao, Z.
    Structure of human cytosolic X-prolyl aminopeptidase: a double Mn(II)-dependent dimeric enzyme with a novel three-domain subunit (2008), J. Biol. Chem., 283, 22858-22866.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.11.9 expressed in Escherichia coli BL21(DE3) cells Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.11.9 hanging drop vapour diffusion method, using 20% (v/v) polyethylene glycol 400, 0.15 M CaCl2, and 100 mM HEPES (pH 7.5) Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.4.11.9 E41A the mutant maintains 91% of the wild type activity and demonstrates that the acidic residue, which is considered as a stabilizing factor in the protonation of catalytic residue His498, plays only a marginal role in catalysis Homo sapiens
3.4.11.9 W477E the mutant, designed to block dimer formation, shows only 6% of the wild type activity Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.11.9 EDTA the activity of the enzyme drops to 10% after treatment with 50 mM EDTA Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.11.9 0.078
-
 bradykinin wild type enzyme in 100 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 37°C Homo sapiens
3.4.11.9 0.308
-
 L-Arg-L-Pro-L-Pro wild type enzyme in 100 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 37°C Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.11.9 cytosol
-
 Homo sapiens 5829
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.11.9 Mn2+ the enzyme is double Mn2+-dependent for its activity Homo sapiens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.11.9 70000
-
 2 * 70000, X-ray crystallography Homo sapiens
3.4.11.9 140000
-
 X-ray crystallography Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
3.4.11.9 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.11.9 Ni-NTA resin column chromatography and Hitrap Q HP affinity column chromatography Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.11.9 bradykinin + H2O
-
 Homo sapiens L-Arg + des-Arg-bradykinin
-
 ?
3.4.11.9 L-Arg-L-Pro-L-Pro + H2O
-
 Homo sapiens L-Arg + L-Pro-L-Pro
-
 ?
3.4.11.9 L-prolyl-peptide + H2O X-prolyl aminopeptidase catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides Homo sapiens L-proline + peptide
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.11.9 homodimer 2 * 70000, X-ray crystallography Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
3.4.11.9 aminopeptidase P
-
 Homo sapiens
3.4.11.9 AP-P
-
 Homo sapiens
3.4.11.9 X-prolyl aminopeptidase
-
 Homo sapiens
3.4.11.9 XPNPEP1
-
 Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.11.9 3.8
-
 bradykinin wild type enzyme in 100 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 37°C Homo sapiens
3.4.11.9 7.7
-
 L-Arg-L-Pro-L-Pro wild type enzyme in 100 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 37°C Homo sapiens